|
Name |
Accession |
Description |
Interval |
E-value |
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
36-1178 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 1943.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVDAV 115
Cdd:COG1038 2 KKIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGEGKGPVDAYLDIEEIIRVAKEKGVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFK 195
Cdd:COG1038 82 HPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 275
Cdd:COG1038 162 AAAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 355
Cdd:COG1038 242 VEIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 356 RSL--PDLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIA 432
Cdd:COG1038 322 YSLddPEIGIpSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGNAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 433 HGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG 512
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDETPELFDFPKRRDRATKLLTYLGDVTVNG 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 513 PTTPIPVNVSPSPVDPAVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIA 592
Cdd:COG1038 482 PPGVKGRPKPDFPKPKLPKVDLGAPPPKGTKQILDELGPEGFAKWLREQKKVLLTDTTFRDAHQSLLATRVRTRDMLKIA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 593 PYVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGM 672
Cdd:COG1038 562 PATARLLPQLFSLEMWGGATFDVAYRFLKEDPWERLAKLREAIPNILFQMLLRGSNAVGYTNYPDNVVRAFVKEAAEAGI 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 673 DVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAA 752
Cdd:COG1038 642 DVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPKRTKYTLDYYVDLAKELEKAGAHILAIKDMAGLLKPYA 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 753 CTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERV 832
Cdd:COG1038 722 AYKLVKALKEEV-DLPIHLHTHDTSGNQLATYLAAIEAGVDIVDVALASMSGLTSQPSLNSLVAALEGTERDTGLDLDAL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 833 FDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSS 912
Cdd:COG1038 801 QELSNYWEAVRKYYAPFE--SGLKAPTAEVYKHEMPGGQYSNLRQQARALGLGDRWEEVKEMYAAVNRLFGDIVKVTPSS 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 913 KIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELE 992
Cdd:COG1038 879 KVVGDMALFMVQNGLTPEDVYEKGKDLDFPDSVVSFFKGELGQPPGGFPEELQKKVLKGRKPITVRPGELLPPVDFDALR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 993 KDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRA 1072
Cdd:COG1038 959 AELEEKLGREPSDRDVLSYLLYPKVFEDYAKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEEGKTLIIKLLAIGEPDED 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1073 GQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTS 1152
Cdd:COG1038 1039 GMRTVFFELNGQPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMKMETTITA 1118
|
1130 1140
....*....|....*....|....*.
gi 251823980 1153 PMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:COG1038 1119 PRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
34-1179 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 1835.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 34 EYKPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENGVD 113
Cdd:PRK12999 1 EMKKIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGEGKHPVRAYLDIDEIIRVAKQAGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 114 AVHPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPII 193
Cdd:PRK12999 81 AIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 194 FKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQ 273
Cdd:PRK12999 161 LKASAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 274 KVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 353
Cdd:PRK12999 241 KVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 354 EGRSLPDLG---LRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKV 430
Cdd:PRK12999 321 EGATLHDLEigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGGNAFAGAEITPYYDSLLVKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 431 IAHGKDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMV 510
Cdd:PRK12999 401 TAWGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDETPELFDFPKRRDRGTKLLTYIADVTV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 511 NGPtTPIPVNVSPSPVDPAVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKK 590
Cdd:PRK12999 481 NGF-PGVKKKPPVFPDPRLPKVDLSAPPPAGTKQILDELGPEGFADWLRDQKRVLLTDTTFRDAHQSLLATRVRTKDLLR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 591 IAPYVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKEN 670
Cdd:PRK12999 560 IAPATARLLPNLFSLEMWGGATFDVAYRFLKEDPWERLAELREAAPNVLFQMLLRGSNAVGYTNYPDNVVRAFVREAAAA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 671 GMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKP 750
Cdd:PRK12999 640 GIDVFRIFDSLNWVENMRVAIDAVRETGKIAEAAICYTGDILDPARAKYDLDYYVDLAKELEKAGAHILAIKDMAGLLKP 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 751 AACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLE 830
Cdd:PRK12999 720 AAAYELVSALKEEV-DLPIHLHTHDTSGNGLATYLAAAEAGVDIVDVAVASMSGLTSQPSLNSIVAALEGTERDTGLDLD 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 831 RVFDYSEYWEGARGLYAAFdcTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTP 910
Cdd:PRK12999 799 AIRKLSPYWEAVRPYYAPF--ESGLKSPTTEVYLHEMPGGQYSNLKQQARALGLGDRFEEVKEMYAAVNRMFGDIVKVTP 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 911 SSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKE 990
Cdd:PRK12999 877 SSKVVGDMALFMVQNGLTPEDVYEPGEDLDFPDSVVSFLKGELGQPPGGFPEPLQKKVLKGEEPITVRPGELLEPVDFEA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 991 LEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLN 1070
Cdd:PRK12999 957 ERAELEEKLGREVTDRDVLSYLLYPKVFEDYIKHREEYGDVSVLPTPTFFYGLRPGEEIEVEIEPGKTLIIKLEAIGEPD 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1071 RAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVV 1150
Cdd:PRK12999 1037 EDGMRTVYFELNGQPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMETTI 1116
|
1130 1140
....*....|....*....|....*....
gi 251823980 1151 TSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK12999 1117 TAPVDGTVKRVLVKAGDQVEAGDLLVELE 1145
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
40-1179 |
0e+00 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 1735.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 40 KVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRG--LAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAANELGIRTVAIYSEEDKLSLHRQKADESYQVGEGpdLGPIEAYLSIDEIIRVAKLNGVDAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:TIGR01235 81 GYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGTDGPPETMEEVLDFAAAIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:TIGR01235 161 WGGGGRGMRVVRSEADVADAFQRAKSEAKAAFGNDEVYVEKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:TIGR01235 241 VAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVDNDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 LP--DLGL-RQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISPHYDSLLVKVIAHG 434
Cdd:TIGR01235 321 LPtpQLGVpNQEDIRTNGYAIQCRVTTEDPANNFQPDTGRIEAYRSAGGFGIRLDGGNSYAGAIITPYYDSLLVKVSAWA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 435 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRAQKLLHYLGHVMVNG-P 513
Cdd:TIGR01235 401 STPEEAAAKMDRALREFRIRGVKTNIPFLENVLGHPKFLDGSYDTRFIDTTPELFQFVKSQDRATKLLTYLADVTVNGhP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 514 TTPIPVNVSPSPVDPAVPVVPIGPPPAGFRDILLREGPEGFARAVRNHQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAP 593
Cdd:TIGR01235 481 EAKDKLKPLENAPRVVVLYADQNPVPRGTKQILDEKGPEGFAEWVRNQKRVLLTDTTFRDAHQSLLATRVRTHDLAKIAP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 594 YVAHNFNKLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMD 673
Cdd:TIGR01235 561 TTSHALPNLFSLECWGGATFDVAMRFLHEDPWERLEDLRKGVPNILFQMLLRGANGVGYTNYPDNVVKYFVKQAAQGGID 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 674 VFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAAC 753
Cdd:TIGR01235 641 IFRVFDSLNWVENMRVGMDAVAEAGKVVEAAICYTGDILDPARPKYDLKYYTNLAVELEKAGAHILGIKDMAGLLKPAAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 754 TMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVF 833
Cdd:TIGR01235 721 KLLIKALREKT-DLPIHFHTHDTSGIAVASMLAAVEAGVDVVDVAVDSMSGLTSQPSLGAIVAALEGSERDPGLNVAWIR 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 834 DYSEYWEGARGLYAAFDCtaTMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSK 913
Cdd:TIGR01235 800 ELSAYWEAVRNLYAAFES--DLKGPASEVYLHEMPGGQYTNLQFQARSLGLGDRWHEVKQAYREANQMFGDIVKVTPSSK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 914 IVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEK 993
Cdd:TIGR01235 878 VVGDMALFMVSNDLTVDDVVEPAEELSFPDSVVEFLKGDIGQPHGGFPEPLQKKVLKGEKPITVRPGSLLEPADLDAIRK 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 994 DLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAG 1073
Cdd:TIGR01235 958 DLQEKHEREVSDFDVASYAMYPKVFTDFAKARDTYGPVSVLPTPAFFYGLADGEEIEVDIEKGKTLIIKLQAVGATDSQG 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1074 QRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSP 1153
Cdd:TIGR01235 1038 EREVFFELNGQPRRIKVPDRSHKAEAAVRRKADPGNPAHVGAPMPGVIIEVKVSSGQAVNKGDPLVVLEAMKMETAIQAP 1117
|
1130 1140
....*....|....*....|....*.
gi 251823980 1154 MEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:TIGR01235 1118 KDGTIKEVLVKAGEQIDAKDLLLVLE 1143
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
37-498 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 717.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 37 PIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVH 116
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIG-PAPAAESYLNIDAIIAAAKATGADAIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 117 PGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKA 196
Cdd:COG4770 80 PGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 197 AYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVV 276
Cdd:COG4770 160 SAGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 277 EIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGR 356
Cdd:COG4770 240 EEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 357 SLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKD 436
Cdd:COG4770 320 PLP---FTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSG-VYEGYEIPPYYDSMIAKLIVWGPD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823980 437 HPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQLRPAQNRA 498
Cdd:COG4770 396 REEAIARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPEEL 457
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
38-485 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 631.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSK-KSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK08591 321 LS---IKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSA-VYTGYTIPPYYDSMIGKLIVHGETR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 251823980 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDEN 485
Cdd:PRK08591 397 EEAIARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKK 444
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
39-488 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 588.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 39 KKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHPG 118
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPA-PPSKSYLNIERIIDVAKKAGADAIHPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 119 YGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAY 198
Cdd:PRK08654 82 YGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 199 GGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEI 278
Cdd:PRK08654 162 GGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 279 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSL 358
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSN-GNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 359 PdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHP 438
Cdd:PRK08654 321 S---FKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVD-SGVHMGYEIPPYYDSMISKLIVWGRTRE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 251823980 439 TAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPEL 488
Cdd:PRK08654 397 EAIARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEETTI 446
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
38-482 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 570.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIG-GPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 LPdlgLRQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDNASAfQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK06111 321 LS---FTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVE-NGVTVTPFYDPMIAKLIAHGETR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 251823980 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFI 482
Cdd:PRK06111 396 EEAISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFL 440
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-490 |
1.36e-180 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 538.15 E-value: 1.36e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK07178 2 IKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD--PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK07178 320 LS---YKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTA-IYTGYTIPPYYDSMCAKLIVWALTW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 251823980 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFQ 490
Cdd:PRK07178 396 EEALDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESHPELTN 448
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
38-485 |
4.74e-178 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 530.44 E-value: 4.74e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPA-SSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 lpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:PRK05586 321 ---LSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSA-VYSGYTIPPYYDSMIGKLIVYGKDR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 251823980 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDEN 485
Cdd:PRK05586 397 EEAIQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIEKK 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
38-484 |
2.47e-176 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 525.87 E-value: 2.47e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPA-PSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAA 197
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 198 YGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVE 277
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 278 IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRS 357
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEFYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 358 LPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNAsAFQGAVISPHYDSLLVKVIAHGKDH 437
Cdd:TIGR00514 321 LS---LKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSH-VYSGYTVPPYYDSMIGKLITYGKTR 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 251823980 438 PTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDE 484
Cdd:TIGR00514 397 EVAIARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEK 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
36-483 |
3.75e-165 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 497.74 E-value: 3.75e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGLAPvQAYLHIPDIIKVAKENGVDAV 115
Cdd:PRK12833 3 SRIRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAA-KSYLNPAAILAAARQCGADAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFK 195
Cdd:PRK12833 82 HPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYgNILHLYERDCSIQRRHQKV 275
Cdd:PRK12833 162 AAAGGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKH-GKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSE 354
Cdd:PRK12833 241 LEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDArGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 355 GRSlpdLGLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHG 434
Cdd:PRK12833 321 GEP---LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVD-SLLYPGYRVPPFYDSLLAKLIVHG 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 251823980 435 KDHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFID 483
Cdd:PRK12833 397 EDRAAALARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLE 445
|
|
| DRE_TIM_PC_TC_5S |
cd07937 |
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes ... |
566-849 |
2.86e-162 |
|
Pyruvate carboxylase and Transcarboxylase 5S, carboxyltransferase domain; This family includes the carboxyltransferase domains of pyruvate carboxylase (PC) and the transcarboxylase (TC) 5S subunit. Transcarboxylase 5S is a cobalt-dependent metalloenzyme subunit of the biotin-dependent transcarboxylase multienzyme complex. Transcarboxylase 5S transfers carbon dioxide from the 1.3S biotin to pyruvate in the second of two carboxylation reactions catalyzed by TC. The first reaction involves the transfer of carbon dioxide from methylmalonyl-CoA to the 1.3S biotin, and is catalyzed by the 12S subunit. These two steps allow a carboxylate group to be transferred from oxaloacetate to propionyl-CoA to yield pyruvate and methylmalonyl-CoA. The catalytic domain of transcarboxylase 5S has a canonical TIM-barrel fold with a large C-terminal extension that forms a funnel leading to the active site. Transcarboxylase 5S forms a homodimer and there are six dimers per complex. In addition to the catalytic domain, transcarboxylase 5S has several other domains including a carbamoyl-phosphate synthase domain, a biotin carboxylase domain, a carboxyltransferase domain, and an ATP-grasp domain. Pyruvate carboxylase, like TC, is a biotin-dependent enzyme that catalyzes the carboxylation of pyruvate to produce oxaloacetate. In mammals, PC has critical roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion. Inherited PC deficiencies are linked to serious diseases in humans such as lactic acidemia, hypoglycemia, psychomotor retardation, and death. PC is a single-chain enzyme and is active only in its homotetrameric form. PC has three domains, an N-terminal biotin carboxylase domain, a carboxyltransferase domain (this alignment model), and a C-terminal biotin-carboxyl carrier protein domain. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163675 Cd Length: 275 Bit Score: 482.32 E-value: 2.86e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 566 LMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFnkLFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:cd07937 1 ITDTTLRDAHQSLLATRMRTEDMLPIAEALDEAG--FFSLEVWGGATFDVCMRFLNEDPWERLRELRKAMPNTPLQMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 646 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDvadpsrTKYSLEYYM 725
Cdd:cd07937 79 GQNLVGYRHYPDDVVELFVEKAAKNGIDIFRIFDALNDVRNLEVAIKAVKKAGKHVEGAICYTGS------PVHTLEYYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 726 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPdLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGM 805
Cdd:cd07937 153 KLAKELEDMGADSICIKDMAGLLTPYAAYELVKALKKEVG-LPIHLHTHDTSGLAVATYLAAAEAGVDIVDTAISPLSGG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 251823980 806 TSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAF 849
Cdd:cd07937 232 TSQPSTESMVAALRGTGRDTGLDLEKLEEISEYFEEVRKKYAPF 275
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
36-485 |
1.03e-158 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 480.01 E-value: 1.03e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 36 KPIKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGrGLAPVQAYLHIPDIIKVAKENGVDAV 115
Cdd:PRK08462 2 KEIKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIG-GAKSSESYLNIPAIISAAEIFEADAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 116 HPGYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFK 195
Cdd:PRK08462 81 FPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 196 AAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKV 275
Cdd:PRK08462 161 AAAGGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 276 VEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEG 355
Cdd:PRK08462 241 IEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 356 RSLPDlglrQENIRINGCAIQCRVTTEDPaRSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGK 435
Cdd:PRK08462 321 EELPS----QESIKLKGHAIECRITAEDP-KKFYPSPGKITKWIAPGGRNVRMD-SHAYAGYVVPPYYDSMIGKLIVWGE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 251823980 436 DHPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDEN 485
Cdd:PRK08462 395 DRNRAIAKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
38-500 |
1.58e-157 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 478.15 E-value: 1.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlaPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTD--PIKGYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSPIS-SLHEAHEFSNTYGFPIIFKA 196
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSeSMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 197 AYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVV 276
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 277 EIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGR 356
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 357 SLPdlgLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKD 436
Cdd:PRK08463 320 ILD---LEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVD-SHIYKDYTIPPYYDSMLAKLIVKATS 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251823980 437 HPTAATKMSRALAEFRVRGVKTNIPFLQNVLNNQQFLAGTVDTQFIDENPELFqLRPAQNRAQK 500
Cdd:PRK08463 396 YDLAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIETHMQEL-LEKTEDRHQE 458
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
568-1179 |
8.09e-157 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 480.49 E-value: 8.09e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 568 DTTFRDAHQSLLATRVRTHDLKKIAPyvahnfnKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 642
Cdd:PRK09282 8 DTTLRDAHQSLLATRMRTEDMLPIAE-------KLdkvgfWSLEVWGGATFDVCIRYLNEDPWERLRKLKKALPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 643 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLE 722
Cdd:PRK09282 81 LLRGQNLVGYRHYPDDVVEKFVEKAAENGIDIFRIFDALNDVRNMEVAIKAAKKAGAHVQGTISYT---TSPVHT---IE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 723 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSM 802
Cdd:PRK09282 155 KYVELAKELEEMGCDSICIKDMAGLLTPYAAYELVKALKEEV-DLPVQLHSHCTSGLAPMTYLKAVEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 803 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMksGNSDVYENEIPGGQYTNLHFQAHSM 882
Cdd:PRK09282 234 AFGTSQPPTESMVAALKGTPYDTGLDLELLFEIAEYFREVRKKYKQFESEFTI--VDTRVLIHQVPGGMISNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 883 GLGSKFKEVKK--AYVEANqmLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGF 960
Cdd:PRK09282 312 NALDKLDEVLEeiPRVRED--LGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------VITKEVKDYVKGLYGRPPAPI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 961 PEPFRSKVLKDLPRIEGRPGASLPPlnlkELEKdlIDRHGEE---VTPEDVLSAAMYPDV----FAQFKDFTATFGPLDS 1033
Cdd:PRK09282 381 NEELRKKIIGDEEPITCRPADLLEP----ELEK--ARKEAEElgkSEKEDVLTYALFPQIakkfLEEREAGELKPEPEPK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1034 LNTRlfLQGPKIAEEFEVELErGKTLHIKALAVSdlnRAGQRQVFFELNGQLRSILVkdtQAMKEMHFHPKALKDVKGQI 1113
Cdd:PRK09282 455 EAAA--AGAEGIPTEFKVEVD-GEKYEVKIEGVK---AEGKRPFYLRVDGMPEEVVV---EPLKEIVVGGRPRASAPGAV 525
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251823980 1114 GAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK09282 526 TSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEIQAPVDGTVKEILVKEGDRVNPGDVLMEIE 591
|
|
| OadA1 |
COG5016 |
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate ... |
564-1021 |
2.61e-130 |
|
Pyruvate/oxaloacetate carboxyltransferase [Energy production and conversion]; Pyruvate/oxaloacetate carboxyltransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 444040 [Multi-domain] Cd Length: 540 Bit Score: 409.28 E-value: 2.61e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 564 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPY-VAHNFnklFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 642
Cdd:COG5016 4 VKITDTTLRDGHQSLFATRMRTEDMLPIAEKlDEAGF---WSLEVWGGATFDSCIRYLNEDPWERLRLLRKAMPNTPLQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 643 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVAdpsrtkYSLE 722
Cdd:COG5016 81 LLRGQNLVGYRHYPDDVVELFVKRAAENGIDIFRIFDALNDVRNLETAIKAAKKAGAHAQGAISYTISPV------HTVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 723 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSM 802
Cdd:COG5016 155 YYVELAKELEDMGADSICIKDMAGLLTPYRAYELVKALKEAL-DIPIELHTHATSGLAPATYLKAIEAGVDIIDTAISPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 803 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKsgNSDVYENEIPGGQYTNLHFQAHSM 882
Cdd:COG5016 234 AGGTSQPPTESMVAALKGTGYDTGLDLEALLEIADYFREVRKKYAKFEPEATGV--DPRVLVHQVPGGMLSNLVSQLKEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 883 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGYIGIPHGGFPE 962
Cdd:COG5016 312 GALDRLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYK--------MITKEVKDYVLGYYGKTPAPIDP 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 251823980 963 PFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIdrhgeEVTPEDVLSAAMYPDVFAQF 1021
Cdd:COG5016 383 EVRKKALGDEEPITCRPADLLEP-ELEKLRKEGL-----AKSDEDVLTYALFPQVAIKF 435
|
|
| oadA |
TIGR01108 |
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate ... |
568-1169 |
1.41e-126 |
|
oxaloacetate decarboxylase alpha subunit; This model describes the bacterial oxaloacetate decarboxylase alpha subunit and its equivalents in archaea. The oxaloacetate decarboxylase Na+ pump is the paradigm of the family of Na+ transport decarboxylases that present in bacteria and archaea. It a multi subunit enzyme consisting of a peripheral alpha-subunit and integral membrane subunits beta and gamma. The energy released by the decarboxylation reaction of oxaloacetate is coupled to Na+ ion pumping across the membrane. [Transport and binding proteins, Cations and iron carrying compounds, Energy metabolism, Other]
Pssm-ID: 273447 [Multi-domain] Cd Length: 582 Bit Score: 400.71 E-value: 1.41e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 568 DTTFRDAHQSLLATRVRTHDLKKIApyvahnfNKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 642
Cdd:TIGR01108 3 DVVLRDAHQSLFATRMRTEDMLPIA-------EKLddvgyWSLEVWGGATFDACIRFLNEDPWERLRELKKALPNTPLQM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 643 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLE 722
Cdd:TIGR01108 76 LLRGQNLLGYRHYADDVVERFVKKAVENGMDVFRIFDALNDPRNLQAAIQAAKKHGAHAQGTISYT---TSPVHT---LE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 723 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSM 802
Cdd:TIGR01108 150 TYLDLAEELLEMGVDSICIKDMAGILTPKAAYELVSALKKRF-GLPVHLHSHATTGMAEMALLKAIEAGADGIDTAISSM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 803 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSM 882
Cdd:TIGR01108 229 SGGTSHPPTETMVAALRGTGYDTGLDIELLLEIAAYFREVRKKYSQFE--GQLKGPDSRILVAQVPGGMLSNLESQLKEQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 883 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAEAqaeelsfpRSVVEFLQGYIGIPHGGFPE 962
Cdd:TIGR01108 307 NALDKLDEVLEEIPRVREDLGYPPLVTPTSQIVGTQAVLNVLTG-ERYKTIT--------KETKGYLKGEYGRTPAPINA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 963 PFRSKVLKDL-PRIEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFKDFTATFGPLDSLntrlfLQ 1041
Cdd:TIGR01108 378 ELQRKILGDEkPIVDCRPADLLEP-ELDKLRAEVREAGAEKNSIEDVLTYALFPQVGLKFLENRHNPAAFEPK-----PE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1042 GPKIAEEfevelergktlHIKAlAVSDLNRAGQRQVFFELNGQLRSILVKD-------TQAMKEMHFHPKALKDVK--GQ 1112
Cdd:TIGR01108 452 EKVIEQE-----------HAQV-VGKYEETHASGSYTVEVEGKAFVVKVSPggdvsqiTASAPANTSGGTVAAKAGagTP 519
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251823980 1113 IGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKV------HVTKDMTL 1169
Cdd:TIGR01108 520 VTAPIAGSIVKVKVSEGQTVAEGEVLLILEAMKMETEIKAAAAGTVREIlvkvgdAVSVGQVL 582
|
|
| PRK14040 |
PRK14040 |
oxaloacetate decarboxylase subunit alpha; |
564-1172 |
2.60e-103 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 237592 [Multi-domain] Cd Length: 593 Bit Score: 338.83 E-value: 2.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 564 LLLMDTTFRDAHQSLLATRVRTHDLKKIAPyvahnfnKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNI 638
Cdd:PRK14040 5 LAITDVVLRDAHQSLFATRLRLDDMLPIAA-------KLdkvgyWSLESWGGATFDACIRFLGEDPWERLRELKKAMPNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 639 PFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTk 718
Cdd:PRK14040 78 PQQMLLRGQNLLGYRHYADDVVERFVERAVKNGMDVFRVFDAMNDPRNLETALKAVRKVGAHAQGTLSYT---TSPVHT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 719 ysLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVA 798
Cdd:PRK14040 154 --LQTWVDLAKQLEDMGVDSLCIKDMAGLLKPYAAYELVSRIKKRV-DVPLHLHCHATTGLSTATLLKAIEAGIDGVDTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 799 VDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQ 878
Cdd:PRK14040 231 ISSMSMTYGHSATETLVATLEGTERDTGLDILKLEEIAAYFREVRKKYAKFE--GQLKGVDSRILVAQVPGGMLTNMESQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 879 AHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEaeaqaeelSFPRSVVEFLQGyigiPHG 958
Cdd:PRK14040 309 LKEQGAADKLDEVLAEIPRVREDLGFIPLVTPTSQIVGTQAVLNVLTG-ERYK--------TITKETAGVLKG----EYG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 959 GFPEPF----RSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGE------EVTPEDVLSAAMYPDV---FAQFKDFT 1025
Cdd:PRK14040 376 ATPAPVnaelQARVLEGAEPITCRPADLLAP-ELDKLEAELRRQAQEkgitlaENAIDDVLTYALFPQIglkFLENRHNP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1026 ATFGPLDSL-NTRLFLQGPKIAEE-FEVELErGKTLHIKalaVSDlnragqrqvffelNGQLRSILVKDTQAMKEMHFHP 1103
Cdd:PRK14040 455 AAFEPVPQAeAAQPAAKAEPAGSEtYTVEVE-GKAYVVK---VSE-------------GGDISQITPAAPAAAPAAAAAA 517
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251823980 1104 KALKDVKGQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD 1172
Cdd:PRK14040 518 APAAAAGEPVTAPLAGNIFKVIVTEGQTVAEGDVLLILEAMKMETEIRAAQAGTVRGIAVK-----EGD 581
|
|
| PRK12331 |
PRK12331 |
oxaloacetate decarboxylase subunit alpha; |
566-1021 |
2.18e-97 |
|
oxaloacetate decarboxylase subunit alpha;
Pssm-ID: 183446 [Multi-domain] Cd Length: 448 Bit Score: 317.80 E-value: 2.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 566 LMDTTFRDAHQSLLATRVRTHDLKKIApyvahnfNKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPF 640
Cdd:PRK12331 6 ITETVLRDGQQSLIATRMTTEEMLPIL-------EKLdnagyHSLEMWGGATFDACLRFLNEDPWERLRKIRKAVKKTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 641 QMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkys 720
Cdd:PRK12331 79 QMLLRGQNLLGYRNYADDVVESFVQKSVENGIDIIRIFDALNDVRNLETAVKATKKAGGHAQVAISYT---TSPVHT--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 721 LEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSgaGVAAM--LACAQAGADVVDVA 798
Cdd:PRK12331 153 IDYFVKLAKEMQEMGADSICIKDMAGILTPYVAYELVKRIKEAV-TVPLEVHTHATS--GIAEMtyLKAIEAGADIIDTA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 799 VDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLY-AAFDCTATMKSGNSDVYENEIPGGQYTNLHF 877
Cdd:PRK12331 230 ISPFAGGTSQPATESMVAALQDLGYDTGLDLEELSEIAEYFNPIRDHYrEEGILNPKVKDVEPKTLIYQVPGGMLSNLLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 878 QAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlSRAEAeaqaeelsFPRSVVEFLQGYIGIPH 957
Cdd:PRK12331 310 QLKEQGAEDKYEEVLKEVPKVRADLGYPPLVTPLSQMVGTQALMNVISG-ERYKM--------VPNEIKDYVRGLYGRPP 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251823980 958 GGFPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRHGEEvtpEDVLSAAMYPDVFAQF 1021
Cdd:PRK12331 381 APIAEEIKKKIIGDEEVITCRPADLIEP-QLEKLREEIAEYAESE---EDVLSYALFPQQAKDF 440
|
|
| PYC_OADA |
pfam02436 |
Conserved carboxylase domain; This domain represents a conserved region in pyruvate ... |
862-1062 |
3.76e-95 |
|
Conserved carboxylase domain; This domain represents a conserved region in pyruvate carboxylase (PYC), oxaloacetate decarboxylase alpha chain (OADA), and transcarboxylase 5s subunit. The domain is found adjacent to the HMGL-like domain (pfam00682) and often close to the biotin_lipoyl domain (pfam00364) of biotin requiring enzymes.
Pssm-ID: 460557 [Multi-domain] Cd Length: 201 Bit Score: 302.07 E-value: 3.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 862 VYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSF 941
Cdd:pfam02436 1 VYKHEIPGGQLSNLQQQAKEQGLGDRFDEVLKEYPRVNKDLGDIPKVTPSSQIVGDQAVFNVLNNLTPEDVLGEGRYKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 942 PRSVVEFLQGYIGIPHGGFPEPFRSKVLKDLPRIEGRPGASLPPLNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1021
Cdd:pfam02436 81 PDSVVDYLKGEYGQPPGGFPEELQKKVLKGEEPITCRPGDLLPPVDLEKLRKELEEKAGRETTEEDVLSYALYPKVAEKF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 251823980 1022 KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIK 1062
Cdd:pfam02436 161 LKFREKYGDVSVLPTPVFFYGLEPGEEYEVEIEGGKYLIVK 201
|
|
| PRK14042 |
PRK14042 |
pyruvate carboxylase subunit B; Provisional |
565-1179 |
1.25e-93 |
|
pyruvate carboxylase subunit B; Provisional
Pssm-ID: 172536 [Multi-domain] Cd Length: 596 Bit Score: 312.43 E-value: 1.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 565 LLMDTTFRDAHQSLLATRVRTHDLKKIApyvahnfNKL-----FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIP 639
Cdd:PRK14042 5 FITDVTLRDAHQCLIATRMRTEDMLPIC-------NKMddvgfWAMEVWGGATFDACLRFLKEDPWSRLRQLRQALPNTQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 640 FQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTKY 719
Cdd:PRK14042 78 LSMLLRGQNLLGYRNYADDVVRAFVKLAVNNGVDVFRVFDALNDARNLKVAIDAIKSHKKHAQGAICYT------TSPVH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 720 SLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAV 799
Cdd:PRK14042 152 TLDNFLELGKKLAEMGCDSIAIKDMAGLLTPTVTVELYAGLK-QATGLPVHLHSHSTSGLASICHYEAVLAGCNHIDTAI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 800 DSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATMKSGNSDVYenEIPGGQYTNLHFQA 879
Cdd:PRK14042 231 SSFSGGASHPPTEALVAALTDTPYDTELDLNILLEIDDYFKAVRKKYSQFESEAQNIDPRVQLY--QVPGGMISNLYNQL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 880 HSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqAEELSFPRSVVEFLQGYIGIPHGG 959
Cdd:PRK14042 309 KEQNALDKMDAVHKEIPRVRKDLGYPPLVTPTSQVVGTQAVINVLTG---------ERYKTITNEVKLYCQGKYGTPPGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 960 FPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFKDFTATFGPL-DSLNTRL 1038
Cdd:PRK14042 380 ISSALRKKAIGRTEVIEVRPGDLLPN-ELDQLQNEISDL---ALSDEDVLLYAMFPEIGRQFLEQRKNNQLIpEPLLTQS 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1039 FLQGPKIAEEFEVELErGKTLHIKaLAVSDLNRAGQRQVFFELNGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMP 1118
Cdd:PRK14042 456 SAPDNSVMSEFDIILH-GESYHVK-VAGYGMIEHGQQSCFLWVDGVPEEVVVQHSELHDKIERSSVNNKIGPGDITVAIP 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251823980 1119 GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK14042 534 GSIIAIHVSAGDEVKAGQAVLVIEAMKMETEIKAPANGVVAEILCQKGDKVTPGQVLIRVE 594
|
|
| PRK14041 |
PRK14041 |
pyruvate carboxylase subunit B; |
565-1054 |
2.75e-90 |
|
pyruvate carboxylase subunit B;
Pssm-ID: 237593 [Multi-domain] Cd Length: 467 Bit Score: 299.01 E-value: 2.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 565 LLMDTTFRDAHQSLLATRVRTHDLKKIApyvaHNFNKL--FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQM 642
Cdd:PRK14041 4 MFVDTTLRDGHQSLIATRMRTEDMLPAL----EAFDRMgfYSMEVWGGATFDVCVRFLNENPWERLKEIRKRLKNTKIQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 643 LLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLE 722
Cdd:PRK14041 80 LLRGQNLVGYRHYADDVVELFVKKVAEYGLDIIRIFDALNDIRNLEKSIEVAKKHGAHVQGAISYT---VSPVHT---LE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 723 YYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSM 802
Cdd:PRK14041 154 YYLEFARELVDMGVDSICIKDMAGLLTPKRAYELVKALKKKF-GVPVEVHSHCTTGLASLAYLAAVEAGADMFDTAISPF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 803 SGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDctATMKSGNSDVYENEIPGGQYTNLHFQAHSM 882
Cdd:PRK14041 233 SMGTSQPPFESMYYAFRENGKETDFDRKALKFLVEYFTKVREKYSEYD--VGMKSPDSRILVSQIPGGMYSNLVKQLKEQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 883 GLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIPHGGFPE 962
Cdd:PRK14041 311 KMLHKLDKVLEEVPRVRKDLGYPPLVTPTSQIVGVQAVLNVLTGERYKRVT---------NETKNYVKGLYGRPPAPIDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 963 PFRSKVLKDLPRIEGRPGASLPPlnlkELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQFkdftatfgpldsLNTRlFLQG 1042
Cdd:PRK14041 382 ELMKKILGDEKPIDCRPADLLEP----ELEKARKELGILAETDEDLLIYVILGEVGKKF------------LKKK-YEEK 444
|
490
....*....|..
gi 251823980 1043 PKIAEEFEVELE 1054
Cdd:PRK14041 445 IGVDFNLLEELS 456
|
|
| PRK12330 |
PRK12330 |
methylmalonyl-CoA carboxytransferase subunit 5S; |
572-1021 |
1.86e-81 |
|
methylmalonyl-CoA carboxytransferase subunit 5S;
Pssm-ID: 183445 [Multi-domain] Cd Length: 499 Bit Score: 275.87 E-value: 1.86e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 572 RDAHQSLLATRVRTHDLKKI------APYvahnfnklFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:PRK12330 13 RDAHQSLMATRMAMEDMVGAcedidnAGY--------WSVECWGGATFDACIRFLNEDPWERLRTFRKLMPNSRLQMLLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 646 GANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvADPSRTkysLEYYM 725
Cdd:PRK12330 85 GQNLLGYRHYEDEVVDRFVEKSAENGMDVFRVFDALNDPRNLEHAMKAVKKVGKHAQGTICYT---VSPIHT---VEGFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 726 GLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMS- 803
Cdd:PRK12330 159 EQAKRLLDMGADSICIKDMAALLKPQPAYDIVKGIKEACgEDTRINLHCHSTTGVTLVSLMKAIEAGVDVVDTAISSMSl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 804 GMTSQPSMgALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAFDCTATmkSGNSDVYENEIPGGQYTNLHFQAHSMG 883
Cdd:PRK12330 239 GPGHNPTE-SLVEMLEGTGYTTKLDMDRLLKIRDHFKKVRPKYKEFESKTT--GVETEIFKSQIPGGMLSNMESQLKQQG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 884 LGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGlsraeaeaqaeelSFPRSVVEF---LQGYIGIPhggf 960
Cdd:PRK12330 316 AGDRMDEVLEEVPRVRKDAGYPPLVTPSSQIVGTQAVFNVLMG-------------RYKVLTGEFadlMLGYYGET---- 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251823980 961 PEPFRSKVLKDLPR------IEGRPGASLPPlNLKELEKDLIDRHGEEVTPEDVLSAAMYPDVFAQF 1021
Cdd:PRK12330 379 PGERNPEVVEQAKKqakkepITCRPADLLEP-EWDKLRAEALALEGCDGSDEDVLTYALFPQVAPKF 444
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
152-359 |
3.68e-77 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 253.00 E-value: 3.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 152 DKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGN 231
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 232 GALFVEKFIEKPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTV 311
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251823980 312 EFLVD-KHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVSEGRSLP 359
Cdd:pfam02786 161 EFALDpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
567-840 |
5.01e-71 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 238.12 E-value: 5.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 567 MDTTFRDAHQSLLATRvRTHDLKKIAPYVAHNfnKLFSMENWGGATFDVAmrFLYECPWRRLQELRELIPNIPFQMLLRG 646
Cdd:cd03174 1 TDTTLRDGLQSEGATF-STEDKLEIAEALDEA--GVDSIEVGSGASPKAV--PQMEDDWEVLRAIRKLVPNVKLQALVRN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 647 anavgytnypdnvVFKFCEVAKENGMDVFRVFDSLNY--------------LPNMLLGMEAAGSAGGVVEAAISYTgdva 712
Cdd:cd03174 76 -------------REKGIERALEAGVDEVRIFDSASEthsrknlnksreedLENAEEAIEAAKEAGLEVEGSLEDA---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 713 dpSRTKYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGA 792
Cdd:cd03174 139 --FGCKTDPEYVLEVAKALEEAGADEISLKDTVGLATPEEVAELVKALREALPDVPLGLHTHNTLGLAVANSLAALEAGA 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 251823980 793 DVVDVAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWE 840
Cdd:cd03174 217 DRVDGSVNGLGERAGNAATEDLVAALEGLGIDTGIDLEKLLEISRYVE 264
|
|
| PRK12581 |
PRK12581 |
oxaloacetate decarboxylase; Provisional |
561-1042 |
7.98e-66 |
|
oxaloacetate decarboxylase; Provisional
Pssm-ID: 79056 [Multi-domain] Cd Length: 468 Bit Score: 230.78 E-value: 7.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 561 HQGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVahnfNKL--FSMENWGGATFDVAMRFLYECPWRRLQELRELIPNI 638
Cdd:PRK12581 10 QQQVAITETVLRDGHQSLMATRLSIEDMLPVLTIL----DKIgyYSLECWGGATFDACIRFLNEDPWERLRTLKKGLPNT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 639 PFQMLLRGANAVGYTNYPDNVVFKFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTgdvadpSRTK 718
Cdd:PRK12581 86 RLQMLLRGQNLLGYRHYADDIVDKFISLSAQNGIDVFRIFDALNDPRNIQQALRAVKKTGKEAQLCIAYT------TSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 719 YSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRdRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVA 798
Cdd:PRK12581 160 HTLNYYLSLVKELVEMGADSICIKDMAGILTPKAAKELVSGIK-AMTNLPLIVHTHATSGISQMTYLAAVEAGADRIDTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 799 VDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEYWEGARGLYAAfDCT--ATMKSGNSDVYENEIPGGQYTNLH 876
Cdd:PRK12581 239 LSPFSEGTSQPATESMYLALKEAGYDITLDETLLEQAANHLRQARQKYLA-DGIldPSLLFPDPRTLQYQVPGGMLSNML 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 877 FQAHSMGLGSKFKEVKKAYVEANQMLGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEaqaeelsfpRSVVEFLQGYIGIP 956
Cdd:PRK12581 318 SQLKQANAESKLEEVLAEVPRVRKDLGYPPLVTPLSQMVGTQAAMNVILGKPYQMVS---------KEIKQYLAGDYGKT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 957 HGGFPEPFRSKVLKDLPRIEGRPGASLPPlNLKELEKDLIDRhgeEVTPEDVLSAAMYPDVFAQFkdFTATFGPLDSLNT 1036
Cdd:PRK12581 389 PAPVNEDLKRSQIGSAPVTTNRPADQLSP-EFEVLKAEVADL---AQTDEDVLTYALFPSVAKPF--LTTKYQTDDVIKV 462
|
....*.
gi 251823980 1037 RLFLQG 1042
Cdd:PRK12581 463 TAFIKA 468
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
38-146 |
2.26e-58 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 195.78 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEIAIRVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIGRGlAPVQAYLHIPDIIKVAKENGVDAVHP 117
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPG-PASESYLNIDAIIDAAKETGADAIHP 79
|
90 100
....*....|....*....|....*....
gi 251823980 118 GYGFLSERADFAQACQDAGVRFIGPSPEV 146
Cdd:pfam00289 80 GYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
99-356 |
3.28e-55 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 192.78 E-value: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 99 HIPDIIKVAKE----NGVDAVHPGYGFLSERAdfAQACQDAGVRfiGPSPEVVRKMGDKVEARAIAIAAGVPVvPGTDsP 174
Cdd:COG0439 1 DIDAIIAAAAElareTGIDAVLSESEFAVETA--AELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFA-L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 175 ISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIEKpRHIEVQILGDQ 254
Cdd:COG0439 75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 255 yGNILHlyerdCSIQRRHQK---VVE---IAPAThLDPQLRSRLTSDSVKLAKQVGYEN-AGTVEFLVDKHGKHYFIEVN 327
Cdd:COG0439 154 -GEVVV-----CSITRKHQKppyFVElghEAPSP-LPEELRAEIGELVARALRALGYRRgAFHTEFLLTPDGEPYLIEIN 226
|
250 260 270
....*....|....*....|....*....|.
gi 251823980 328 SRLQVEH--TVTEEITDVDLVHAQIHVSEGR 356
Cdd:COG0439 227 ARLGGEHipPLTELATGVDLVREQIRLALGE 257
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
376-483 |
2.98e-50 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 172.60 E-value: 2.98e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 376 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 455
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVD-SGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*...
gi 251823980 456 VKTNIPFLQNVLNNQQFLAGTVDTQFID 483
Cdd:smart00878 80 VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
376-484 |
5.15e-44 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 154.96 E-value: 5.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 376 QCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDnASAFQGAVISPHYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRG 455
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVD-SGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG 79
|
90 100
....*....|....*....|....*....
gi 251823980 456 VKTNIPFLQNVLNNQQFLAGTVDTQFIDE 484
Cdd:pfam02785 80 VKTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| HMGL-like |
pfam00682 |
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and ... |
566-838 |
2.15e-29 |
|
HMGL-like; This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase.
Pssm-ID: 459902 [Multi-domain] Cd Length: 264 Bit Score: 118.60 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 566 LMDTTFRDAHQSLlATRVRTHDLKKIAPyvahnfnklfSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLR 645
Cdd:pfam00682 4 ICDTTLRDGEQAL-GVAFSIDEKLAIAR----------ALDAAGVDEIEVGFPAASEDDFEVVRAIAKVIPHARILVLCR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 646 GAnavgytnypDNVVFKFCEVAKENGMDVFRVFDSLNYLP-NMLLGM---EAAGSAGGVVEAAISYTGDVA----DPSRT 717
Cdd:pfam00682 73 AR---------EHDIKAAVEALKGAGAVRVHVFIATSDLHrKYKLGKdreEVAKRAVAAVKAARSRGIDVEfspeDASRT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 718 kySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPD-LPLHIHTHDTSGAGVAAMLACAQAGADVVD 796
Cdd:pfam00682 144 --DPEFLAEVVEAAIEAGATRINIPDTVGVLTPNEAAELISALKARVPNkAIISVHCHNDLGMAVANSLAAVEAGADRVD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 251823980 797 VAVDSMSGMTSQPSMGALVACTKGTPLDTEVPLERVFDYSEY 838
Cdd:pfam00682 222 GTVNGIGERAGNAALEEVAAALEGLGVDTGLDLQRLRSIANL 263
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
1112-1178 |
1.31e-25 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 100.95 E-value: 1.31e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251823980 1112 QIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:cd06850 1 EVTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
1112-1178 |
5.72e-20 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 84.96 E-value: 5.72e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823980 1112 QIGAPMPGKVID-----IKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:pfam00364 2 EIKSPMIGESVRegvveWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
1111-1179 |
3.93e-15 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 73.39 E-value: 3.93e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251823980 1111 GQIGAPMPGKV-------IDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:COG0511 61 GAVKSPMVGTFyrapspgAKPFVKVGDKVKAGDTLCIIEAMKMMNEIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PRK06549 |
PRK06549 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1113-1175 |
6.47e-14 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235826 [Multi-domain] Cd Length: 130 Bit Score: 69.84 E-value: 6.47e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251823980 1113 IGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1175
Cdd:PRK06549 64 MPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMENEIVASSAGTVTAIHVTPGQVVNpGDGLI 127
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
36-330 |
9.14e-14 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 76.19 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 36 KPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQAYlHIPDII 104
Cdd:TIGR01369 4 TDIKKILVIGSGPIVIgqaaefdysgsQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIE-----PLTPE-AVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 105 KvaKENgVDAVHPGYG---------FLSERAdfaqACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGtdSPI 175
Cdd:TIGR01369 78 E--KER-PDAILPTFGgqtalnlavELEESG----VLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPES--EIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 176 SSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRayseALAAFGNGALFVEKFIEKPRHIEVQILGDQY 255
Cdd:TIGR01369 149 HSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAER----ALSASPINQVLVEKSLAGWKEIEYEVMRDSN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 256 GNILHLyerdCSIQR-----RH--QKVVeIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVD-KHGKHYFIEVN 327
Cdd:TIGR01369 225 DNCITV----CNMENfdpmgVHtgDSIV-VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNpDSGRYYVIEVN 299
|
...
gi 251823980 328 SRL 330
Cdd:TIGR01369 300 PRV 302
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
102-414 |
5.00e-13 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 73.85 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 102 DIIKVAKENGVDAVHPGYGflSERA-DFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSpiSSLHE 180
Cdd:PRK12815 621 DVLNVAEAENIKGVIVQFG--GQTAiNLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTA--TDEEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 181 AHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSealaafGNGALFVEKFIEKpRHIEVQILGDQY----- 255
Cdd:PRK12815 697 AFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAENAS------QLYPILIDQFIDG-KEYEVDAISDGEdvtip 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 256 GNILHLYER-----DcSIQrrhqkvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRl 330
Cdd:PRK12815 770 GIIEHIEQAgvhsgD-SIA--------VLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVL-ANDEIYVLEVNPR- 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 331 qVEHTV--TEEITDVDLVHAQIHVSEGRSLPDLGLRQENIRINGcaiqcRVTTEDPARSFQ--PDTGRI---EVFRSGEG 403
Cdd:PRK12815 839 -ASRTVpfVSKATGVPLAKLATKVLLGKSLAELGYPNGLWPGSP-----FIHVKMPVFSYLkyPGVDNTlgpEMKSTGEV 912
|
330
....*....|.
gi 251823980 404 MGIRLDNASAF 414
Cdd:PRK12815 913 MGIDKDLEEAL 923
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
129-420 |
5.30e-13 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 73.88 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 129 AQACQDAGVRFIGPSPEVVrkmgDKVEARAIAIAA----GVPVVPGtdSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRG 204
Cdd:TIGR01369 646 AKALEEAGVPILGTSPESI----DRAEDREKFSELldelGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPSYVLGGRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 205 MRVVHSYEELeenyTRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQ-----YGNILHLyER------DCSIqrrhq 273
Cdd:TIGR01369 720 MEIVYNEEEL----RRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMEHI-EEagvhsgDSTC----- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 274 kvveIAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVdKHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVS 353
Cdd:TIGR01369 790 ----VLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV-KDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVM 864
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823980 354 EGRSLPDLGLRQEniringcAIQCRVTTEDPARSFQPDTGR-----IEVFRSGEGMGIRLDNASAFQGAVIS 420
Cdd:TIGR01369 865 LGKKLEELGVGKE-------KEPKYVAVKEPVFSFSKLAGVdpvlgPEMKSTGEVMGIGRDLAEAFLKAQLS 929
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1111-1175 |
1.68e-12 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 66.42 E-value: 1.68e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251823980 1111 GQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLE-GDDLI 1175
Cdd:PRK05641 85 NVVTAPMPGKILRILVREGQQVKVGQGLLILEAMKMENEIPAPKDGVVKKILVKEGDTVDtGQPLI 150
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
129-329 |
9.55e-12 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 69.14 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 129 AQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTdsPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVV 208
Cdd:COG0458 91 EEAGILEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSG--TATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 209 HSYEELEEnytrAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNIL------HLyER------DcSIqrrhqkVV 276
Cdd:COG0458 169 YNEEELEE----YLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIivgimeHI-EPagvhsgD-SI------CV 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 251823980 277 eiAPATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKhGKHYFIEVNSR 329
Cdd:COG0458 237 --APPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDD-GRVYVIEVNPR 286
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
1112-1179 |
1.82e-11 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 60.57 E-value: 1.82e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 251823980 1112 QIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTK-DMTLEGDDLiLEIE 1179
Cdd:PRK08225 3 KVYASMAGNVWKIVVKVGDTVEEGQDVVILESMKMEIPIVAEEAGTVKKINVQEgDFVNEGDVL-LEIE 70
|
|
| DRE_TIM_HMGL |
cd07938 |
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; ... |
691-799 |
2.49e-10 |
|
3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain; 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163676 Cd Length: 274 Bit Score: 62.80 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 691 MEAAGSAGGVVEAAIS------YTGDVaDPSRTkysleyyMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF 764
Cdd:cd07938 120 AELAKAAGLRVRGYVStafgcpYEGEV-PPERV-------AEVAERLLDLGCDEISLGDTIGVATPAQVRRLLEAVLERF 191
|
90 100 110
....*....|....*....|....*....|....*
gi 251823980 765 PDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAV 799
Cdd:cd07938 192 PDEKLALHFHDTRGQALANILAALEAGVRRFDSSV 226
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
101-348 |
6.54e-10 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 61.50 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 101 PDIIKVAKENGVDAVHPGYGFLSERADFAQACQDAGVRFIgPSPEVVRKMGDKVEARAIAIAAGVPVvpgtdsP----IS 176
Cdd:COG0189 46 PELYRGEDLSEFDAVLPRIDPPFYGLALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPV------PptlvTR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 177 SLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHIEVQI--LGDQ 254
Cdd:COG0189 119 DPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALE-----SILEALTELGSEPVLVQEFIPEEDGRDIRVlvVGGE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 255 YgniLHLYER-----DCSIQRRHQKVVEiapATHLDPQLRSRLtsdsVKLAKQVGYENAGtVEFLVDKHGkHYFIEVNSR 329
Cdd:COG0189 194 P---VAAIRRipaegEFRTNLARGGRAE---PVELTDEERELA----LRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVT 261
|
250
....*....|....*....
gi 251823980 330 LQVEHtvTEEITDVDLVHA 348
Cdd:COG0189 262 PGFRG--LERATGVDIAEA 278
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
152-327 |
1.48e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 60.51 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 152 DKVEARAIAIAAGVPVVPGTDSPISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALaAFGN 231
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA----ALEEAF-KYDD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 232 GALfVEKFIEkPRHIEVQILGDQYGNILHL---------------YERDcsiqrrhqKVVEIAPAtHLDPQLRSRLTSDS 296
Cdd:COG1181 170 KVL-VEEFID-GREVTVGVLGNGGPRALPPieivpengfydyeakYTDG--------GTEYICPA-RLPEELEERIQELA 238
|
170 180 190
....*....|....*....|....*....|.
gi 251823980 297 VKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:COG1181 239 LKAFRALGCRGYARVDFRLDEDGEPYLLEVN 269
|
|
| LeuA |
COG0119 |
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; ... |
700-799 |
1.53e-08 |
|
Isopropylmalate/homocitrate/citramalate synthases [Amino acid transport and metabolism]; Isopropylmalate/homocitrate/citramalate synthases is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439889 [Multi-domain] Cd Length: 452 Bit Score: 58.64 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 700 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHD 775
Cdd:COG0119 124 AVKYAKEHGLEVEfsaeDATRT--DPDFLLEVLEAAIEAGADRINLPDTVGGATPNEVADLIEELRERVPDVILSVHCHN 201
|
90 100
....*....|....*....|....
gi 251823980 776 TSGAGVAAMLACAQAGADVVDVAV 799
Cdd:COG0119 202 DLGLAVANSLAAVEAGADQVEGTI 225
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
1119-1178 |
3.54e-08 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 51.64 E-value: 3.54e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1119 GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVETDKATVEVEAPAAGVLAKILVEEGDTVPVGQVIAVI 74
|
|
| Biotinyl_lipoyl_domains |
cd06663 |
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
1112-1178 |
7.25e-08 |
|
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.
Pssm-ID: 133456 [Multi-domain] Cd Length: 73 Bit Score: 50.52 E-value: 7.25e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 251823980 1112 QIGAPMP------GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:cd06663 1 TILIPDLaqhlgdGTVVKWLKKVGDKVKKGDVLAEIEAMKATSDVEAPKSGTVKKVLVKEGTKVEGDTPLVKI 73
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
162-327 |
8.34e-08 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 53.86 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 162 AAGVPVVP------GTDSPISSLHEAHEFSnTYGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEALAAfgNGALF 235
Cdd:pfam07478 4 AAGLPVVPfvtftrADWKLNPKEWCAQVEE-ALGYPVFVKPARLGSSVGVSKVESREELQA----AIEEAFQY--DEKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 236 VEKFIEKpRHIEVQILGDQYGNILHLYER--DCSIQRRHQKVVE-----IAPAtHLDPQLRSRLTSDSVKLAKQVGYENA 308
Cdd:pfam07478 77 VEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDdsaqiVVPA-DLEEEQEEQIQELALKAYKALGCRGL 154
|
170
....*....|....*....
gi 251823980 309 GTVEFLVDKHGKHYFIEVN 327
Cdd:pfam07478 155 ARVDFFLTEDGEIVLNEVN 173
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
1112-1178 |
1.05e-07 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 50.07 E-value: 1.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251823980 1112 QIGAPM-PGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:COG0508 9 DLGESMtEGTIVEWLVKEGDTVKEGDPLAEVETDKATMEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
79-329 |
7.08e-07 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 52.58 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 79 QKADEAYLIGRGLAPvqAYlhIPDIIKVAKENGVDAVHPGY----GFLSE-RADFaqacQDAGVRFIGPSPEVVRKMGDK 153
Cdd:PRK12767 41 YFADKFYVVPKVTDP--NY--IDRLLDICKKEKIDLLIPLIdpelPLLAQnRDRF----EEIGVKVLVSSKEVIEICNDK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 154 VEARAIAIAAGVPVvPGTDSPISSLH-EAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEenytRAYSEalaafgNG 232
Cdd:PRK12767 113 WLTYEFLKENGIPT-PKSYLPESLEDfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELE----FLLEY------VP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 233 ALFVEKFIEkprHIE--VQILGDQYGNILHlyerdcSIQRRHQKVV--EIAPA-THLDPQLRSRLtsdsVKLAKQVGYEN 307
Cdd:PRK12767 182 NLIIQEFIE---GQEytVDVLCDLNGEVIS------IVPRKRIEVRagETSKGvTVKDPELFKLA----ERLAEALGARG 248
|
250 260
....*....|....*....|..
gi 251823980 308 AGTVEFLVDKhGKHYFIEVNSR 329
Cdd:PRK12767 249 PLNIQCFVTD-GEPYLFEINPR 269
|
|
| PRK09389 |
PRK09389 |
(R)-citramalate synthase; Provisional |
713-799 |
2.29e-06 |
|
(R)-citramalate synthase; Provisional
Pssm-ID: 236493 [Multi-domain] Cd Length: 488 Bit Score: 51.48 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 713 DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRfPDLPLHIHTHDTSGAGVAAMLACAQAGA 792
Cdd:PRK09389 136 DASRA--DLDFLKELYKAGIEAGADRICFCDTVGILTPEKTYELFKRLSEL-VKGPVSIHCHNDFGLAVANTLAALAAGA 212
|
....*..
gi 251823980 793 DVVDVAV 799
Cdd:PRK09389 213 DQVHVTI 219
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
136-330 |
3.76e-06 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.51 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 136 GVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVvPGTDSpISSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELE 215
Cdd:PRK12815 112 GVELLGTNIEAIQKGEDRERFRALMKELGEPV-PESEI-VTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 216 ENYTRAysEALAAFGNgaLFVEKFIEKPRHIEVQILGDQYGNILHLyerdCSIQRrhqkvVE-----------IAPATHL 284
Cdd:PRK12815 190 QLFKQG--LQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCITV----CNMEN-----IDpvgihtgdsivVAPSQTL 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 251823980 285 DPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYF-IEVNSRL 330
Cdd:PRK12815 257 TDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYlIEVNPRV 303
|
|
| DRE_TIM_IPMS |
cd07940 |
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate ... |
701-799 |
3.98e-06 |
|
2-isopropylmalate synthase (IPMS), N-terminal catalytic TIM barrel domain; 2-isopropylmalate synthase (IPMS) catalyzes an aldol-type condensation of acetyl-CoA and 2-oxoisovalerate yielding 2-isopropylmalate and CoA, the first committed step in leucine biosynthesis. This family includes the Arabidopsis thaliana IPMS1 and IPMS2 proteins, the Glycine max GmN56 protein, and the Brassica insularis BatIMS protein. This family also includes a group of archeal IPMS-like proteins represented by the Methanocaldococcus jannaschii AksA protein. AksA catalyzes the condensation of alpha-ketoglutarate and acetyl-CoA to form trans-homoaconitate, one of 13 steps in the conversion of alpha-ketoglutarate and acetylCoA to alpha-ketosuberate, a precursor to coenzyme B and biotin. AksA also catalyzes the condensation of alpha-ketoadipate or alpha-ketopimelate with acetylCoA to form, respectively, the (R)-homocitrate homologs (R)-2-hydroxy-1,2,5-pentanetricarboxylic acid and (R)-2-hydroxy-1,2,6- hexanetricarboxylic acid. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163678 Cd Length: 268 Bit Score: 49.75 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 701 VEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP--DLPLHIHTH 774
Cdd:cd07940 120 VEYAKSHGLDVEfsaeDATRT--DLDFLIEVVEAAIEAGATTINIPDTVGYLTPEEFGELIKKLKENVPniKVPISVHCH 197
|
90 100
....*....|....*....|....*
gi 251823980 775 DTSGAGVAAMLACAQAGADVVDVAV 799
Cdd:cd07940 198 NDLGLAVANSLAAVEAGARQVECTI 222
|
|
| PRK05889 |
PRK05889 |
biotin/lipoyl-binding carrier protein; |
1115-1178 |
4.20e-06 |
|
biotin/lipoyl-binding carrier protein;
Pssm-ID: 180306 [Multi-domain] Cd Length: 71 Bit Score: 45.57 E-value: 4.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 251823980 1115 APMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:PRK05889 7 AEIVASVLEVVVNEGDQIGKGDTLVLLESMKMEIPVLAEVAGTVSKVSVSVGDVIQAGDLIAVI 70
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
129-369 |
7.15e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.48 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 129 AQACQDAGVRFIGPSPEVVrkmgDKVEAR----AIAIAAGVPVVP-GTdspISSLHEAHEFSNTYGFPIIFKAAYGGGGR 203
Cdd:PRK05294 646 AKALEAAGVPILGTSPDAI----DLAEDRerfsKLLEKLGIPQPPnGT---ATSVEEALEVAEEIGYPVLVRPSYVLGGR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 204 GMRVVHSYEELEEnYTRaysEALAAFGNGALFVEKFIEKPRHIEVQILGD----QYGNIL-HLyER------D--CSIqr 270
Cdd:PRK05294 719 AMEIVYDEEELER-YMR---EAVKVSPDHPVLIDKFLEGAIEVDVDAICDgedvLIGGIMeHI-EEagvhsgDsaCSL-- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 271 rhqkvveiaPATHLDPQLRSRLTSDSVKLAKQ---VGYENagtVEFLVdKHGKHYFIEVN---SRlqvehTV--TEEITD 342
Cdd:PRK05294 792 ---------PPQTLSEEIIEEIREYTKKLALElnvVGLMN---VQFAV-KDDEVYVIEVNpraSR-----TVpfVSKATG 853
|
250 260
....*....|....*....|....*..
gi 251823980 343 VDLVHAQIHVSEGRSLPDLGLRQENIR 369
Cdd:PRK05294 854 VPLAKIAARVMLGKKLAELGYTKGLIP 880
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1113-1179 |
8.61e-06 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 49.87 E-value: 8.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251823980 1113 IGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:TIGR01348 8 IGDNEEGEVIEVLVKPGDKVEAGQSLITLESDKASMEVPSSAAGIIKEIKVKVGDTLPVGGVIATLE 74
|
|
| DRE_TIM_HOA |
cd07943 |
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy ... |
724-805 |
1.78e-05 |
|
4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain; 4-hydroxy 2-ketovalerate aldolase (Also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. This family includes the Escherichia coli MhpE aldolase, the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF ) and is inactive without it. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163681 Cd Length: 263 Bit Score: 47.88 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 724 YMGLAEELVR-------AGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVD 796
Cdd:cd07943 136 HMASPEELAEqaklmesYGADCVYVTDSAGAMLPDDVRERVRALREALDPTPVGFHGHNNLGLAVANSLAAVEAGATRID 215
|
....*....
gi 251823980 797 VavdSMSGM 805
Cdd:cd07943 216 G---SLAGL 221
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
142-325 |
3.49e-05 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 47.38 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 142 PSPEVVRKMGDKVEARAIAIAAGVPVVPGTdsPISSLHEAHEFSNTYGFPIIFKAAyggggrgmR---------VVHSYE 212
Cdd:COG0026 79 PGPEALEIAQDRLLEKAFLAELGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTR--------RggydgkgqvVIKSAA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 213 ELEenytraysEALAAFGNGALFVEKFI--EKprhiEVQILG--DQYGNILHlY---ErdcSIQRRHQKVVEIAPAtHLD 285
Cdd:COG0026 149 DLE--------AAWAALGGGPCILEEFVpfER----ELSVIVarSPDGEVAT-YpvvE---NVHRNGILDESIAPA-RIS 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 251823980 286 PQLRSRLTSDSVKLAKQVGYenAGT--VEFLVDKHGK--------------HYFIE 325
Cdd:COG0026 212 EALAAEAEEIAKRIAEALDY--VGVlaVEFFVTKDGEllvneiaprphnsgHWTIE 265
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1119-1179 |
4.16e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 47.69 E-value: 4.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251823980 1119 GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11854 15 VEVTEILVKVGDKVEAEQSLITVEGDKASMEVPSPQAGVVKEIKVKVGDKVETGALIMIFE 75
|
|
| DRE_TIM_CMS |
cd07945 |
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic ... |
718-840 |
6.84e-05 |
|
Leptospira interrogans citramalate synthase (CMS) and related proteins, N-terminal catalytic TIM barrel domain; Citramalate synthase (CMS) catalyzes the conversion of pyruvate and acetyl-CoA to (R)-citramalate in the first dedicated step of the citramalate pathway. Citramalate is only found in Leptospira interrogans and a few other microorganisms. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163683 [Multi-domain] Cd Length: 280 Bit Score: 46.21 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 718 KYSLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDV 797
Cdd:cd07945 143 RDSPDYVFQLVDFLSDLPIKRIMLPDTLGILSPFETYTYISDMVKRYPNLHFDFHAHNDYDLAVANVLAAVKAGIKGLHT 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 251823980 798 AVDSMSGMTSQPSMGALVACTKG-TPLDTEVPLERVFDYSEYWE 840
Cdd:cd07945 223 TVNGLGERAGNAPLASVIAVLKDkLKVKTNIDEKRLNRASRLVE 266
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1105-1179 |
7.24e-05 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 46.92 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1105 ALKDVKgqigapMP------GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:PRK11854 205 GVKDVN------VPdiggdeVEVTEVMVKVGDKVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVKTGSLIMRF 278
|
.
gi 251823980 1179 E 1179
Cdd:PRK11854 279 E 279
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
152-327 |
7.99e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.87 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 152 DKVEARAIAIAAGVPVVPGT--DSPISSLHEAHEFsntyGFPIIFKAAYGGGGRGMRVVHSYEELEEnytrAYSEAlAAF 229
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIvlTREEDLLAAIDKL----GLPLVVKPAREGSSVGVSKVKEEDELQA----ALELA-FKY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 230 GNGALfVEKFIeKPRHIEVQILGDQygnILhlyerdcsiqrrhqKVVEIAPATH--------------------LDPQLR 289
Cdd:PRK01372 169 DDEVL-VEKYI-KGRELTVAVLGGK---AL--------------PVIEIVPAGEfydyeakylaggtqyicpagLPAEIE 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 251823980 290 SRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:PRK01372 230 AELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVN 267
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1119-1179 |
8.36e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 46.74 E-value: 8.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 251823980 1119 GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11855 133 VEVIEWLVKVGDTVEEDQSLITVETDKATMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIE 193
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
1113-1179 |
8.58e-05 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 46.74 E-value: 8.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 251823980 1113 IGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:PRK11855 10 IGEVVEVEVIEWLVKEGDTVEEDQPLVTVETDKATMEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIE 76
|
|
| PRK14573 |
PRK14573 |
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase; |
139-327 |
9.80e-05 |
|
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
Pssm-ID: 184752 [Multi-domain] Cd Length: 809 Bit Score: 46.73 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 139 FIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGtdSPISsLHE--------AHEFSNTYGFPIIFKAAYGGGGRGMRVVHS 210
Cdd:PRK14573 555 YTGPSLAFSAIAMDKVLTKRFASDVGVPVVPY--QPLT-LAGwkrepelcLAHIVEAFSFPMFVKTAHLGSSIGVFEVHN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 211 YEELEEnytrAYSEALAAfgNGALFVEKFIEKPRHIEVQILGDQYGN--ILHLYERdC------SIQRRH----QKVVEI 278
Cdd:PRK14573 632 VEELRD----KISEAFLY--DTDVFVEESRLGSREIEVSCLGDGSSAyvIAGPHER-RgsggfiDYQEKYglsgKSSAQI 704
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 251823980 279 APATHLDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVN 327
Cdd:PRK14573 705 VFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMN 753
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
1119-1179 |
1.21e-04 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 45.94 E-value: 1.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 251823980 1119 GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTkdmtlEGD-----DLILEIE 1179
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVETDKATVEIPSPVAGTVAKLLVE-----EGDvvpvgSVIAVIE 77
|
|
| aksA |
PRK11858 |
trans-homoaconitate synthase; Reviewed |
713-799 |
2.15e-04 |
|
trans-homoaconitate synthase; Reviewed
Pssm-ID: 183341 [Multi-domain] Cd Length: 378 Bit Score: 45.17 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 713 DPSRTKYS-LEYYMGLAEElvrAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHDTSGAGVAAMLACAQAG 791
Cdd:PRK11858 138 DASRTDLDfLIEFAKAAEE---AGADRVRFCDTVGILDPFTMYELVKELVEAV-DIPIEVHCHNDFGMATANALAGIEAG 213
|
....*...
gi 251823980 792 ADVVDVAV 799
Cdd:PRK11858 214 AKQVHTTV 221
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
1105-1179 |
2.23e-04 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 45.38 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 1105 ALKDVKgqigapMP------GKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEI 1178
Cdd:PRK11854 104 AAKDVH------VPdigsdeVEVTEILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVSTGSLIMVF 177
|
.
gi 251823980 1179 E 1179
Cdd:PRK11854 178 E 178
|
|
| PDHac_trf_long |
TIGR01348 |
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model ... |
1106-1179 |
2.29e-04 |
|
pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; This model describes a subset of pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase specifically close by both phylogenetic and per cent identity (UPGMA) trees. Members of this set include two or three copies of the lipoyl-binding domain. E. coli AceF is a member of this model, while mitochondrial and some other bacterial forms belong to a separate model. [Energy metabolism, Pyruvate dehydrogenase]
Pssm-ID: 273566 [Multi-domain] Cd Length: 546 Bit Score: 45.25 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 251823980 1106 LKDVK-GQIGAPMPGKVIDIKVAAGDKVAKGQPLCVLSAMKMETVVTSPMEGTIRKVHVTKDMTLEGDDLILEIE 1179
Cdd:TIGR01348 116 VQEVTvPDIGDIEKVTVIEVLVKVGDTVSADQSLITLESDKASMEVPAPASGVVKSVKVKVGDSVPTGDLILTLS 190
|
|
| PLN02983 |
PLN02983 |
biotin carboxyl carrier protein of acetyl-CoA carboxylase |
1115-1158 |
2.99e-04 |
|
biotin carboxyl carrier protein of acetyl-CoA carboxylase
Pssm-ID: 215533 [Multi-domain] Cd Length: 274 Bit Score: 44.06 E-value: 2.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 251823980 1115 APMPGKVIDIKVaaGDKVAKGQPLCVLSAMKMETVVTSPMEGTI 1158
Cdd:PLN02983 211 SPAPGEPPFVKV--GDKVQKGQVVCIIEAMKLMNEIEADQSGTI 252
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
38-329 |
3.64e-04 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 44.70 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 38 IKKVMVANRGEI--------------AIRVFRactELGIRTVAVYSEQDTGQMHRQKADEAYLIgrglaPVQaylhiPDI 103
Cdd:PRK05294 7 IKKILIIGSGPIvigqacefdysgtqACKALR---EEGYRVVLVNSNPATIMTDPEMADATYIE-----PIT-----PEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 104 I-KV-AKENgVDAVHPGYG---------------FLSERadfaqacqdaGVRFIGPSPEVVRKMGDKVEARAIAIAAGVP 166
Cdd:PRK05294 74 VeKIiEKER-PDAILPTMGgqtalnlavelaesgVLEKY----------GVELIGAKLEAIDKAEDRELFKEAMKKIGLP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 167 VVPGTdsPISSLHEAHEFSNTYGFPIIFKAAYGgggrgM-----RVVHSYEELEENYTRayseALAAFGNGALFVEKFIE 241
Cdd:PRK05294 143 VPRSG--IAHSMEEALEVAEEIGYPVIIRPSFT-----LggtggGIAYNEEELEEIVER----GLDLSPVTEVLIEESLL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 242 KPRHIEVQILGDQYGN--ILhlyerdCSIqrrhqkvvE--------------IAPATHLDPQLRSRLTSDSVKLAKQVGY 305
Cdd:PRK05294 212 GWKEYEYEVMRDKNDNciIV------CSI--------EnidpmgvhtgdsitVAPAQTLTDKEYQMLRDASIAIIREIGV 277
|
330 340
....*....|....*....|....*.
gi 251823980 306 ENAGT-VEFLVD-KHGKHYFIEVNSR 329
Cdd:PRK05294 278 ETGGCnVQFALNpKDGRYIVIEMNPR 303
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
137-420 |
4.13e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 44.77 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 137 VRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDSpiSSLHEAHEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEe 216
Cdd:PLN02735 687 VKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIA--RSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 217 nytRAYSEALAAFGNGALFVEKFIEKPRHIEVQILGDQYGNI-------------LHLYERDCSIqrrhqkvveiaPATH 283
Cdd:PLN02735 764 ---TYLETAVEVDPERPVLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL-----------PTQT 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 284 LDPQLRSRLTSDSVKLAKQVGYENAGTVEFLVDKHGKHYFIEVNSRlqVEHT---VTEEITDVDLVHAQIhVSEGRSLPD 360
Cdd:PLN02735 830 IPSSCLATIRDWTTKLAKRLNVCGLMNCQYAITPSGEVYIIEANPR--ASRTvpfVSKAIGHPLAKYASL-VMSGKSLKD 906
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 251823980 361 LGLRQENIrINGCAIQCRVTtedPARSFQ-PDTGRIEVFRS-GEGMGIRLDNASAFQGAVIS 420
Cdd:PLN02735 907 LGFTEEVI-PAHVSVKEAVL---PFDKFQgCDVLLGPEMRStGEVMGIDYEFSKAFAKAQIA 964
|
|
| DRE_TIM_NifV |
cd07939 |
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) ... |
700-799 |
7.87e-04 |
|
Streptomyces rubellomurinus FrbC and related proteins, catalytic TIM barrel domain; FrbC (NifV) of Streptomyces rubellomurinus catalyzes the condensation of acetyl-CoA and alpha-ketoglutarate to form homocitrate and CoA, a reaction similar to one catalyzed by homocitrate synthase. The gene encoding FrbC is one of several genes required for the biosynthesis of FR900098, a potent antimalarial antibiotic. This protein is also required for assembly of the nitrogenase MoFe complex but its exact role is unknown. This family also includes the NifV proteins of Heliobacterium chlorum and Gluconacetobacter diazotrophicus, which appear to be orthologous to FrbC. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163677 [Multi-domain] Cd Length: 259 Bit Score: 42.49 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 700 VVEAAISYTGDVA----DPSRTkySLEYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFpDLPLHIHTHD 775
Cdd:cd07939 115 LVGRAKDRGLFVSvgaeDASRA--DPDFLIEFAEVAQEAGADRLRFADTVGILDPFTTYELIRRLRAAT-DLPLEFHAHN 191
|
90 100
....*....|....*....|....
gi 251823980 776 TSGAGVAAMLACAQAGADVVDVAV 799
Cdd:cd07939 192 DLGLATANTLAAVRAGATHVSVTV 215
|
|
| DRE_TIM_LeuA3 |
cd07941 |
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel ... |
757-795 |
9.37e-04 |
|
Desulfobacterium autotrophicum LeuA3 and related proteins, N-terminal catalytic TIM barrel domain; Desulfobacterium autotrophicum LeuA3 is sequence-similar to alpha-isopropylmalate synthase (LeuA) but its exact function is unknown. Members of this family have an N-terminal TIM barrel domain that belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163679 Cd Length: 273 Bit Score: 42.44 E-value: 9.37e-04
10 20 30
....*....|....*....|....*....|....*....
gi 251823980 757 VSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVV 795
Cdd:cd07941 186 VKEVRERLPGVPLGIHAHNDSGLAVANSLAAVEAGATQV 224
|
|
| YcjR |
COG1082 |
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism]; |
100-174 |
1.78e-03 |
|
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
Pssm-ID: 440699 [Multi-domain] Cd Length: 254 Bit Score: 41.54 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 100 IPDIIKVAKENGVDAVHPGYGFLSE--RADFAQACQDAGVRFIG---------PSPEVVRKMGDKVEaRAIAIAA--GVP 166
Cdd:COG1082 15 LEEALRAAAELGYDGVELAGGDLDEadLAELRAALADHGLEISSlhapglnlaPDPEVREAALERLK-RAIDLAAelGAK 93
|
90
....*....|.
gi 251823980 167 VV---PGTDSP 174
Cdd:COG1082 94 VVvvhPGSPPP 104
|
|
| PLN02746 |
PLN02746 |
hydroxymethylglutaryl-CoA lyase |
727-838 |
1.99e-03 |
|
hydroxymethylglutaryl-CoA lyase
Pssm-ID: 178347 Cd Length: 347 Bit Score: 41.70 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 727 LAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFPDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAVDSMSGMT 806
Cdd:PLN02746 202 VAKELYDMGCYEISLGDTIGVGTPGTVVPMLEAVMAVVPVDKLAVHFHDTYGQALANILVSLQMGISTVDSSVAGLGGCP 281
|
90 100 110
....*....|....*....|....*....|....*...
gi 251823980 807 SQPSMGALVACT------KGTPLDTEVPLERVFDYSEY 838
Cdd:PLN02746 282 YAKGASGNVATEdvvymlNGLGVSTNVDLGKLMAAGDF 319
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
22-330 |
2.79e-03 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 22 SAPVASPNVRRLeyKPIKKVMVANRGEIAI-----------RVFRACTELGIRTVAVYSEQDTGQMHRQKADEAYLigrg 90
Cdd:PLN02735 9 RAWSAATKAGKR--TDLKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTYI---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 91 lAPVQaylhiPDIIK--VAKENGvDAVHPGYG---------FLSERADFAQAcqdaGVRFIGPSPEVVRKMGDKVEARAI 159
Cdd:PLN02735 83 -APMT-----PELVEqvIAKERP-DALLPTMGgqtalnlavALAESGILEKY----GVELIGAKLDAIKKAEDRELFKQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 160 AIAAGVPVVPgtdSPI-SSLHEAHEFSNTYG-FPIIFKAAYGGGGRGMRVVHSYEELEENYTraysEALAAFGNGALFVE 237
Cdd:PLN02735 152 MEKIGLKTPP---SGIaTTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICK----AGLAASITSQVLVE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 238 KFIEKPRHIEVQILGDQYGNILHLyerdCSIQRRHQKVVE------IAPATHLDPQLRSRLTSDSVKLAKQVGYENAGT- 310
Cdd:PLN02735 225 KSLLGWKEYELEVMRDLADNVVII----CSIENIDPMGVHtgdsitVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSn 300
|
330 340
....*....|....*....|.
gi 251823980 311 VEFLVD-KHGKHYFIEVNSRL 330
Cdd:PLN02735 301 VQFAVNpVDGEVMIIEMNPRV 321
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
67-364 |
3.35e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 41.76 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 67 VYSEQDT---GQMHRQKA----DEAYLI--GRGLAPVQAYLHIPDIikVAKENGVDAVHpgyGFLSERADFA--QACQDA 135
Cdd:PRK02186 6 VFIESNTtgtGELLLRKAllrgFTPYFLtaNRGKYPFLDAIRVVTI--SADTSDPDRIH---RFVSSLDGVAgiMSSSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 136 gvrFIGPSPEVVRKMG-DKVEARAIAIA------------AGVPVvPGTDSpISSLHEAHEFSNTYGFPIIFKAAYGGGG 202
Cdd:PRK02186 81 ---FIEVASEVARRLGlPAANTEAIRTCrdkkrlartlrdHGIDV-PRTHA-LALRAVALDALDGLTYPVVVKPRMGSGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 203 RGMRVVHSYEELEenytrAYSEALAAFGNGALFVEKFIEKPRHiEVQILGDQYGniLHLYerdcSIQRRHQ----KVVEI 278
Cdd:PRK02186 156 VGVRLCASVAEAA-----AHCAALRRAGTRAALVQAYVEGDEY-SVETLTVARG--HQVL----GITRKHLgpppHFVEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 279 A---PATHLDPQlRSRLTSDSVKLAKQVGYE-NAGTVEFLVdKHGKHYFIEVNSRLQ--VEHTVTEEITDVDLVHAQIHV 352
Cdd:PRK02186 224 GhdfPAPLSAPQ-RERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEINPRLAggMIPVLLEEAFGVDLLDHVIDL 301
|
330
....*....|..
gi 251823980 353 SEGRSlPDLGLR 364
Cdd:PRK02186 302 HLGVA-AFADPT 312
|
|
| PLN03228 |
PLN03228 |
methylthioalkylmalate synthase; Provisional |
722-819 |
4.46e-03 |
|
methylthioalkylmalate synthase; Provisional
Pssm-ID: 178767 [Multi-domain] Cd Length: 503 Bit Score: 41.06 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 251823980 722 EYYMGLAEELVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRFP---DLPLHIHTHDTSGAGVAAMLACAQAGADVVDVA 798
Cdd:PLN03228 239 EFLCKILGEAIKAGATSVGIADTVGINMPHEFGELVTYVKANTPgidDIVFSVHCHNDLGLATANTIAGICAGARQVEVT 318
|
90 100
....*....|....*....|.
gi 251823980 799 VDSMSGMTSQPSMGALVACTK 819
Cdd:PLN03228 319 INGIGERSGNASLEEVVMALK 339
|
|
| PRK08195 |
PRK08195 |
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated |
726-799 |
9.85e-03 |
|
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,; Validated
Pssm-ID: 181282 [Multi-domain] Cd Length: 337 Bit Score: 39.43 E-value: 9.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 251823980 726 GLAEE---LVRAGTHILCIKDMAGLLKPAACTMLVSSLRDRF-PDLPLHIHTHDTSGAGVAAMLACAQAGADVVDVAV 799
Cdd:PRK08195 145 KLAEQaklMESYGAQCVYVVDSAGALLPEDVRDRVRALRAALkPDTQVGFHGHNNLGLGVANSLAAVEAGATRIDGSL 222
|
|
| |
