|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
3-899 |
0e+00 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 1634.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 3 NPFAHLAEPLdAAQPGKRFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPAR 82
Cdd:PTZ00092 14 NPFEKVLKTL-KDGGSYKYYSLNELHDPRLKKLPYSIRVLLESAVRNCDEFDVTSKDVENILNWEENSKKQIEIPFKPAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 83 VILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQ 162
Cdd:PTZ00092 93 VLLQDFTGVPAVVDLAAMRDAMKRLGGDPAKINPLVPVDLVIDHSVQVDFSRSPDALELNQEIEFERNLERFEFLKWGSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 163 AFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVMLG 242
Cdd:PTZ00092 173 AFKNLLIVPPGSGIVHQVNLEYLARVVFNKDGLLYPDSVVGTDSHTTMINGLGVLGW----------GVGGIEAEAVMLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 243 QPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPV 322
Cdd:PTZ00092 243 QPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 323 DEVSIAYLLQTGREEDKVKHIQKYLQAVGMFRDFNDtsqDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESC 402
Cdd:PTZ00092 323 DEKTLDYLKQTGRSEEKVELIEKYLKANGLFRTYAE---QIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTAC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 403 LGAKQGFKGFQVAPDRHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLS 482
Cdd:PTZ00092 400 LSAPVGFKGFGIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIKTSLS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 483 PGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLA 562
Cdd:PTZ00092 480 PGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITNNDLVAAAVLSGNRNFEGRVHPLTRANYLA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 563 SPPLVIAYAIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEK 642
Cdd:PTZ00092 560 SPPLVVAYALAGRVNIDFETEPLGSDKTGKPVFLRDIWPSREEIQALEAKYVKPEMFKEVYSNITQGNKQWNELQVPKGK 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 643 LYAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSR 722
Cdd:PTZ00092 640 LYEWDEKSTYIHNPPFFQTMELEPPPIKSIENAYCLLNLGDSITTDHISPAGNIAKNSPAAKYLMERGVERKDFNTYGAR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 723 RGNDAIMARGTFANIRLLNKFLNKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGI 802
Cdd:PTZ00092 720 RGNDEVMVRGTFANIRLINKLCGKVGPNTVHVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGSGSSRDWAAKGPYLQGV 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 803 KAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTINIPE-DLKPRMTVQIKLDTGKTFQAVMRFDTDVEL 881
Cdd:PTZ00092 800 KAVIAESFERIHRSNLVGMGILPLQFLNGENADSLGLTGKEQFSIDLNSgELKPGQDVTVKTDTGKTFDTILRIDTEVEV 879
|
890
....*....|....*...
gi 18098515 882 TYFHNGGILNYMIRKMAQ 899
Cdd:PTZ00092 880 EYFKHGGILQYVLRKLVK 897
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
17-899 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 1522.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 17 PGK--RFFNLNKLEDSRYG---RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGV 91
Cdd:PRK09277 16 GGKsyDYYSLRALEAKGLGdisRLPYSLRVLLENLLRNEDGRSVTEEDIEALAEWLPKAKPDREIPFRPARVVMQDFTGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 92 PAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIP 171
Cdd:PRK09277 96 PAVVDLAAMRDAIADLGGDPAKINPLVPVDLVIDHSVQVDYFGTPDAFEKNVELEFERNEERYQFLKWGQKAFDNFRVVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 172 PGSGIIHQVNLEYLARVVF-DQDGC--YYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVMLGQPISMV 248
Cdd:PRK09277 176 PGTGICHQVNLEYLAPVVWtREDGElvAYPDTLVGTDSHTTMINGLGVLGW----------GVGGIEAEAAMLGQPSSML 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 249 LPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIA 328
Cdd:PRK09277 246 IPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 329 YLLQTGREEDKVKHIQKYLQAVGMFRDfndTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQG 408
Cdd:PRK09277 326 YLRLTGRDEEQVALVEAYAKAQGLWRD---PLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKSAELGVQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 409 FKGFQVAPDrhndrktflysNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVV 488
Cdd:PRK09277 403 GFGLDEAEE-----------GEDYELPDGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 489 TYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVI 568
Cdd:PRK09277 472 TDYLEKAGLLPYLEALGFNLVGYGCTTCIGNSGPLPPEIEKAINDNDLVVTAVLSGNRNFEGRIHPLVKANYLASPPLVV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 569 AYAIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNP 648
Cdd:PRK09277 552 AYALAGTVDIDLEKDPLGTDKDGNPVYLKDIWPSDEEIDAVVAKAVKPEMFRKEYADVFEGDERWNAIEVPEGPLYDWDP 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 649 KSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAI 728
Cdd:PRK09277 632 DSTYIRNPPYFEGMLAEPGPVRDIKGARVLALLGDSITTDHISPAGAIKADSPAGKYLLEHGVEPKDFNSYGSRRGNHEV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 729 MARGTFANIRLLNKFLN-KQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLA 807
Cdd:PRK09277 712 MMRGTFANIRIRNEMVPgVEGGYTRHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIA 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 808 ESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTINIPEDLKPR--MTVQIKLDTG--KTFQAVMRFDTDVELTY 883
Cdd:PRK09277 792 ESFERIHRSNLVGMGVLPLQFKPGESRKTLGLDGTETFDIEGLEDLKPGatVTVVITRADGevVEFPVLCRIDTAVEVDY 871
|
890
....*....|....*.
gi 18098515 884 FHNGGILNYMIRKMAQ 899
Cdd:PRK09277 872 YRNGGILQYVLRDLLA 887
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
20-899 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 1511.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 20 RFFNLNKLEDSRYG--RLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDF 97
Cdd:COG1048 19 TYYSLPALEEAGGDisRLPYSLKILLENLLRNEDGETVTEEDIKALANWLPKARGDDEIPFRPARVLMQDFTGVPAVVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 98 AAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIPPGSGII 177
Cdd:COG1048 99 AAMRDAVARLGGDPKKINPLVPVDLVIDHSVQVDYFGTPDALEKNLELEFERNRERYQFLKWGQQAFDNFRVVPPGTGIV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 178 HQVNLEYLARVVF--DQDG--CYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVMLGQPISMVLPQVI 253
Cdd:COG1048 179 HQVNLEYLAFVVWtrEEDGetVAYPDTLVGTDSHTTMINGLGVLGW----------GVGGIEAEAAMLGQPVSMLIPEVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 254 GYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQT 333
Cdd:COG1048 249 GVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 334 GREEDKVKHIQKYLQAVGMFRDfnDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGfkgfq 413
Cdd:COG1048 329 GRSEEQIELVEAYAKAQGLWRD--PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVG----- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 414 vapDRHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLR 493
Cdd:COG1048 402 ---EELDKPVRVEVDGEEFELGHGAVVIAAITSCTNTSNPSVMIAAGLLAKKAVEKGLKVKPWVKTSLAPGSKVVTDYLE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 494 ESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIA 573
Cdd:COG1048 479 RAGLLPYLEALGFNVVGYGCTTCIGNSGPLPPEISEAIEENDLVVAAVLSGNRNFEGRIHPDVKANFLASPPLVVAYALA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 574 GTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYI 653
Cdd:COG1048 559 GTVDIDLTTDPLGTDKDGKPVYLKDIWPSGEEIPAAVFKAVTPEMFRARYADVFDGDERWQALEVPAGELYDWDPDSTYI 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 654 KSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGT 733
Cdd:COG1048 639 RRPPFFEGLQLEPEPFKDIKGARVLAKLGDSITTDHISPAGAIKADSPAGRYLLEHGVEPKDFNSYGSRRGNHEVMMRGT 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 734 FANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYER 812
Cdd:COG1048 719 FANIRIKNLLApGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFER 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 813 IHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTI-NIPEDLKPRMTVQIKLD----TGKTFQAVMRFDTDVELTYFHNG 887
Cdd:COG1048 799 IHRSNLVGMGVLPLQFPEGESAESLGLTGDETFDIeGLDEGLAPGKTVTVTATradgSTEEFPVLHRIDTPVEVEYYRAG 878
|
890
....*....|..
gi 18098515 888 GILNYMIRKMAQ 899
Cdd:COG1048 879 GILQYVLRQLLA 890
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
2-899 |
0e+00 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 1382.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 2 KNPFAHLAEPLDAAQPGK--RFFNLNKLEDSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFK 79
Cdd:PLN00070 42 ENPFKGILTSLPKPGGGEfgKYYSLPALNDPRIDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWENTSPKQVEIPFK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 80 PARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKW 159
Cdd:PLN00070 122 PARVLLQDFTGVPAVVDLACMRDAMNNLGGDPNKINPLVPVDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 160 GSQAFCNMRIIPPGSGIIHQVNLEYLARVVFDQDGCYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAV 239
Cdd:PLN00070 202 GSTAFQNMLVVPPGSGIVHQVNLEYLGRVVFNTDGILYPDSVVGTDSHTTMIDGLGVAGW----------GVGGIEAEAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 240 MLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAF 319
Cdd:PLN00070 272 MLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 320 FPVDEVSIAYLLQTGREEDKVKHIQKYLQAVGMFRDFNDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDF 399
Cdd:PLN00070 352 FPVDHVTLQYLKLTGRSDETVAMIEAYLRANKMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADW 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 400 ESCLGAKQGFKGFQVAPDRHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKT 479
Cdd:PLN00070 432 HSCLDNKVGFKGFAVPKEAQSKVAKFSFHGQPAELRHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACELGLEVKPWIKT 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 480 SLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRAN 559
Cdd:PLN00070 512 SLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITENDIVAAAVLSGNRNFEGRVHPLTRAN 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 560 YLASPPLVIAYAIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAP 639
Cdd:PLN00070 592 YLASPPLVVAYALAGTVDIDFEKEPIGTGKDGKDVFFRDIWPSNEEVAEVVQSSVLPDMFKSTYEAITKGNPMWNQLSVP 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 640 SEKLYAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSY 719
Cdd:PLN00070 672 SGTLYSWDPKSTYIHEPPYFKNMTMSPPGPHGVKDAYCLLNFGDSITTDHISPAGSIHKDSPAAKYLMERGVDRKDFNSY 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 720 GSRRGNDAIMARGTFANIRLLNKFLNKQ-APQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPF 798
Cdd:PLN00070 752 GSRRGNDEIMARGTFANIRIVNKLLKGEvGPKTVHIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPM 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 799 LLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTINIP---EDLKPRMTVQIKLDTGKTFQAVMRF 875
Cdd:PLN00070 832 LLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLGLTGHERYTIDLPsniSEIKPGQDVTVTTDNGKSFTCTLRF 911
|
890 900
....*....|....*....|....
gi 18098515 876 DTDVELTYFHNGGILNYMIRKMAQ 899
Cdd:PLN00070 912 DTEVELAYFDHGGILPYVIRNLIK 935
|
|
| aconitase_1 |
TIGR01341 |
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate ... |
21-897 |
0e+00 |
|
aconitate hydratase 1; This model represents one form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It is found in bacteria, archaea, and eukaryotic cytosol. It has been shown to act also as an iron-responsive element binding protein in animals and may have the same role in other eukaryotes. [Energy metabolism, TCA cycle]
Pssm-ID: 273562 [Multi-domain] Cd Length: 876 Bit Score: 1323.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 21 FFNLNKLEDS--RYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDFA 98
Cdd:TIGR01341 5 YYSLKALEESggKISKLPYSIRILLESVLRNLDGFSITEEDIENILKWKIGEVADTEIAFKPARVVMQDFTGVPAVVDLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 99 AMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAFCNMRIIPPGSGIIH 178
Cdd:TIGR01341 85 AMREAMKNLGGDPKKINPLVPVDLVIDHSVQVDYYGTEYALEFNMELEFERNLERYQFLKWAQKAFRNFRVVPPGTGIIH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 179 QVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVMLGQPISMVLPQVIG 254
Cdd:TIGR01341 165 QVNLEYLATVVFkaevDGELTAYPDSLVGTDSHTTMINGLGVLGW----------GVGGIEAEAAMLGQPYYMNVPEVIG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 255 YKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLLQTG 334
Cdd:TIGR01341 235 VKLTGKLQEGVTATDLVLTVTQMLRKKGVVGKFVEFFGPGLSELSLADRATIANMAPEYGATCGFFPIDDVTLQYLRLTG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 335 REEDKVKHIQKYLQAVGMFRDFndtSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESCLGAKQGFKGFQV 414
Cdd:TIGR01341 315 RDGDHVELVEKYARAQGLFYDD---SEEPRYTDVVELDLSDVEPSVAGPKRPQDRIPLREVKAKFSKELEKNGGDKGFTL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 415 apdrHNDRKTFLYSNSEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRE 494
Cdd:TIGR01341 392 ----RKEPLKKKVNGQNKQLEDGAVVIAAITSCTNTSNPSVMLGAGLLAKKAVELGLKVPPYVKTSLAPGSKVVTDYLAE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 495 SGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAG 574
Cdd:TIGR01341 468 SGLLPYLEELGFNLVGYGCTTCIGNSGPLPKYVEEAIKKNDLEVYAVLSGNRNFEGRIHPLVKGNYLASPPLVVAYALAG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 575 TVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPSEKLYAWNPKSTYIK 654
Cdd:TIGR01341 548 NIDINLYTEPIGTDKDGKPVYLRDIWPSNKEIAAYVNMAVKPEMFKKEYENIFEGNERWNSIKTPSGDTYSWDEKSTYIR 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 655 SPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTF 734
Cdd:TIGR01341 628 LPPFFEEMKQDPEEVEDIKGARILLLLGDSITTDHISPAGSITKDSPAGKYLQERGVSRRDFNSYGSRRGNHEVMMRGTF 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 735 ANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERI 813
Cdd:TIGR01341 708 ANIRIKNLMVkGKEGGYTVHFPDGKVASVYDAAMQYKKEGTPLVVIAGKEYGSGSSRDWAAKGTKLLGVKAVIAESFERI 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 814 HRSNLVGMGVIPLEYLPGETADSLGLTGREryTINIP--EDLKPRMTVQIKLDTGK----TFQAVMRFDTDVELTYFHNG 887
Cdd:TIGR01341 788 HRSNLVGMGVIPLQFPQGEDAETLGLTGDE--TIDIDgiKDLKPGKEVTVTFTNSKgekiTFKCVLRIDTEVELDYYKHG 865
|
890
....*....|
gi 18098515 888 GILNYMIRKM 897
Cdd:TIGR01341 866 GILQYVLRKF 875
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
11-899 |
0e+00 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 1307.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 11 PLDAAQPGK---RFFNLNKLE---DSRYGRLPFSIRVLLEAAVRNCDEFLVKKNDIENILNWNVMQHKNIEVPFKPARVI 84
Cdd:PRK12881 8 TLKEFDVGGktyKFYSLPALGkelGGDLARLPVSLRVLLENLLRNEDGKKVTEEHLEALANWLPERKSDDEIPFVPARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 85 LQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGSQAF 164
Cdd:PRK12881 88 MQDFTGVPALVDLAAMRDAAAEAGGDPAKINPLVPVDLVVDHSVAVDYFGQKDALDLNMKIEFQRNAERYQFLKWGMQAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 165 CNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVM 240
Cdd:PRK12881 168 DNFRVVPPGTGIMHQVNLEYLARVVHtkedDGDTVAYPDTLVGTDSHTTMINGIGVLGW----------GVGGIEAEAVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 241 LGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFF 320
Cdd:PRK12881 238 LGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 321 PVDEVSIAYLLQTGREEDKVKHIQKYLQAVGMFRDfndTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFE 400
Cdd:PRK12881 318 PVDEQTLDYLRLTGRTEAQIALVEAYAKAQGLWGD---PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 401 SCLGAKQGFKGFQVAPDRHNDrktflysnseFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYIKTS 480
Cdd:PRK12881 395 DLFSKPVAENGFAKKAQTSNG----------VDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVKPWVKTS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 481 LSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANY 560
Cdd:PRK12881 465 LAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQAITKNDLVAAAVLSGNRNFEGRIHPNIKANF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 561 LASPPLVIAYAIAGTVRIDFEKEPLGVNAQGRQVFLKDIWPTRDEIQAVERQHVIPGMFKEVYQKIETVNKSWNALAAPS 640
Cdd:PRK12881 545 LASPPLVVAYALAGTVRRDLMTEPLGKGKDGRPVYLKDIWPSSAEIDALVAFAVDPEDFRKNYAEVFKGSELWAAIEAPD 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 641 EKLYAWNPKSTYIKSPPFFESLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYG 720
Cdd:PRK12881 625 GPLYDWDPKSTYIRRPPFFDFSMGPAASIATVKGARPLAVLGDSITTDHISPAGAIKADSPAGKYLKENGVPKADFNSYG 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 721 SRRGNDAIMARGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFL 799
Cdd:PRK12881 705 SRRGNHEVMMRGTFANVRIKNLMIpGKEGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRL 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 800 LGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRERYTIN-IPEDLKPRM--TVQIKLDTGKT--FQAVMR 874
Cdd:PRK12881 785 LGVKAVIAESFERIHRSNLVGMGVLPLQFKGGDSRQSLGLTGGETFDIEgLPGEIKPRQdvTLVIHRADGSTerVPVLCR 864
|
890 900
....*....|....*....|....*
gi 18098515 875 FDTDVELTYFHNGGILNYMIRKMAQ 899
Cdd:PRK12881 865 IDTPIEVDYYKAGGILPYVLRQLLA 889
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
82-576 |
0e+00 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 820.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNKERFEFLKWGS 161
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAMRDAVKRLGGDPEKINPLIPVDLVIDHSVQVDFYGTADALAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 162 QAFCNMRIIPPGSGIIHQVNLEYLARVVF----DQDGCYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAE 237
Cdd:cd01586 81 KAFKNLRVVPPGTGIIHQVNLEYLARVVFtseeDGDGVAYPDSVVGTDSHTTMINGLGVLGW----------GVGGIEAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 238 AVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATA 317
Cdd:cd01586 151 AVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 318 AFFPVDevsiayllqtgreedkvkhiqkylqavgmfrdfndtsqdpdfTQVVELDLKTVVPCCSGPKRPQDKVAVsemkk 397
Cdd:cd01586 231 GFFPVD------------------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPL----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 398 dfesclgakqgfkgfqvapdrhndrktflysnseftlaHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVKPYI 477
Cdd:cd01586 264 --------------------------------------HGSVVIAAITSCTNTSNPSVMLAAGLLAKKAVELGLKVKPYV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 478 KTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTR 557
Cdd:cd01586 306 KTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEAIKENDLVVAAVLSGNRNFEGRIHPLVR 385
|
490
....*....|....*....
gi 18098515 558 ANYLASPPLVIAYAIAGTV 576
Cdd:cd01586 386 ANYLASPPLVVAYALAGTV 404
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
61-574 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 662.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 61 ENILNWNVMQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGNPEKINPVCPADLVIDHSiqvdfnrrADSLQ 140
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHA--------PDALD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 141 KNQDLEFERNKERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYlarvvfdqdGCYYPD-SLVGTDSHTTMIDGLGVLGW 219
Cdd:pfam00330 73 KNIEDEISRNKEQYDFLEWNAKKF-GIRFVPPGQGIVHQVGLEY---------GLALPGmTIVGTDSHTTTHGGLGALAF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 220 eafpcsavtaGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLS 299
Cdd:pfam00330 143 ----------GVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 300 IADRATIANMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVkhIQKYLQAVGMFRDFNDtsQDPDFTQVVELDLKTVVPC 379
Cdd:pfam00330 213 MEGRATICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPK--GEAYDKAVAWKTLASD--PGAEYDKVVEIDLSTIEPM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 380 CSGPKRPQDKVAVSEMKKD-FESCLGAKQGFKGFQVAPDRHNDRktflysnseftLAHGSVVIAAITSCTNTSNPSVMLG 458
Cdd:pfam00330 289 VTGPTRPQDAVPLSELVPDpFADAVKRKAAERALEYMGLGPGTP-----------LSDGKVDIAFIGSCTNSSIEDLRAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 459 AGLLaKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEpvveaitqGDlva 538
Cdd:pfam00330 358 AGLL-KKAVEKGLKVAPGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLPP--------GE--- 425
|
490 500 510
....*....|....*....|....*....|....*.
gi 18098515 539 VGVLSGNRNFEGRVHPNTRAnYLASPPLVIAYAIAG 574
Cdd:pfam00330 426 RCVSSSNRNFEGRQGPGGRT-HLASPALVAAAAIAG 460
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
680-847 |
6.80e-112 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 340.02 E-value: 6.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 680 NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKFLNKQAPQ-TVHLPSGE 758
Cdd:cd01580 1 LLGDSVTTDHISPAGSIAKDSPAGKYLAERGVKPRDFNSYGSRRGNDEVMMRGTFANIRLRNKLVPGTEGGtTHHPPTGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 759 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLG 838
Cdd:cd01580 81 VMSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGENADSLG 160
|
....*....
gi 18098515 839 LTGRERYTI 847
Cdd:cd01580 161 LTGEETYDI 169
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
82-576 |
2.11e-103 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 326.38 E-value: 2.11e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAVVDFAAMRDAVKklggnpekINPVCPADLVIDHSIQvdfnrradslqknqdLEFERNKERFEFLKWgS 161
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALGK--------VADPSQIACVHDHAVQ---------------LEKPVNNEGHKFLSF-F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 162 QAFCNMRIIPPGSGIIHQVNLEYLArvvfdqdgcYYPDSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGIEAEAVML 241
Cdd:cd01351 57 AALQGIAFYRPGVGIIHQIMVENLA---------LPGDLLVGSDSHTTSYGGLGAIST----------GAGGGDVAFVMA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 242 GQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFP 321
Cdd:cd01351 118 GGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 322 VDEVSIAYLLQTGREEDKVKhiqkylqaVGMFRDFNDTSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKdfes 401
Cdd:cd01351 198 EDKTTLKWLEATGRPLLKNL--------WLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG---- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 402 clgakqgfkgfqvapdrhndrktflysnseftlahGSVVIAAITSCTNtSNPSVMLGAGLLAKKAVeaglsVKPYIKTSL 481
Cdd:cd01351 266 -----------------------------------TKIDQVLIGSCTN-NRYSDMLAAAKLLKGAK-----VAPGVRLIV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 482 SPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPepvveaitqgDLVAVGVLSGNRNFEGRVHPNTRANYL 561
Cdd:cd01351 305 TPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLV----------ADGEVGVSSGNRNFPGRLGTYERHVYL 374
|
490
....*....|....*
gi 18098515 562 ASPPLVIAYAIAGTV 576
Cdd:cd01351 375 ASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
75-899 |
3.07e-90 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 299.75 E-value: 3.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 75 EVPFKPARVILQDFTGVPAVVDFAAM-RDAVK-KLggnpekinpvcpADLVIDHS-IQVDFnrradslqknqdlefeRNK 151
Cdd:PRK07229 24 EIAIRIDQTLTQDATGTMAYLQFEAMgLDRVKtEL------------SVQYVDHNlLQADF----------------ENA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 152 ERFEFLKWGSQAFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLgweafpcsAVtaG 230
Cdd:PRK07229 76 DDHRFLQSVAAKY-GIYFSKPGNGICHQVHLERFAF----------PgKTLLGSDSHTPTAGGLGML--------AI--G 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 231 VGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV---VGKFVEFFGPGVAQLSIADRATIA 307
Cdd:PRK07229 135 AGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILEL---LRRLTVkggVGKIIEYFGPGVATLSVPERATIT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 308 NMCPEYGATAAFFPVDEVSIAYLLQTGREEDKVKhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKR 385
Cdd:PRK07229 212 NMGAELGATTSIFPSDERTREFLKAQGREDDWVE-----LLA------------DPDaeYDEVIEIDLSELEPLIAGPHS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 386 PQDKVAVSEMKkdfesclGAKqgfkgfqvapdrhndrktflysnseftlahgsVVIAAITSCTNTSNPSVMLGAGLLAKK 465
Cdd:PRK07229 275 PDNVVPVSEVA-------GIK--------------------------------VDQVLIGSCTNSSYEDLMRAASILKGK 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 466 AVEAGLSvkpyikTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGplpEPVVEAITqgdlvavgVLSGN 545
Cdd:PRK07229 316 KVHPKVS------LVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNVS--------LRTFN 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 546 RNFEGRV-HPNTRAnYLASPPLVIAYAIAGtvRIDfekEPlgvnaqgRQVFLKDI-WPtrdEIQAVERQHVIPGMF---K 620
Cdd:PRK07229 379 RNFPGRSgTKDAQV-YLASPETAAASALTG--VIT---DP-------RTLALENGeYP---KLEEPEGFAVDDAGIiapA 442
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 621 EVYQKIETVnkswnalaapseklyawnpKSTYIKSPPffesltlDLQPPKSIVDAYVLLNLGDSVTTDHISPAGniarns 700
Cdd:PRK07229 443 EDGSDVEVV-------------------RGPNIKPLP-------LLEPLPDLLEGKVLLKVGDNITTDHIMPAG------ 490
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 701 paARYLtnrgltprefnSYgsrRGN-DAImARGTFanIRLLNKFlnkqapqtvhlpsgetldvfdaAERYQQAGlPLIVL 779
Cdd:PRK07229 491 --AKWL-----------PY---RSNiPNI-SEFVF--EGVDNTF----------------------PERAKEQG-GGIVV 528
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 780 AGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLgltgRERYTINIP--EDLKPRM 857
Cdd:PRK07229 529 GGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKANLINFGILPLTFADPADYDKI----EEGDVLEIEdlREFLPGG 604
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 18098515 858 TVQIKLDT-GKTFQAVMRFdTDVELTYFHNGGILNYMIRKMAQ 899
Cdd:PRK07229 605 PLTVVNVTkDEEIEVRHTL-SERQIEILLAGGALNLIKKKLAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
82-575 |
5.45e-54 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 193.43 E-value: 5.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAVVDFAAmrdavkklGGNPEkinPVCPADLVIDHSIQVdfnrradSLQKNQDLEF--ERNKERFEFLKW 159
Cdd:cd01584 1 RVAMQDATAQMALLQFMS--------SGLPK---VAVPSTIHCDHLIEA-------QVGGEKDLKRakDINKEVYDFLAS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 160 GSQAFcNMRIIPPGSGIIHQVNLEYLArvvfdqdgcyYPDSL-VGTDSHTTMIDGLGvlgweafpcsAVTAGVGGIEAEA 238
Cdd:cd01584 63 AGAKY-GIGFWKPGSGIIHQIVLENYA----------FPGLLmIGTDSHTPNAGGLG----------GIAIGVGGADAVD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 239 VMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAA 318
Cdd:cd01584 122 VMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 319 FFPVDEVSIAYLLQTGREEdkvkhIQKYLQAVGMFRDFNDTSQDPDftQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKD 398
Cdd:cd01584 202 VFPYNERMKKYLKATGRAE-----IADLADEFKDDLLVADEGAEYD--QLIEINLSELEPHINGPFTPDLATPVSKFKEV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 399 FEsclgaKQGFkgfqvaPDRhndrktflysnseftlahgsVVIAAITSCTNTSNPSvMLGAGLLAKKAVEAGLSVKpyIK 478
Cdd:cd01584 275 AE-----KNGW------PLD--------------------LRVGLIGSCTNSSYED-MGRAASIAKQALAHGLKCK--SI 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 479 TSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPlpepvvEAITQGDLVAVgVLSGNRNFEGR--VHPNT 556
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDR------KDIKKGEKNTI-VTSYNRNFTGRndANPAT 393
|
490
....*....|....*....
gi 18098515 557 RAnYLASPPLVIAYAIAGT 575
Cdd:cd01584 394 HA-FVASPEIVTAMAIAGT 411
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
702-831 |
6.58e-53 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 180.25 E-value: 6.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 702 AARYLTNRGLTPREFNSYGSRRGNDAIMARGTFANIRLLNKFL-NKQAPQTVHLPSGETLDVFDAAERYQQAGLPLIVLA 780
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFeGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18098515 781 GKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPG 831
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
84-576 |
1.29e-51 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 185.73 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 84 ILQDFTGVPAVVDFAAMrdavkklgGNPEKINPVCPAdlVIDHS-IQVDFnrradslqknqdlefeRNKERFEFLKWGSQ 162
Cdd:cd01585 4 LTQDATGTMAYLQFEAM--------GVDRVRTELSVS--YVDHNtLQTDF----------------ENADDHRFLQTVAA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 163 AFcNMRIIPPGSGIIHQVNLEYLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGweafpcsavtAGVGGIEAEAVML 241
Cdd:cd01585 58 RY-GIYFSRPGNGICHQVHLERFAV----------PgKTLLGSDSHTPTAGGLGMLA----------IGAGGLDVALAMA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 242 GQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFP 321
Cdd:cd01585 117 GEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 322 VDEVSIAYLLQTGREEdkvkhiqkylqavgmfrDFNDTSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEMkkdf 399
Cdd:cd01585 197 SDERTREFLAAQGRED-----------------DWVELAADADaeYDEEIEIDLSELEPLIARPHSPDNVVPVREV---- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 400 esclgakQGFKGFQVapdrhndrktflysnseftlahgsvviaAITSCTNTSNPSVMLGAGLLAKKAVEAGLSVkpyikt 479
Cdd:cd01585 256 -------AGIKVDQV----------------------------AIGSCTNSSYEDLMTVAAILKGRRVHPHVSM------ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 480 SLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPvveaitqgdlvAVGVLSGNRNFEGRVHPNTRAN 559
Cdd:cd01585 295 VVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTG-----------GVSVRTFNRNFEGRSGTKDDLV 363
|
490
....*....|....*..
gi 18098515 560 YLASPPLVIAYAIAGTV 576
Cdd:cd01585 364 YLASPEVAAAAALTGVI 380
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
82-576 |
1.10e-45 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 168.91 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNKERF--EFLKW 159
Cdd:cd01583 1 LHLVHDVTSPQA---FEGLREAGREKVWDPEKIV------AVFDHNVPTP-----DIKAAEQVKTLRKFAKEFgiNFFDV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 160 GSQafcnmriippgsGIIHQVNLE-YLARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLgweAFpcsavtaGVGGIEAE 237
Cdd:cd01583 67 GRQ------------GICHVILPEkGLTL----------PgMTIVGGDSHTCTHGAFGAF---AT-------GIGTTDVA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 238 AVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATA 317
Cdd:cd01583 115 HVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 318 AFFPVDEVSIAYLlqTGREEDKVKHIQKylqavgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVSEM 395
Cdd:cd01583 195 GIVAPDETTFEYL--KGRGKAYWKELKS----------------DEDaeYDKVVEIDASELEPQVAWPHSPDNVVPVSEV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 396 KKdfesclgakqgfkgfqVAPDRhndrktflysnseftlahgsVVIAaitSCTNTSNPSVMLGAGLLAKKaveaglSVKP 475
Cdd:cd01583 257 EG----------------IKIDQ--------------------VFIG---SCTNGRLEDLRAAAEILKGR------KVAD 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 476 YIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEPVVEAITQgdlvavgvlsgNRNFEGRVHP 554
Cdd:cd01583 292 GVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGVLAPGERCVSTS-----------NRNFKGRMGS 360
|
490 500
....*....|....*....|..
gi 18098515 555 NTRANYLASPPLVIAYAIAGTV 576
Cdd:cd01583 361 PGARIYLASPATAAASAITGEI 382
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
82-576 |
3.19e-42 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 159.81 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAvvdFAAMRdavkKLGG----NPEKInpVcpadLVIDHSIQVDfnrraDSLQKNQDLEFERNKERFefl 157
Cdd:COG0065 30 LHLVHDVTSPQA---FEGLR----EAGGrkvwDPDRI--V----AVFDHNVPTK-----DPKSAEQVKTLREFAKEF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 158 kwgsqafcNMRIIPPGS-GIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGVLGWeafpcsavtaGVGGI 234
Cdd:COG0065 89 --------GITFFDVGDpGICHVVLPEQgLVL----------PgMTIVGGDSHTCTHGAFGAFAF----------GIGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 235 EAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYG 314
Cdd:COG0065 141 DVAHVLATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 315 ATAAFFPVDEVSIAYLLQTGREEDKVkhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAV 392
Cdd:COG0065 221 AKAGIIAPDETTFEYLKGRPFAPWRT------LKS------------DEDavYDKEVEIDASDLEPQVAWPHSPDNVVPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 393 SEMKKdfesclgakqgfkgfqVAPDRhndrktflysnseftlahgsvviAAITSCTNtsnpsvmlgaG----LLAKKAVE 468
Cdd:COG0065 283 SELEG----------------IKIDQ-----------------------VFIGSCTN----------GriedLRAAAEIL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 469 AGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDlvaVGVLSGNRN 547
Cdd:COG0065 314 KGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGmNMGVLAP--------GE---RCASTSNRN 382
|
490 500 510
....*....|....*....|....*....|
gi 18098515 548 FEGRV-HPNTRAnYLASPPLVIAYAIAGTV 576
Cdd:COG0065 383 FEGRMgSPGSRT-YLASPATAAASAIAGRI 411
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
83-574 |
4.19e-32 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 129.91 E-value: 4.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 83 VILQDFTGVPAVVDFaamrdavKKLGG----NPEKINpvcpadLVIDHSIQVDfNRRADSLQKnqdleFERnkerfEFLK 158
Cdd:PRK00402 31 VMAHDITGPLAIKEF-------EKIGGdkvfDPSKIV------IVFDHFVPAK-DIKSAEQQK-----ILR-----EFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 159 wgSQAFCNMRIIppGSGIIHQVNLEY-LARvvfdqdgcyyP-DSLVGTDSHTTMIDGLGvlgweAFpcsavTAGVGGIEA 236
Cdd:PRK00402 87 --EQGIPNFFDV--GEGICHQVLPEKgLVR----------PgDVVVGADSHTCTYGALG-----AF-----ATGMGSTDM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 237 EAVM-LGQpISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGVVG---KFVEFFGPGVAQLSIADRATIANMCPE 312
Cdd:PRK00402 143 AAAMaTGK-TWFKVPETIKVVLEGKLPPGVTAKDVILHI---IGDIGVDGatyKALEFTGETIEALSMDERMTLANMAIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 313 YGATAAFFPVDEVSIAYLLQTGREEDKVkhiqkyLQAvgmfrdfndtsqDPD--FTQVVELDLKTVVPCCSGPKRPQDKV 390
Cdd:PRK00402 219 AGAKAGIFAPDEKTLEYLKERAGRDYKP------WKS------------DEDaeYEEVYEIDLSKLEPQVAAPHLPDNVK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 391 AVSEMkkdfesclgakqgfkgfqvapdrhndrktflysnseftlAHGSVVIAAITSCTNtsnpsvmlgaGLLAKKAVEA- 469
Cdd:PRK00402 281 PVSEV---------------------------------------EGTKVDQVFIGSCTN----------GRLEDLRIAAe 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 470 ---GLSVKPYIKTSLSPGSGVVtyYLR--ESGVMPYLSQLGFdVVGY-GCMTCIGNS-GPLPEpvveaitqGDlvaVGVL 542
Cdd:PRK00402 312 ilkGRKVAPGVRLIVIPASQKI--YLQalKEGLIEIFVDAGA-VVSTpTCGPCLGGHmGVLAP--------GE---VCLS 377
|
490 500 510
....*....|....*....|....*....|...
gi 18098515 543 SGNRNFEGRV-HPNTRAnYLASPPLVIAYAIAG 574
Cdd:PRK00402 378 TTNRNFKGRMgSPESEV-YLASPAVAAASAVTG 409
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
82-574 |
2.14e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 120.01 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 82 RVILQDFTGVPAvvdFAAMRDAVKKLGgNPEKinpvcpADLVIDHSIQVDFNRRA---DSLQKNQDLEFERNKERFeflk 158
Cdd:PRK12466 30 RHLLNEYTSPQA---FSGLRARGRTVR-RPDL------TLAVVDHVVPTRPGRDRgitDPGGALQVDYLRENCADF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 159 wGSQAFcnmRIIPPGSGIIHqvnleylarVVFDQDGCYYPDSLVGT-DSHTTMIDGLGVLGWeafpcsavtaGVGGIEAE 237
Cdd:PRK12466 96 -GIRLF---DVDDPRQGIVH---------VVAPELGLTLPGMVIVCgDSHTTTYGALGALAF----------GIGTSEVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 238 AVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATA 317
Cdd:PRK12466 153 HVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 318 AFFPVDEVSIAYLlqTGREED-KVKHIQkylQAVGMFRDFndtSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVS- 393
Cdd:PRK12466 233 GLIAPDETTFDYL--RGRPRApKGALWD---AALAYWRTL---RSDADavFDREVEIDAADIAPQVTWGTSPDQAVPITg 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 394 -----EMKKDFESCLGAKQGFKGFQVAPDRHndrktflysnseftLAHGSVVIAAITSCTNtsnpsvmlgaG----LLAK 464
Cdd:PRK12466 305 rvpdpAAEADPARRAAMERALDYMGLTPGTP--------------LAGIPIDRVFIGSCTN----------GriedLRAA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 465 KAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIGnsgplpepvveaiTQGDLVAVG---V 541
Cdd:PRK12466 361 AAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLA-------------MNDDVLAPGercA 427
|
490 500 510
....*....|....*....|....*....|...
gi 18098515 542 LSGNRNFEGRVHPNTRAnYLASPPLVIAYAIAG 574
Cdd:PRK12466 428 STTNRNFEGRQGPGART-HLMSPAMVAAAAVAG 459
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
79-574 |
1.46e-26 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 113.32 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 79 KPARVILQDFTGVPAvvdFAAMRDAVKKLGGNPEKINpvcpadLVIDHSIQVDFNRRAdslqknqdlefERNKERFEFLK 158
Cdd:TIGR02086 25 EVDLAMTHDGTGPLA---IKALRELGVARVWDPEKIV------IAFDHNVPPPTVEAA-----------EMQKEIREFAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 159 wgsqafcNMRI--IPPGSGIIHQVnleyLARVVFDQDGcyypDSLVGTDSHTTMIDGLGVLGweafpcsavtAGVGGIE- 235
Cdd:TIGR02086 85 -------RHGIknFDVGEGICHQI----LAEEGYALPG----MVVVGGDSHTCTSGAFGAFA----------TGMGATDm 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 236 AEAVMLGQPISMVlPQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGA 315
Cdd:TIGR02086 140 AIALATGKTWIKV-PETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 316 TAAFFPVDEVSIAYLLQTGREEdkvkhiqkylqavgmfrdFNDTSQDPD--FTQVVELDLKTVVPCCSGPKRPQDKVAVS 393
Cdd:TIGR02086 219 KAGIIEPDEETYEYLKKRRGLE------------------FRILVPDPGanYYKEIEIDLSDLEPQVAVPHSVDNVKPVS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 394 EMkkdfesclgakQGFKGFQVapdrhndrktflysnseFtlahgsvviaaITSCTNTSNPSVMLGAGLLAkkaveaGLSV 473
Cdd:TIGR02086 281 DV-----------EGTEIDQV-----------------F-----------IGSCTNGRLEDLRIAAEILK------GRRV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 474 KPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDVVGYGCMTCIG-NSGPLPEpvveaitqGDLVavgVLSGNRNFEGRV 552
Cdd:TIGR02086 316 HPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGaHMGVLGD--------GEVC---LSTTNRNFKGRM 384
|
490 500
....*....|....*....|...
gi 18098515 553 -HPNTRAnYLASPPLVIAYAIAG 574
Cdd:TIGR02086 385 gSPNAEI-YLASPATAAASAVEG 406
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
110-576 |
7.74e-25 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 107.31 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 110 NPEKInpVCpadlVIDHSIQvdfNRRADSLQKNQDLEFERNKERFEFLkwgsqafcnmriiPPGSGIIHQVNLEylarvv 189
Cdd:cd01582 25 NPDQI--VM----TLDHDVQ---NKSEKNLKKYKNIESFAKKHGIDFY-------------PAGRGIGHQIMIE------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 190 fdqDGCYYPDSL-VGTDSHTTMIDGLGVLGweafpCSAVTAGVGGIEAEAVMLGQpismvLPQVIGYKLMGKPHPLVTST 268
Cdd:cd01582 77 ---EGYAFPGTLaVASDSHSNMYGGVGCLG-----TPIVRTDAAAIWATGQTWWQ-----IPPVAKVELKGQLPKGVTGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 269 DIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDevsiayllqtgreedkVKHIQkylq 348
Cdd:cd01582 144 DVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD----------------AKHLI---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 349 avgmfrdfndtsqdpdftqvveLDLKTVVPCCSGPkrpqDKVAVSEMKKDFEsclgaKQGFKgfqvapdrhndrktflys 428
Cdd:cd01582 204 ----------------------LDLSTLSPYVSGP----NSVKVSTPLKELE-----AQNIK------------------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 429 nseftlahgsVVIAAITSCTNTSNPSVMLGAGLL-AKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFD 507
Cdd:cd01582 235 ----------INKAYLVSCTNSRASDIAAAADVVkGKKEKNGKIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGAT 304
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18098515 508 VVGYGCMTCIGNSGPLPEPvveaitqGDlvaVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTV 576
Cdd:cd01582 305 PLPAGCGPCIGLGQGLLEP-------GE---VGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
772-847 |
1.08e-20 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 87.14 E-value: 1.08e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18098515 772 AGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGEtaDSLGLTGRERYTI 847
Cdd:cd00404 13 PAGPGVVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPE--DYLKLHTGDELDI 86
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
681-828 |
9.09e-20 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 85.57 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 681 LGDSVTTDHISPAGniarnspaARYLTNRgltprefnsygsrrgndaimargtfANIRLLNKFlnkqapqtvhlpsgeTL 760
Cdd:cd01579 2 VGDNITTDHIMPAG--------AKVLPLR-------------------------SNIPAISEF---------------VF 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 761 DVFDA--AERYQQAGlPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY 828
Cdd:cd01579 34 HRVDPtfAERAKAAG-PGFIVGGENYGQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTF 102
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
205-576 |
4.85e-17 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 84.79 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 205 DSHTTMIDGLGVLgweAFpcsavtaGVGGIEAEAVMLGQPISMVLPQVIGYKLMGKPHPLVTSTDIVLTItkhLRQVGV- 283
Cdd:PRK05478 128 DSHTSTHGAFGAL---AF-------GIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAI---IGKIGTa 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 284 --VGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIAYLlqTGREedkvkHIQK---YLQAVGMFRDFNd 358
Cdd:PRK05478 195 ggTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYL--KGRP-----FAPKgedWDKAVAYWKTLK- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 359 TSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSEMKKDFESclgakqgfkgFQVAPDRHNDRKTFLYSNseftLAHG- 437
Cdd:PRK05478 267 SDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPED----------FADPVKRASAERALAYMG----LKPGt 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 438 -----SVVIAAITSCTNtsnpsvmlgaG----LLAKKAVEAGLSVKPYIKTSLSPGSGVVTYYLRESGVMPYLSQLGFDV 508
Cdd:PRK05478 333 pitdiKIDKVFIGSCTN----------SriedLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEW 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18098515 509 VGYGCMTCIG-NSGPLPEpvveaitqGDLVAVgvlSGNRNFEGRVHPNTRaNYLASPPLVIAYAIAGTV 576
Cdd:PRK05478 403 REPGCSMCLAmNPDKLPP--------GERCAS---TSNRNFEGRQGKGGR-THLVSPAMAAAAAITGHF 459
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
686-840 |
1.03e-13 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 69.42 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 686 TTDHISPAGniarnsPAARYltnrgltprefnsygsrrgndaimaRGTFANIRllNKFL-------NKQAPQTVHLPSGE 758
Cdd:cd01578 7 TTDHISAAG------PWLKY-------------------------RGHLDNIS--NNLLigainaeNGKANSVKNQVTGE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 759 TLDVFDAAERYQQAGLPLIVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYL--------- 829
Cdd:cd01578 54 YGPVPDTARDYKAHGIKWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAdpadydkih 133
|
170
....*....|.
gi 18098515 830 PGETADSLGLT 840
Cdd:cd01578 134 PDDKVDILGLT 144
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
682-871 |
2.21e-13 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 69.82 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 682 GDSVTTDHISPAgniarnspaaRYLtnRGLTPREFnsygsrrgndaimARGTFANIRLLNK-----FLNkqapqtvhlps 756
Cdd:COG0066 15 GDNIDTDQIIPA----------RFL--KTIDREGL-------------GKHLFEDWRYDRSpdpdfVLN----------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 757 getldvfdaAERYQQAGlplIVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEyLPGET 833
Cdd:COG0066 59 ---------QPRYQGAD---ILVAGRNFGCGSSREhapWALKD---YGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEA 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18098515 834 ADSL--GLTGRERYTINIpeDLkPRMTvqIKLDTGKTFQA 871
Cdd:COG0066 123 VDALfaAIEANPGDELTV--DL-EAGT--VTNGTGETYPF 157
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
170-338 |
7.87e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 69.27 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 170 IPPGSGIIHQVNLEYLArvvfdqdGCyyPDSLVGTDSHTTMidglGVLGWEAFpcsavtaGVGGIEAEAVMLGQPISMVL 249
Cdd:PRK11413 123 VPPHIAVIHQYMREMMA-------GG--GKMILGSDSHTRY----GALGTMAV-------GEGGGELVKQLLNDTYDIDY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 250 PQVIGYKLMGKPHPLVTSTDIVLTITKHLRQVGVV-GKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSIA 328
Cdd:PRK11413 183 PGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHN 262
|
170
....*....|
gi 18098515 329 YLLQTGREED 338
Cdd:PRK11413 263 WLALHGRGQD 272
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
774-843 |
2.71e-11 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 60.68 E-value: 2.71e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18098515 774 LPLIVLAGKEYGSGSSR---DWAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGETADSLGLTGRE 843
Cdd:cd01577 17 LGDIIVAGKNFGCGSSRehaPWALKD---AGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEVEAKPGDE 86
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
777-895 |
1.23e-09 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 57.82 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 777 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEylpgetADSLGLTGRERYTINIpedlkpr 856
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLIE------AKTEGIKDGDEVTVDL------- 116
|
90 100 110
....*....|....*....|....*....|....*....
gi 18098515 857 MTVQIKLDTGKTFqaVMRFDTDVELTYFHNGGILNYMIR 895
Cdd:TIGR02087 117 ETGEIRVNGNEEY--KGEPLPDFLLEILREGGLLEYLKK 153
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
777-827 |
5.56e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 56.35 E-value: 5.56e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 18098515 777 IVLAGKEYGSGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLE 827
Cdd:PRK14023 52 ILVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFE 102
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
777-899 |
8.48e-08 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 52.52 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 777 IVLAGKEYGSGSSRD---WAAKGpflLGIKAVLAESYERIHRSNLVGMGVIPLEYlpGETADSLGlTGRErytINIpeDL 853
Cdd:PRK00439 51 IIVAGKNFGCGSSREhapIALKA---AGVSAVIAKSFARIFYRNAINIGLPVLEC--DEAVDKIE-DGDE---VEV--DL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18098515 854 KprmTVQIK-LDTGKTFQA-----VMRfdtdvELtyFHNGGILNYMIRKMAQ 899
Cdd:PRK00439 120 E---TGVITnLTTGEEYKFkpipeFML-----EI--LKAGGLIEYLKKKGRF 161
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
767-837 |
4.66e-06 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 48.20 E-value: 4.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18098515 767 ERYQQAGlplIVLAGKEYGSGSSRD---WAakgpfLL--GIKAVLAESYERIHRSNLVGMGVIPLEyLPGETADSL 837
Cdd:PRK01641 63 PRYQGAS---ILLAGDNFGCGSSREhapWA-----LAdyGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDEL 129
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
681-827 |
2.10e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 47.16 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18098515 681 LGDSVTTDHISPAGniarnspaarYLTNRGLTPREFNSYGSrrgndaimargtFANIRLlnkflnKQAPQTVHLPSGETl 760
Cdd:PLN00072 76 VGDNIDTDQIIPAE----------YLTLVPSKPDEYEKLGS------------YALIGL------PAFYKTRFVEPGEM- 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18098515 761 dvfdaAERYQqaglplIVLAGKEYGSGSSRDWAakgPFLLG---IKAVLAESYERIHRSNLVGMG-VIPLE 827
Cdd:PLN00072 127 -----KTKYS------IIIGGENFGCGSSREHA---PVALGaagAKAVVAESYARIFFRNSVATGeVYPLE 183
|
|
| |
