|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
401-550 |
1.04e-49 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 168.67 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 401 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 480
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161333819 481 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 550
Cdd:pfam08030 72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
297-570 |
2.24e-49 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 169.79 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 297 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 370
Cdd:cd06186 1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 371 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 450
Cdd:cd06186 81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 451 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 530
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 161333819 531 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 570
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
165-423 |
3.69e-31 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 128.81 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 165 GGLYVAvTRLAGITGIVITLcliliitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERivrgqtaesleeHnldic 244
Cdd:PLN02844 234 GRIYLA-GEIALVTGLVIWI-------TSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGDR------------H----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 245 adkieewgkikecpvpkfagnppmtWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQ 323
Cdd:PLN02844 289 -------------------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 324 YIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSY 401
Cdd:PLN02844 344 VIFMKIPSISRFQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRY 423
|
250 260
....*....|....*....|..
gi 161333819 402 EVVMLVGAGIGVTPFASILKSV 423
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEI 445
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
296-548 |
7.79e-24 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 99.83 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 296 VITKVVTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP-EEDFFSIHIRIV--GDWTEGLFNACGCD 372
Cdd:cd00322 1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 373 KqefqdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKycdnatsLKLKKIYFYWLCRDTHAFe 452
Cdd:cd00322 80 E-----------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD-------KPGGEITLLYGARTPADL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 453 WFADLLQLLetqmqERNNANFLsynIYLTGWDESQANHFAVHHDeekdvitglkqktlygrpnwDNEFKTIASEHPNTTI 532
Cdd:cd00322 141 LFLDELEEL-----AKEGPNFR---LVLALSRESEAKLGPGGRI--------------------DREAEILALLPDDSGA 192
|
250
....*....|....*.
gi 161333819 533 GVFLCGPEALAETLSK 548
Cdd:cd00322 193 LVYICGPPAMAKAVRE 208
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
299-395 |
8.31e-24 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 96.25 E-value: 8.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 299 KVVTHPFKTIELQMKK--KGFKMEVGQYIFVKC-PKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFN-ACGCDKQ 374
Cdd:pfam08022 8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANyLSSSCPK 87
|
90 100
....*....|....*....|.
gi 161333819 375 EFQDAWKLPKIAVDGPFGTAS 395
Cdd:pfam08022 88 SPENGKDKPRVLIEGPYGPPS 108
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
170-439 |
1.87e-21 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 98.40 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 170 AVTRLAGitgiVITLCLILIITSST-KTIRRSYFEVFWYTHHLFVIFFIGLAIHgaerivrgqtaesleehnLDICADKI 248
Cdd:PLN02292 247 GVSNLAG----EIALVAGLVMWATTyPKIRRRFFEVFFYTHYLYIVFMLFFVFH------------------VGISFALI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 249 eewgkikecPVPKFagnppmtwkwivgpmFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQM-KKKGFKMEVGQYIFV 327
Cdd:PLN02292 305 ---------SFPGF---------------YIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFsKNPMLMYSPTSIMFV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 328 KCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAwklpkIAVDGPFGTASEDVFSYEVVM 405
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQIDRLA-----VSVEGPYGPASTDFLRHESLV 435
|
250 260 270
....*....|....*....|....*....|....
gi 161333819 406 LVGAGIGVTPFASILKSVWykYCDNATSLKLKKI 439
Cdd:PLN02292 436 MVSGGSGITPFISIIRDLI--YTSSTETCKIPKI 467
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
152-549 |
9.65e-18 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 85.72 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 152 YLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTktIRR--SYfEVFWYTHHLFVIFFIGLAIHGAerivr 229
Cdd:COG4097 103 KWLVGWGGLPARLAALLTLLRGLAELLGEWAFYLLLALVVLSL--LRRrlPY-ELWRLTHRLLAVAYLLLAFHHL----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 230 gqtaeSLeehnldicadkieewgkikecpVPKFAGNPPMTWKWI---VGPMFLYLCERLVRFWRSQQKV-VITKVVTHPF 305
Cdd:COG4097 175 -----LL----------------------GGPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 306 KTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRIVGDWTEGLFnacgcdkqefqdaw 380
Cdd:COG4097 228 DVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRLG-------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 381 KLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykycdNATSLKLKKIYFYWLCRDTHAf 451
Cdd:COG4097 294 RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL------AARPGDQRPVDLFYCVRDEED- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 452 ewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqktlyGRPNwdneFKTIASEHPN-T 530
Cdd:COG4097 362 ---APFLEELRALAARLAGLRL-------------------HLVVSDED-----------GRLT----AERLRRLVPDlA 404
|
410
....*....|....*....
gi 161333819 531 TIGVFLCGPEALAETLSKQ 549
Cdd:COG4097 405 EADVFFCGPPGMMDALRRD 423
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
65-220 |
2.32e-16 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 75.38 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 65 MLILLPVCRNLLSFLRGSSaccstrirrqLDRNLTFHKMVAWMIALHTAIHTIAHLFNvewcvnarvgisdrysialsdi 144
Cdd:pfam01794 11 LLLLLALRNNPLEWLTGLS----------YDRLLLFHRWLGRLAFLLALLHVILYLIY---------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333819 145 gdneneeylnfarEKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLA 220
Cdd:pfam01794 59 -------------WLRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
322-549 |
3.15e-10 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 60.57 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 322 GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDwteGLFnacgcdKQEFQDAWKlP--KIAVDGPFGTasedvF 399
Cdd:COG1018 37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG---GGG------SNWLHDHLK-VgdTLEVSGPRGD-----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 400 SYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCR--DTHAfewFADLLQLLETQMqernnAN 472
Cdd:COG1018 102 VLDPeparpLLLIAGGIGITPFLSMLRTL-------LARGPFRPVTLVYGARspADLA---FRDELEALAARH-----PR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333819 473 FlsyniyltgwdesqanHFAVHHDEEKDVITglkqktlyGRPNwDNEFKTIASEHPNTTigVFLCGPEALAETLSKQ 549
Cdd:COG1018 167 L----------------RLHPVLSREPAGLQ--------GRLD-AELLAALLPDPADAH--VYLCGPPPMMEAVRAA 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
401-550 |
1.04e-49 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 168.67 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 401 YEVVMLVGAGIGVTPFASILKSVWYKYCdnatSLKLKKIYFYWLCRDTHAFEWFADLLQLLETQMQErnnanFLSYNIYL 480
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSK----KLKTKKIKFYWVVRDLSSLEWFKDVLNELEELKEL-----NIEIHIYL 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 161333819 481 TGWDESQAN--------HFAVHHDEEKDVITGLKQKTLYGRPNWDNEFKTIASEHPNTTIGVFLCGPEALAETLSKQS 550
Cdd:pfam08030 72 TGEYEAEDAsdqsdssiRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
297-570 |
2.24e-49 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 169.79 E-value: 2.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 297 ITKVVTHPF-KTIELQMKK-KGFKMEVGQYIFVKCPKV-SKLEWHPFTLTSAPEE--DFFSIHIRIV-GDWTEGLFNACG 370
Cdd:cd06186 1 IATVELLPDsDVIRLTIPKpKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 371 CDKQEFQdawklPKIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKYcdnATSLKLKKIYFYWLCRDTHA 450
Cdd:cd06186 81 SPGGGVS-----LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS---SKTSRTRRVKLVWVVRDRED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 451 FEWFADLLqlletqMQERNNANFLSYNIYLTgwdesqanhfavhhdeekdvitglkqktlygrpnwdnefktiasehpnt 530
Cdd:cd06186 153 LEWFLDEL------RAAQELEVDGEIEIYVT------------------------------------------------- 177
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 161333819 531 tiGVFLCGPEALAETLSKQSISNsesgpRGVHFIFNKENF 570
Cdd:cd06186 178 --RVVVCGPPGLVDDVRNAVAKK-----GGTGVEFHEESF 210
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
165-423 |
3.69e-31 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 128.81 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 165 GGLYVAvTRLAGITGIVITLcliliitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAERivrgqtaesleeHnldic 244
Cdd:PLN02844 234 GRIYLA-GEIALVTGLVIWI-------TSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAGDR------------H----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 245 adkieewgkikecpvpkfagnppmtWKWIVGPMFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKKK-GFKMEVGQ 323
Cdd:PLN02844 289 -------------------------FYMVFPGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVLPKDpGLKYAPTS 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 324 YIFVKCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAWKLPKIAVDGPFGTASEDVFSY 401
Cdd:PLN02844 344 VIFMKIPSISRFQWHPFSITSSSniDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVAIEGPYGPASVDFLRY 423
|
250 260
....*....|....*....|..
gi 161333819 402 EVVMLVGAGIGVTPFASILKSV 423
Cdd:PLN02844 424 DSLLLVAGGIGITPFLSILKEI 445
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
296-548 |
7.79e-24 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 99.83 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 296 VITKVVTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAP-EEDFFSIHIRIV--GDWTEGLFNACGCD 372
Cdd:cd00322 1 VATEDVTDDVRLFRLQ-LPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPdEEGELELTVKIVpgGPFSAWLHDLKPGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 373 KqefqdawklpkIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKSVWYKycdnatsLKLKKIYFYWLCRDTHAFe 452
Cdd:cd00322 80 E-----------VEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD-------KPGGEITLLYGARTPADL- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 453 WFADLLQLLetqmqERNNANFLsynIYLTGWDESQANHFAVHHDeekdvitglkqktlygrpnwDNEFKTIASEHPNTTI 532
Cdd:cd00322 141 LFLDELEEL-----AKEGPNFR---LVLALSRESEAKLGPGGRI--------------------DREAEILALLPDDSGA 192
|
250
....*....|....*.
gi 161333819 533 GVFLCGPEALAETLSK 548
Cdd:cd00322 193 LVYICGPPAMAKAVRE 208
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
299-395 |
8.31e-24 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 96.25 E-value: 8.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 299 KVVTHPFKTIELQMKK--KGFKMEVGQYIFVKC-PKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDWTEGLFN-ACGCDKQ 374
Cdd:pfam08022 8 KVALLPDNVLKLRVSKpkKPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANyLSSSCPK 87
|
90 100
....*....|....*....|.
gi 161333819 375 EFQDAWKLPKIAVDGPFGTAS 395
Cdd:pfam08022 88 SPENGKDKPRVLIEGPYGPPS 108
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
170-439 |
1.87e-21 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 98.40 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 170 AVTRLAGitgiVITLCLILIITSST-KTIRRSYFEVFWYTHHLFVIFFIGLAIHgaerivrgqtaesleehnLDICADKI 248
Cdd:PLN02292 247 GVSNLAG----EIALVAGLVMWATTyPKIRRRFFEVFFYTHYLYIVFMLFFVFH------------------VGISFALI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 249 eewgkikecPVPKFagnppmtwkwivgpmFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQM-KKKGFKMEVGQYIFV 327
Cdd:PLN02292 305 ---------SFPGF---------------YIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFsKNPMLMYSPTSIMFV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 328 KCPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQDAwklpkIAVDGPFGTASEDVFSYEVVM 405
Cdd:PLN02292 361 NIPSISKLQWHPFTITSSSklEPEKLSVMIKSQGKWSTKLYHMLSSSDQIDRLA-----VSVEGPYGPASTDFLRHESLV 435
|
250 260 270
....*....|....*....|....*....|....
gi 161333819 406 LVGAGIGVTPFASILKSVWykYCDNATSLKLKKI 439
Cdd:PLN02292 436 MVSGGSGITPFISIIRDLI--YTSSTETCKIPKI 467
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
171-434 |
5.43e-21 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 97.04 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 171 VTRLAGITGIVITLCLILiitSSTKTIRRSYFEVFWYTHHLFVIFFIGLAIHGAErivrgqtaesleehnldicadkiee 250
Cdd:PLN02631 231 VPNLAGTIAMVIGIAMWV---TSLPSFRRKKFELFFYTHHLYGLYIVFYVIHVGD------------------------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 251 wgkikecpvpkfagnppmTWKWIVGP-MFLYLCERLVRFWRSQQKVVITKVVTHPFKTIELQMKK-KGFKMEVGQYIFVK 328
Cdd:PLN02631 283 ------------------SWFCMILPnIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLH 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 329 CPKVSKLEWHPFTLTSAP--EEDFFSIHIRIVGDWTEGLFNACGCDKQEFQdawklpkIAVDGPFGTASEDVFSYEVVML 406
Cdd:PLN02631 345 VPSISKLQWHPFTITSSSnlEKDTLSVVIRRQGSWTQKLYTHLSSSIDSLE-------VSTEGPYGPNSFDVSRHNSLIL 417
|
250 260
....*....|....*....|....*...
gi 161333819 407 VGAGIGVTPFASILKSVWYKYCDNATSL 434
Cdd:PLN02631 418 VSGGSGITPFISVIRELIFQSQNPSTKL 445
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
152-549 |
9.65e-18 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 85.72 E-value: 9.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 152 YLNFAREKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTktIRR--SYfEVFWYTHHLFVIFFIGLAIHGAerivr 229
Cdd:COG4097 103 KWLVGWGGLPARLAALLTLLRGLAELLGEWAFYLLLALVVLSL--LRRrlPY-ELWRLTHRLLAVAYLLLAFHHL----- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 230 gqtaeSLeehnldicadkieewgkikecpVPKFAGNPPMTWKWI---VGPMFLYLCERLVRFWRSQQKV-VITKVVTHPF 305
Cdd:COG4097 175 -----LL----------------------GGPFYWSPPAGVLWAalaAAGLAAAVYSRLGRPLRSRRHPyRVESVEPEAG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 306 KTIELQMK---KKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEED-FFSIHIRIVGDWTEGLFnacgcdkqefqdaw 380
Cdd:COG4097 228 DVVELTLRpegGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDgRLRFTIKALGDFTRRLG-------------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 381 KLP---KIAVDGPFGTasedvFSYEV------VMLVGAGIGVTPFASILKSVwykycdNATSLKLKKIYFYWLCRDTHAf 451
Cdd:COG4097 294 RLKpgtRVYVEGPYGR-----FTFDRrdtaprQVWIAGGIGITPFLALLRAL------AARPGDQRPVDLFYCVRDEED- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 452 ewfADLLQLLETQMQERNNANFlsyniyltgwdesqanhfaVHHDEEKDvitglkqktlyGRPNwdneFKTIASEHPN-T 530
Cdd:COG4097 362 ---APFLEELRALAARLAGLRL-------------------HLVVSDED-----------GRLT----AERLRRLVPDlA 404
|
410
....*....|....*....
gi 161333819 531 TIGVFLCGPEALAETLSKQ 549
Cdd:COG4097 405 EADVFFCGPPGMMDALRRD 423
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
307-549 |
9.76e-17 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 79.22 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 307 TIELQMKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSAPEEDFfsiHIRIV----GDWTEGLfnacgcdkqefqdAWKL 382
Cdd:cd06198 11 TLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDG---RLRFTikalGDYTRRL-------------AERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 383 P---KIAVDGPFGtasedVFSYEV----VMLVGAGIGVTPFASILKsvwykycDNATSLKLKKIYFYWlCRDTHAFEWFA 455
Cdd:cd06198 75 KpgtRVTVEGPYG-----RFTFDDrrarQIWIAGGIGITPFLALLE-------ALAARGDARPVTLFY-CVRDPEDAVFL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 456 DLLQlletqmqernnanflsyniyltgwDESQANHFAVHhdeekdVITGlkqktlyGRPNWDNEFKTIASEHPN-TTIGV 534
Cdd:cd06198 142 DELR------------------------ALAAAAGVVLH------VIDS-------PSDGRLTLEQLVRALVPDlADADV 184
|
250
....*....|....*
gi 161333819 535 FLCGPEALAETLSKQ 549
Cdd:cd06198 185 WFCGPPGMADALEKG 199
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
65-220 |
2.32e-16 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 75.38 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 65 MLILLPVCRNLLSFLRGSSaccstrirrqLDRNLTFHKMVAWMIALHTAIHTIAHLFNvewcvnarvgisdrysialsdi 144
Cdd:pfam01794 11 LLLLLALRNNPLEWLTGLS----------YDRLLLFHRWLGRLAFLLALLHVILYLIY---------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333819 145 gdneneeylnfarEKIKNPEGGLYVAVTRLAGITGIVITLCLILIITSSTKTIRRSYFEVFWYTHHLFVIFFIGLA 220
Cdd:pfam01794 59 -------------WLRFSLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
294-447 |
1.34e-13 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 70.66 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 294 KVVITKVVTHPFKTIELQMKKKGFKMEVGQYIFVKCPKvsKLEWHPFTLTSAP-EEDFFSIHIRIVGDWTEGLFNacgcd 372
Cdd:COG0543 1 KVVSVERLAPDVYLLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPrEDGTIELHIRVVGKGTRALAE----- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 161333819 373 KQEFQdawklpKIAVDGPFGTAsedvFSYEV----VMLVGAGIGVTPFASILKSVWYKYCdnatslklkKIYFYWLCRD 447
Cdd:COG0543 74 LKPGD------ELDVRGPLGNG----FPLEDsgrpVLLVAGGTGLAPLRSLAEALLARGR---------RVTLYLGART 133
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
322-549 |
3.15e-10 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 60.57 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 322 GQYIFVKCPKVSKLEWHPFTLTSAPEEDFFSIHIRIVGDwteGLFnacgcdKQEFQDAWKlP--KIAVDGPFGTasedvF 399
Cdd:COG1018 37 GQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG---GGG------SNWLHDHLK-VgdTLEVSGPRGD-----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 400 SYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCR--DTHAfewFADLLQLLETQMqernnAN 472
Cdd:COG1018 102 VLDPeparpLLLIAGGIGITPFLSMLRTL-------LARGPFRPVTLVYGARspADLA---FRDELEALAARH-----PR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 161333819 473 FlsyniyltgwdesqanHFAVHHDEEKDVITglkqktlyGRPNwDNEFKTIASEHPNTTigVFLCGPEALAETLSKQ 549
Cdd:COG1018 167 L----------------RLHPVLSREPAGLQ--------GRLD-AELLAALLPDPADAH--VYLCGPPPMMEAVRAA 216
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
306-422 |
3.85e-09 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 57.58 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 306 KTIELQmKKKGFKMEVGQYIFVKCPKVSKLEWHPFTLtSAPEEDFFSIHIRIVGDWTEGLFNacgcdKQEFQdawklpKI 385
Cdd:PRK00054 20 YTLVLD-GEKVFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLSK-----LKEGD------EL 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 161333819 386 AVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKS 422
Cdd:PRK00054 87 DIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKE 123
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
297-458 |
5.06e-08 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 54.25 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 297 ITKVVTHPFKTIELQMK--KKGFKMEVGQYIFVKCPKVSKLEWHPFTLTSA-PEEDFFSIHIRIVGDWTEGLFNacgcdk 373
Cdd:cd06192 1 IVKKEQLEPNLVLLTIKapLAARLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLIAE------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 374 qefqdaWKLP-KIAVDGPFGTASEDVFSYEVVMLVGAGIGVTPFASILKsvwYKYCDNAtslklkKIYFYWLCRDTHA-- 450
Cdd:cd06192 75 ------LKPGeKLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK---KLAANGN------KVTVLAGAKKAKEef 139
|
170
....*....|..
gi 161333819 451 ----FEWFADLL 458
Cdd:cd06192 140 ldeyFELPADVE 151
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
295-434 |
1.87e-07 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 52.25 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 295 VVITKVV--THPFKTIELQMKkkgFKMEVGQYIFVKCPKVSKLewhPFTLTSAPEEDffSIHIRIVGDWTEGLFNACGCD 372
Cdd:cd06220 1 VTIKEVIdeTPTVKTFVFDWD---FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPN--SITVKKVGEATSALHDLKEGD 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 161333819 373 KqefqdawklpkIAVDGPFGTASEDVfsYEVVMLVGAGIGVTPFASILKSvwYKYCDNATSL 434
Cdd:cd06220 73 K-----------LGIRGPYGNGFELV--GGKVLLIGGGIGIAPLAPLAER--LKKAADVTVL 119
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
322-473 |
1.73e-06 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 49.08 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 322 GQYIFVKCPKVSKLewhPFTLTSAPEED-FFSIHIRIV--GDWTEGLFNACGCDKqefqdawklpKIAVDGPFGTASEDV 398
Cdd:cd06189 29 GQYLDLLLDDGDKR---PFSIASAPHEDgEIELHIRAVpgGSFSDYVFEELKENG----------LVRIEGPLGDFFLRE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 161333819 399 FSYEVVMLVGAGIGVTPFASILksvwykycDNATSLKLK-KIYFYWLCRDThafewfADLLQLLETQMQERNNANF 473
Cdd:cd06189 96 DSDRPLILIAGGTGFAPIKSIL--------EHLLAQGSKrPIHLYWGARTE------EDLYLDELLEAWAEAHPNF 157
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
322-541 |
3.96e-05 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 45.24 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 322 GQYIFVKCPKVSKLEWHP--FTLTSAPEEDFFSI----------------HIRiVGDwteglfnacgcdkqefqdawklp 383
Cdd:cd06184 40 GQYLSVRVKLPGLGYRQIrqYSLSDAPNGDYYRIsvkrepgglvsnylhdNVK-VGD----------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 384 KIAVDGPFGTasedvFSYEV-----VMLVGAGIGVTPFASILKSVwykycdnATSLKLKKIYFYWLCRD--THAF-EWFA 455
Cdd:cd06184 96 VLEVSAPAGD-----FVLDEasdrpLVLISAGVGITPMLSMLEAL-------AAEGPGRPVTFIHAARNsaVHAFrDELE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 456 DLLQlletqmqerNNANFLSYNIY--LTGWDESQANHFAVHHDEEKdvitgLKQKTLygrpnwdnefktiaseHPNTTig 533
Cdd:cd06184 164 ELAA---------RLPNLKLHVFYsePEAGDREEDYDHAGRIDLAL-----LRELLL----------------PADAD-- 211
|
....*...
gi 161333819 534 VFLCGPEA 541
Cdd:cd06184 212 FYLCGPVP 219
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
301-422 |
2.44e-04 |
|
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99793 [Multi-domain] Cd Length: 218 Bit Score: 42.61 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 301 VTHPFKTIELQmKKKGFKMEVGQYIFVKCPKVS-KLEWHPFTLTSAPEEDFFSIHIRIVGDwTEGLFNACGcdkqefqDA 379
Cdd:cd06196 11 VTHDVKRLRFD-KPEGYDFTPGQATEVAIDKPGwRDEKRPFTFTSLPEDDVLEFVIKSYPD-HDGVTEQLG-------RL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 161333819 380 WKLPKIAVDGPFGTAS---EDVFsyevvmlVGAGIGVTPFASILKS 422
Cdd:cd06196 82 QPGDTLLIEDPWGAIEykgPGVF-------IAGGAGITPFIAILRD 120
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|
| FNR_like_2 |
cd06197 |
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ... |
340-423 |
1.95e-03 |
|
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99794 Cd Length: 220 Bit Score: 40.07 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161333819 340 FTLTSAPE----EDFFSIHIRIVGDWTEGLFNAcgcDKQEFQDAWKLPKIAVDGPFgTASEDVFSYEVVML-VGAGIGVT 414
Cdd:cd06197 63 FTVSSAPPhdpaTDEFEITVRKKGPVTGFLFQV---ARRLREQGLEVPVLGVGGEF-TLSLPGEGAERKMVwIAGGVGIT 138
|
....*....
gi 161333819 415 PFASILKSV 423
Cdd:cd06197 139 PFLAMLRAI 147
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