|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00178 |
PLN00178 |
sulfite reductase |
15-635 |
0e+00 |
|
sulfite reductase
Pssm-ID: 177773 [Multi-domain] Cd Length: 623 Bit Score: 1277.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 15 GAAAQLPRSRVLGRPIRVAPPAAARPGGASAGS--IRAVSAPAKKDAS-EVKRSKVEIIKEKSNFLRYPLNEELVSEAPN 91
Cdd:PLN00178 1 ASKSSSAVSLLLARQSAATTAFSTGPSRSRSGRlvIRAVATPVKKPTTePPKRSKVEIIKENSNFLRHPLNEELATEAPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 92 INESAVQLIKFHGSYQQTDRDVRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLK 171
Cdd:PLN00178 81 INEDAVQLIKFHGSYQQDNREKRGGKAYQFMLRTKQPAGKVPNRLYLVMDDLADEFGIGTLRLTTRQTFQLHGVLKKDLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 172 TVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKKDILFAQQTAENIAALLTPQSGAYYDLWVDGEKIMSAEePPEVTKAR 251
Cdd:PLN00178 161 TVMSSIIKNMGSTLGACGDVNRNVLAPAAPFARKDYLFAQELAKNIAALLAPQSGAYYDIWVDGEKIMSAE-PPEVTKAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 252 NDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPR 331
Cdd:PLN00178 240 NDNSHGTNFEDSPEPIYGTQFLPRKFKIAVTVPGDNSVDILTNDIGVVVVSDEAGEPQGYNIYVGGGMGRTHRNETTFPR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 332 LADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQ 411
Cdd:PLN00178 320 LADPLGYVPKEDILYAVKAIVATQRDYGRRDDRKQSRMKYLVHSWGIEKFRSVVEQYYGKKFEPFRELPEWEFKSYLGWH 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 412 EQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTA 491
Cdd:PLN00178 400 EQGDGKLFYGVHVDNGRIKGEAKKALREVIEKYNLPVRLTPNQNLILCDIRPAWKEPITAALAAAGLLEPEEVDPLNRTA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 492 MACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPN 571
Cdd:PLN00178 480 MACPALPLCPLAITEAERGIPDILKRVRAMFNKVGLKYDESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPN 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1145994699 572 QSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVNKWAESPSAA 635
Cdd:PLN00178 560 QTRLAEPFMDKVKVDDLEKVLEPLFYMWKQQRQEKESFGDFTNRVGFEALKEYIESYAGSVVAP 623
|
|
| sir |
TIGR02042 |
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ... |
59-628 |
0e+00 |
|
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite reductase (NADPH) found in Proteobacteria and Eubacteria, sulfite reductase (ferredoxin) is a cyanobacterial and plant monomeric enzyme that also catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131097 [Multi-domain] Cd Length: 577 Bit Score: 998.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 59 ASEVKRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRDVRGQ---KNYSFMLRTKNPCGKVPNQ 135
Cdd:TIGR02042 1 AKPQKRSKVEILKERSNFLREPLNEQLLEEATHFNEDAVQILKFHGSYQQDNRDNRGKgqeKDYQFMLRTKNPGGYVPPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 136 LYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKK-DILFAQQTA 214
Cdd:TIGR02042 81 LYLTLDDLADEYGNGTLRATTRQTFQLHGILKKNLKTVISTIVKNLGSTLGACGDLNRNVMAPPAPFRKRpEYEFAREYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 215 ENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTN 294
Cdd:TIGR02042 161 DNIADLLTPQSGAYYELWLDGEKVMSAEPDPEVVAARNDNSHGTNFADSPEPLYGTQYLPRKFKIAVTVPGDNSIDLFTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 295 DIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLID 374
Cdd:TIGR02042 241 DIGLVVVSNERGELEGFNIYVGGGMGRTHNKEETFARLADPLGYVPKEDIYYAVKAIVATQRDYGDRDDRRHARMKYLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 375 RWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRVGG----QAKKTLREIIEKYNLDVSI 450
Cdd:TIGR02042 321 DWGIEKFREVVEQYFGKKIAPVRELPEFEYKDYLGWHEQGDGKWFLGLHIDSGRVKDdgnwQLKKALREIVEKYNLPVRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 451 TPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDs 530
Cdd:TIGR02042 401 TPNQNIILYDIQPEWKRAITTVLAQRGVLQPEAIDPLNRYAMACPALPTCGLAITESERAIPGILKRIRALLEKVGLPD- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 531 ESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFG 610
Cdd:TIGR02042 480 EHFVVRMTGCPNGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLEKVLEPLFVHFKQSRQSGESFG 559
|
570
....*....|....*...
gi 1145994699 611 SFTNRTGFDKLKEVVNKW 628
Cdd:TIGR02042 560 DFCDRVGFDALREFVESY 577
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
98-626 |
2.15e-176 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 511.20 E-value: 2.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 98 QLIKFHGSYQQTDRDvrgqknYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTV 177
Cdd:COG0155 38 LRLKFHGLYQQRDPD------GAFMLRVRIPGGVLTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILREL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 178 IKNMGSTLGACGDLNRNVLAPAAPFVKKDILF-AQQTAENIAALLTPqsgayydlwvdgekimsaeeppevtkarndnsh 256
Cdd:COG0155 112 AEVGLTTIGACGDVVRNVTASPLAGVDPDELFdVRPYAEAISQHLLG--------------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 257 gtnfpdspEPIYgtQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEpIGFNIYVGGGMGRThrvettfPRLADPL 336
Cdd:COG0155 159 --------HPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGL-VGFNVLVGGGLGRT-------PRLADVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 337 G-YVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYY-GKKFESF-RPLPEWQFNSYLGWQEQ 413
Cdd:COG0155 221 GeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEYlGFPLEPApRPLPAFARWDHLGVHEQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 414 G-DGKLFYGVHVDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPkdVDPLNLTA 491
Cdd:COG0155 301 KqDGLYYVGLSVENGRITDEQLRALADLAERYgSGEIRLTPNQNLILADVPEEDLPALEAALRALGLATP--PSGLRRDS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 492 MACPALPLCPLAQTEAERgILP-ILKRIRAvfNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPK----SYQIWL 566
Cdd:COG0155 379 IACPGLPTCKLAIAESKR-LAPaLADRLEE--DLDGLHDDEPIRIRISGCPNSCGRHYIADIGLVGKAKKgvveAYQLYL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1145994699 567 GGTPNQST-LAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVN 626
Cdd:COG0155 456 GGGLGGDArLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIEPLKELLY 516
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
217-388 |
1.33e-50 |
|
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 172.07 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 217 IAALLTPQSGAYYDLWVDGEKIMSAEEppevtkarndnshgtnfpDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDI 296
Cdd:pfam01077 5 RNVTLCPGAGLCPEELLDTRPLAKAIE------------------DEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 297 GVVVVSDDAGEpIGFNIYVGGGMGRTHRVETTFPRLadplGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRW 376
Cdd:pfam01077 67 GFVGVWKDGGE-IGFNILVGGGLGRTPGAAATLKVV----PFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERL 141
|
170
....*....|..
gi 1145994699 377 GIDRFRAEVEKY 388
Cdd:pfam01077 142 GLEKFREEVEER 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00178 |
PLN00178 |
sulfite reductase |
15-635 |
0e+00 |
|
sulfite reductase
Pssm-ID: 177773 [Multi-domain] Cd Length: 623 Bit Score: 1277.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 15 GAAAQLPRSRVLGRPIRVAPPAAARPGGASAGS--IRAVSAPAKKDAS-EVKRSKVEIIKEKSNFLRYPLNEELVSEAPN 91
Cdd:PLN00178 1 ASKSSSAVSLLLARQSAATTAFSTGPSRSRSGRlvIRAVATPVKKPTTePPKRSKVEIIKENSNFLRHPLNEELATEAPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 92 INESAVQLIKFHGSYQQTDRDVRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLK 171
Cdd:PLN00178 81 INEDAVQLIKFHGSYQQDNREKRGGKAYQFMLRTKQPAGKVPNRLYLVMDDLADEFGIGTLRLTTRQTFQLHGVLKKDLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 172 TVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKKDILFAQQTAENIAALLTPQSGAYYDLWVDGEKIMSAEePPEVTKAR 251
Cdd:PLN00178 161 TVMSSIIKNMGSTLGACGDVNRNVLAPAAPFARKDYLFAQELAKNIAALLAPQSGAYYDIWVDGEKIMSAE-PPEVTKAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 252 NDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPR 331
Cdd:PLN00178 240 NDNSHGTNFEDSPEPIYGTQFLPRKFKIAVTVPGDNSVDILTNDIGVVVVSDEAGEPQGYNIYVGGGMGRTHRNETTFPR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 332 LADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQ 411
Cdd:PLN00178 320 LADPLGYVPKEDILYAVKAIVATQRDYGRRDDRKQSRMKYLVHSWGIEKFRSVVEQYYGKKFEPFRELPEWEFKSYLGWH 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 412 EQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTA 491
Cdd:PLN00178 400 EQGDGKLFYGVHVDNGRIKGEAKKALREVIEKYNLPVRLTPNQNLILCDIRPAWKEPITAALAAAGLLEPEEVDPLNRTA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 492 MACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPN 571
Cdd:PLN00178 480 MACPALPLCPLAITEAERGIPDILKRVRAMFNKVGLKYDESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPN 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1145994699 572 QSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVNKWAESPSAA 635
Cdd:PLN00178 560 QTRLAEPFMDKVKVDDLEKVLEPLFYMWKQQRQEKESFGDFTNRVGFEALKEYIESYAGSVVAP 623
|
|
| sir |
TIGR02042 |
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ... |
59-628 |
0e+00 |
|
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite reductase (NADPH) found in Proteobacteria and Eubacteria, sulfite reductase (ferredoxin) is a cyanobacterial and plant monomeric enzyme that also catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131097 [Multi-domain] Cd Length: 577 Bit Score: 998.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 59 ASEVKRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRDVRGQ---KNYSFMLRTKNPCGKVPNQ 135
Cdd:TIGR02042 1 AKPQKRSKVEILKERSNFLREPLNEQLLEEATHFNEDAVQILKFHGSYQQDNRDNRGKgqeKDYQFMLRTKNPGGYVPPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 136 LYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKK-DILFAQQTA 214
Cdd:TIGR02042 81 LYLTLDDLADEYGNGTLRATTRQTFQLHGILKKNLKTVISTIVKNLGSTLGACGDLNRNVMAPPAPFRKRpEYEFAREYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 215 ENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTN 294
Cdd:TIGR02042 161 DNIADLLTPQSGAYYELWLDGEKVMSAEPDPEVVAARNDNSHGTNFADSPEPLYGTQYLPRKFKIAVTVPGDNSIDLFTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 295 DIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLID 374
Cdd:TIGR02042 241 DIGLVVVSNERGELEGFNIYVGGGMGRTHNKEETFARLADPLGYVPKEDIYYAVKAIVATQRDYGDRDDRRHARMKYLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 375 RWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRVGG----QAKKTLREIIEKYNLDVSI 450
Cdd:TIGR02042 321 DWGIEKFREVVEQYFGKKIAPVRELPEFEYKDYLGWHEQGDGKWFLGLHIDSGRVKDdgnwQLKKALREIVEKYNLPVRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 451 TPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDs 530
Cdd:TIGR02042 401 TPNQNIILYDIQPEWKRAITTVLAQRGVLQPEAIDPLNRYAMACPALPTCGLAITESERAIPGILKRIRALLEKVGLPD- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 531 ESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFG 610
Cdd:TIGR02042 480 EHFVVRMTGCPNGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLEKVLEPLFVHFKQSRQSGESFG 559
|
570
....*....|....*...
gi 1145994699 611 SFTNRTGFDKLKEVVNKW 628
Cdd:TIGR02042 560 DFCDRVGFDALREFVESY 577
|
|
| PRK13504 |
PRK13504 |
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit; |
59-626 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
Pssm-ID: 237402 [Multi-domain] Cd Length: 569 Bit Score: 812.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 59 ASEVKRSKVEIIKEKSNFLRYPLNEELVSEA-PNINESAVQLIKFHGSYQQTDRDVR--GQKN-----YSFMLRTKNPCG 130
Cdd:PRK13504 6 AVEGKLSDVERIKLESNYLRGTIAEELNDGLtGGFSEDDFQLLKFHGSYQQDDRDIRaeRAEQklepaYQFMLRCRLPGG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 131 KVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKKDILFA 210
Cdd:PRK13504 86 VITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESRLHAEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 211 QQTAENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEvtkarndnshgtnfpdspEPIYGTQYLPRKFKVAVTAAGDNSVD 290
Cdd:PRK13504 166 YEWAKKISDHLLPRTRAYAEIWLDGEKVATFSGTEE------------------EPIYGKTYLPRKFKIAVAVPPDNDVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 291 ILTNDIGVVVVSDDaGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMK 370
Cdd:PRK13504 228 VYANDLGFVAIAEN-GKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTDRKNARLK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 371 YLIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRV---GGQAKKT-LREIIEKYNL 446
Cdd:PRK13504 307 YTLERVGLDWFKAEVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIkdyPGRPLKTgLREIAKIHKG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 447 DVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERgILP-ILKRIRAVFNKV 525
Cdd:PRK13504 387 DFRLTANQNLIIANVPPSDKAKIEALLREYGLIDGVEESPLRRNSMACVALPTCGLAMAEAER-YLPsFIDRIEALLAKH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 526 GIKDsESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQE 605
Cdd:PRK13504 466 GLSD-EHIVIRMTGCPNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREP 544
|
570 580
....*....|....*....|.
gi 1145994699 606 GESFGSFTNRTGFdkLKEVVN 626
Cdd:PRK13504 545 GEGFGDFVIRAGI--IREVLD 563
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
98-626 |
2.15e-176 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 511.20 E-value: 2.15e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 98 QLIKFHGSYQQTDRDvrgqknYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTV 177
Cdd:COG0155 38 LRLKFHGLYQQRDPD------GAFMLRVRIPGGVLTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILREL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 178 IKNMGSTLGACGDLNRNVLAPAAPFVKKDILF-AQQTAENIAALLTPqsgayydlwvdgekimsaeeppevtkarndnsh 256
Cdd:COG0155 112 AEVGLTTIGACGDVVRNVTASPLAGVDPDELFdVRPYAEAISQHLLG--------------------------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 257 gtnfpdspEPIYgtQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEpIGFNIYVGGGMGRThrvettfPRLADPL 336
Cdd:COG0155 159 --------HPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGL-VGFNVLVGGGLGRT-------PRLADVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 337 G-YVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYY-GKKFESF-RPLPEWQFNSYLGWQEQ 413
Cdd:COG0155 221 GeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEYlGFPLEPApRPLPAFARWDHLGVHEQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 414 G-DGKLFYGVHVDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPkdVDPLNLTA 491
Cdd:COG0155 301 KqDGLYYVGLSVENGRITDEQLRALADLAERYgSGEIRLTPNQNLILADVPEEDLPALEAALRALGLATP--PSGLRRDS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 492 MACPALPLCPLAQTEAERgILP-ILKRIRAvfNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPK----SYQIWL 566
Cdd:COG0155 379 IACPGLPTCKLAIAESKR-LAPaLADRLEE--DLDGLHDDEPIRIRISGCPNSCGRHYIADIGLVGKAKKgvveAYQLYL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1145994699 567 GGTPNQST-LAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVN 626
Cdd:COG0155 456 GGGLGGDArLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIEPLKELLY 516
|
|
| CysI |
TIGR02041 |
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ... |
68-618 |
2.11e-153 |
|
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a six electron reduction of sulfite to sulfide in prokaryotic organisms. It is a complex oligomeric enzyme composed of two different peptides with a subunit composition of alpha(8)-beta(4). The alpha component, encoded by cysJ, is a flavoprotein containing both FMN and FAD, while the beta component, encoded by cysI, is a siroheme, iron-sulfur protein. In Salmonella typhimurium and Escherichia coli, both the alpha and beta subunits of sulfite reductase are located in a unidirectional gene cluster along with phosphoadenosine phosphosulfate reductase, which catalyzes a two step reduction of PAPS to give free sulfite. In cyanobacteria and plant species, sulfite reductase ferredoxin (EC 1.8.7.1) catalyzes the reduction of sulfite to sulfide. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273941 [Multi-domain] Cd Length: 541 Bit Score: 453.04 E-value: 2.11e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 68 EIIKEKSNFLRYPLNEELVSEAPN-INESAVQLIKFHGSYQQTDRDVRGQKN-------YSFMLRTKNPCGKVPNQLYLA 139
Cdd:TIGR02041 1 ERIKEESNYLRGTILEDLADPLTGgFKGDNFQLIRFHGMYQQDDRDLRAERAeqkleprYAMMLRCRLPGGVITPKQWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 140 MDTLADEFGI-GTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPFVKKDILFAQQTAENIA 218
Cdd:TIGR02041 81 IDKFAREYTNyGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 219 ALLTPQSGAYYDLWVDGEKIMSAEEPpevtkarndnshgtnfpdspEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGV 298
Cdd:TIGR02041 161 EHLLPRTRAYAEIWLDQEKVAGTEEV--------------------EPILGPTYLPRKFKTTVVIPPQNDVDVYANDLGF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 299 VVVSDDaGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGI 378
Cdd:TIGR02041 221 VAIAEN-GKLVGFNVLIGGGLSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTKYTIERMGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 379 DRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRV----GGQAKKTLREIIEKYNLDVSITPNQ 454
Cdd:TIGR02041 300 DTFKAEVERRAGIKFEPARPYEFTGRGDRIGWVKGIDGNWHLTLFIENGRIldypDKPLKTGLLEIAKIHKGDFRITANQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 455 NLILCGIDQAWREPITTALAQAGLLEpkDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDsESVV 534
Cdd:TIGR02041 380 NLIIAGVPEGGKAKIEKLARQYGLIN--AVTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMAKHGLSD-EEIV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 535 VRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTN 614
Cdd:TIGR02041 457 LRVTGCPNGCGRAMLAEIGLVGKAPGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLI 536
|
....
gi 1145994699 615 RTGF 618
Cdd:TIGR02041 537 RAGI 540
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
217-388 |
1.33e-50 |
|
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 172.07 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 217 IAALLTPQSGAYYDLWVDGEKIMSAEEppevtkarndnshgtnfpDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDI 296
Cdd:pfam01077 5 RNVTLCPGAGLCPEELLDTRPLAKAIE------------------DEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 297 GVVVVSDDAGEpIGFNIYVGGGMGRTHRVETTFPRLadplGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRW 376
Cdd:pfam01077 67 GFVGVWKDGGE-IGFNILVGGGLGRTPGAAATLKVV----PFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERL 141
|
170
....*....|..
gi 1145994699 377 GIDRFRAEVEKY 388
Cdd:pfam01077 142 GLEKFREEVEER 153
|
|
| nirA |
PRK09567 |
NirA family protein; |
16-635 |
5.00e-45 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 169.04 E-value: 5.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 16 AAAQLPRSRVLGRPirvAPPAAARPGGASAGSIRA---VSAPAKKDASEvkrskvEIIK-EKSNFLRYPLNEELVSEAPN 91
Cdd:PRK09567 23 DAARATRGAAGGQT---PAAPAAEPTGPDAIHIKAqdrFLAAGKKLCDQ------EKWKrEENPFDAWDRLKAQAAAGAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 92 INESAVQLIKFHGSYQqtdrdVRGQKNySFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLK 171
Cdd:PRK09567 94 PKPADNFRWKYHGLFY-----VAPAQD-SYMCRLRIPNGILTHWQFAGLADLADRHGGGYSHVTTRANLQLREIPPEHAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 172 TVLSTVIKNMGSTLGACGDLNRNVLApaapfvkkdilfaqqtaeniaallTPQSGayydlwVDGEKIMSAEeppevTKAR 251
Cdd:PRK09567 168 PVLEGLVDLGLTARGSGADNIRNVTG------------------------SPTAG------IDPQELLDTR-----PYAR 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 252 NDNSHGTNFPDspepIYGtqyLPRKFKVAVTAAGDNSVDILTNDIG--VVVVSDDAGEPIG--FNIYVGGGMGrtHRvet 327
Cdd:PRK09567 213 EWHHHILNDRS----LYG---LPRKFNVAFDGGGRIATLEDTNDIGfqAVRVLEGAGVAPGvyFRLVLGGITG--HK--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 328 tfpRLADPLGYVPKEDILYAI-KAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYYGKKF-----ESFRPLPE 401
Cdd:PRK09567 281 ---DFARDTGVLLRPEEATAVaDAIVRVFIENGDRTNRKKARLKYVLDAWGFDKFLEAVEEKLGRPLtrvpaEAVAPRPA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 402 WQFNSYLGWQEQGDGKLFY-GVHVDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREPITTALAQAGLl 479
Cdd:PRK09567 358 ADRFAHVGVHPQKQPGLNWiGVVLPVGRLTTDQMRGLAKIAARYgDGEIRLTVWQNLLISGVPDADVAAVEAAIEALGL- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 480 epkDVDPLNLTA--MACPALPLCPLAQTEAERGILPILKRIRAVfnkvgIKDSESVVVRITGCPNGCARPYMAELGFVG- 556
Cdd:PRK09567 437 ---TTEASSIRAglVACTGNAGCKFAAADTKGHALAIADYCEPR-----VALDQPVNIHLTGCHHSCAQHYIGDIGLIGa 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 557 -------DGPKSYQIWLGG--TPNQSTLAESFMDkVKLDDIEKVLEPLFTYWNGTRQE-GESFGSFTNRTGFDKLKEVVn 626
Cdd:PRK09567 509 kvavsegDTVEGYHIVVGGgfGEDAAIGREVFRD-VKAEDAPRLVERLLRAYLAHRQGpDETFQAFTRRHDPEALRSLA- 586
|
....*....
gi 1145994699 627 kwAESPSAA 635
Cdd:PRK09567 587 --EEQPVLA 593
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
108-595 |
1.19e-42 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 160.94 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 108 QTDRDVR-------------GQknysFMLRTKNPCGKVPNQLYLAMDTLADEFG-IGTLRLTTRQTFQLHGVL------- 166
Cdd:PRK09566 44 ETDLELRlkwlgmfwrpvtpGK----FMLRLRVPNGILTSEQLRVLASIVQRYGdDGSADITTRQNLQLRGILledlpei 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 167 KKNLKTV-LSTVIKNMgstlgacgDLNRNVlapaapfvkkdilfaqqTAENIAALltpqsgayydlwvDGEKIMSAEepP 245
Cdd:PRK09566 120 LNRLKAVgLTSVQSGM--------DNVRNI-----------------TGSPVAGI-------------DPDELIDTR--P 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 246 EVTKARN---DNSHGtnfpdSPEpiygTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDagEPIGFNIYVGGGMGrT 322
Cdd:PRK09566 160 LTQKLQDmltNNGEG-----NPE----FSNLPRKFNIAIAGGRDNSVHAEINDIAFVPAYKD--GVLGFNVLVGGFFS-S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 323 HRVETTFPRLAdplgYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYYGKKFESFRPLPE- 401
Cdd:PRK09566 228 QRCAYAIPLNA----WVKPDEVVRLCRAILEVYRDNGLRANRQKGRLMWLIDEWGIEKFRAAVEAQFGPPLLTAAPGDEi 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 402 -WQFNSYLG-WQEQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREpittALAQAGL 478
Cdd:PRK09566 304 dWEKRDHIGvHPQKQAGLNYVGLHVPVGRLYAEDMFELARLAEVYgSGEIRLTVEQNVIIPNIPDENLE----TFLAEPL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 479 LEPKDVDPLNLTA--MACPALPLCPLAQTEAERGILPILKRIravfnkvgikDSESVV---VRI--TGCPNGCARPYMAE 551
Cdd:PRK09566 380 LQKFSLEPGPLARglVSCTGNQYCNFALIETKNRALALAKEL----------DAELDLpqpVRIhwTGCPNSCGQPQVAD 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1145994699 552 LGFVGDGPK-------SYQIWLGGTP-NQSTLAESFMDKVKLDDIEKVLEPL 595
Cdd:PRK09566 450 IGLMGTKARkngktveGVDIYMGGKVgKDAKLGECVQKGIPCEDLKPVLKDL 501
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
273-593 |
1.66e-30 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 126.43 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 273 LPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDaGEpIGFNIYVGGGMGRTHRVEttfprlADPLG-YVPKEDILYAIKAI 351
Cdd:PLN02431 252 LPRKWNVCVVGSHDLFEHPHINDLAYMPATKD-GR-FGFNLLVGGFFSPKRCAE------AIPLDaWVPADDVVPLCKAI 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 352 VVTQRENGRRDDRKYSRMKYLIDRWGIDRFRAEVEKYY-GKKFEsfRPLPE------WQFNSYLGWQEQG-DGKLFYGVH 423
Cdd:PLN02431 324 LEAFRDLGTRGNRQKTRMMWLIDELGVEGFRSEVEKRMpNGELE--RAASEdlvdkkWERRDYLGVHPQKqEGLSYVGLH 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 424 VDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREpittALAQAGLLEPKDVDPLNLTA--MACPALPLC 500
Cdd:PLN02431 402 VPVGRLQAADMDELARLADEYgSGELRLTVEQNIIIPNVPNSKVE----ALLAEPLLQRFSPNPGLLLKglVACTGNQFC 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 501 PLAQTEAERgilpilkRIRAVFNKVGIKDSESVVVRI--TGCPNGCARPYMAELGFVG------DGP--KSYQIWLGGT- 569
Cdd:PLN02431 478 GQAIIETKA-------RALKVTEELERLVEVPRPVRMhwTGCPNSCGQVQVADIGFMGcmardeNGKavEGADIFVGGRv 550
|
330 340
....*....|....*....|....
gi 1145994699 570 PNQSTLAESFMDKVKLDDIEKVLE 593
Cdd:PLN02431 551 GSDSHLAEEYKKGVPCDELVPVVA 574
|
|
| CobG |
TIGR02435 |
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated ... |
120-559 |
3.30e-17 |
|
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated into the macrocycle at C-20. In the aerobic cobalamin biosythesis pathway, four enzymes are involved in the conversion of precorrin-3A to precorrin-6A. The first of the four steps is carried out by EC 1.14.13.83, precorrin-3B synthase (CobG), yielding precorrin-3B as the product. This is followed by three methylation reactions, which introduce a methyl group at C-17 (CobJ; EC 2.1.1.131), C-11 (CobM; EC 2.1.1.133) and C-1 (CobF; EC 2.1.1.152) of the macrocycle, giving rise to precorrin-4, precorrin-5 and precorrin-6A, respectively. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274131 [Multi-domain] Cd Length: 390 Bit Score: 84.08 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 120 SFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNlkTVLSTVIKNMGstLGACG---DLNRNVL 196
Cdd:TIGR02435 17 GLLVRVRLPGGRLTPAQAIGLADLAERLGNGIIEVTARGNLQLRGLTADH--DALSQALLAAG--LGAAGaaaDDIRNIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 197 APaaPFVKKD---ILFAQQTAENIAALLtpqsgayydlwvdgekimsaeeppEVTKArndnshgtnfpdspepiygTQYL 273
Cdd:TIGR02435 93 VS--PLAGIDpgeIADTRPLAAELRAAL------------------------ENERA-------------------LLEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 274 PRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGepIGFNIYVGGGMGRthrvettfprlADPLGYVPKEDILYAIKAIVV 353
Cdd:TIGR02435 128 PPKFSVAIDGGGRLVLLGDTADVRLQALTTGAG--VAWVVSLAGISTS-----------ARSLVTVAPDAAVPVAVALLR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 354 TQRENGRRddrkySRMKYLIDRWGIDRFRAEVEKyyGKKF-----ESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGR 428
Cdd:TIGR02435 195 VFVELGGA-----ARGRDLDDAFLFALALELVED--SRPLipdaaEGEAPRPAVDAAAPLGLHPQGDAGVTLGAGLALGQ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 429 VGGQAKKTLREII-EKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLL-EPKDvdPLNLTAmACPALPLC--PLAQ 504
Cdd:TIGR02435 268 LTAAQLRGLAQLAqALGDGDLRLTPWRALLVLGLPPERADAAQRALAALGLVtSASD--PRARII-ACTGAPGCasALAD 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1145994699 505 TEAErgilpilkrirAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGP 559
Cdd:TIGR02435 345 TRAD-----------AEALAAYCEPTAPITVHLSGCAKGCAHPGPAAITLVAAGA 388
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
114-174 |
9.32e-14 |
|
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 66.40 E-value: 9.32e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1145994699 114 RGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVL 174
Cdd:pfam03460 1 HPQKDGDYMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELL 61
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
412-476 |
1.82e-10 |
|
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 56.77 E-value: 1.82e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1145994699 412 EQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKY-NLDVSITPNQNLILCGIDQAWREPITTALAQA 476
Cdd:pfam03460 2 PQKDGDYMVRVRVPGGRLTAEQLRALADIAEKYgDGEIRLTTRQNLELHGVPEEDLPELLEELAEA 67
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|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
490-627 |
1.42e-07 |
|
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 51.12 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 490 TAMACPALPLCPLAQTEAErgilPILKRIRAVFN----------KVGIKdsesvvvrITGCPNGCARPYMAELGFVG--- 556
Cdd:pfam01077 6 NVTLCPGAGLCPEELLDTR----PLAKAIEDEFEpdygfpylprKFKIA--------VSGCPNNCVAAHANDIGFVGvwk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1145994699 557 DGPKS-YQIWLGG----TPNqstLAESFMD--KVKLDDIEKVLEPLFTYWN--GTR--QEGESFGSFTNRTGFDKLKEVV 625
Cdd:pfam01077 74 DGGEIgFNILVGGglgrTPG---AAATLKVvpFVPEEDVLEVIEAILEVYRdhGDRenRKKERLKYLIERLGLEKFREEV 150
|
..
gi 1145994699 626 NK 627
Cdd:pfam01077 151 EE 152
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