|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13504 |
PRK13504 |
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit; |
3-569 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
Pssm-ID: 237402 [Multi-domain] Cd Length: 569 Bit Score: 1127.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 3 TKILKAPDGSPSDVERIKEESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRV 82
Cdd:PRK13504 1 HPGPLAVEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 83 RMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSE 162
Cdd:PRK13504 81 RLPGGVITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 163 IHSEVYEWSKKLSDDLLPRTRAYHEIWLDEERVAGTP-EEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVE 241
Cdd:PRK13504 161 LHAEAYEWAKKISDHLLPRTRAYAEIWLDGEKVATFSgTEEEPIYGKTYLPRKFKIAVAVPPDNDVDVYANDLGFVAIAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 242 DGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEE 321
Cdd:PRK13504 241 NGKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTDRKNARLKYTLERVGLDWFKAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 322 LENRLGWSLEEAKPYHFDHNGDRYGWVEGIKDKWHFTLFVEGGRVTDYDDYKLMTGLREIAKVHTGEFRLTANQNLIIAN 401
Cdd:PRK13504 321 VERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLREIAKIHKGDFRLTANQNLIIAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 402 VSSDKKDEISALIEQYGLTDGKHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGLRDQEITIRMTGCP 481
Cdd:PRK13504 401 VPPSDKAKIEALLREYGLIDGVEESPLRRNSMACVALPTCGLAMAEAERYLPSFIDRIEALLAKHGLSDEHIVIRMTGCP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 482 NGCARHALGEIGFIGKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAGIIKA 561
Cdd:PRK13504 481 NGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREPGEGFGDFVIRAGIIRE 560
|
....*....
gi 1732945831 562 TTDGT-NFH 569
Cdd:PRK13504 561 VLDGArDFH 569
|
|
| CysI |
TIGR02041 |
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ... |
17-559 |
0e+00 |
|
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: 960.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 17 ERIKEESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRVRMPGGVSTPEQWLV 96
Cdd:TIGR02041 1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 97 MDDLSQKYGN-GTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSEIHSEVYEWSKKLS 175
Cdd:TIGR02041 81 IDKFAREYTNyGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 176 DDLLPRTRAYHEIWLDEERVAGTpEEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGFNVAIGGG 255
Cdd:TIGR02041 161 EHLLPRTRAYAEIWLDQEKVAGT-EEVEPILGPTYLPRKFKTTVVIPPQNDVDVYANDLGFVAIAENGKLVGFNVLIGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 256 MGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENRLGWSLEEAKP 335
Cdd:TIGR02041 240 LSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTKYTIERMGLDTFKAEVERRAGIKFEPARP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 336 YHFDHNGDRYGWVEGIKDKWHFTLFVEGGRVTDYDDYKLMTGLREIAKVHTGEFRLTANQNLIIANVSSDKKDEISALIE 415
Cdd:TIGR02041 320 YEFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIAKIHKGDFRITANQNLIIAGVPEGGKAKIEKLAR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 416 QYGLTDgkHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGLRDQEITIRMTGCPNGCARHALGEIGFI 495
Cdd:TIGR02041 400 QYGLIN--AVTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMAKHGLSDEEIVLRVTGCPNGCGRAMLAEIGLV 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732945831 496 GKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAGII 559
Cdd:TIGR02041 478 GKAPGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLIRAGII 541
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
13-560 |
0e+00 |
|
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: 620.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 13 PSDVERIKEESDYLR-GTLKEVMLDRISAGIPDDDNRL-MKHHGSYLQDDrdlrnerqkqklePAYQFMLRVRMPGGVST 90
Cdd:COG0155 1 LYKYERIKREDVRSRlGTFAEQLGRFLTGEISEDDFRLrLKFHGLYQQRD-------------PDGAFMLRVRIPGGVLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 91 PEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQS--EIHsEVY 168
Cdd:COG0155 68 PEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDpdELF-DVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 169 EWSKKLSDDLLprtrayheiwldeervagtpeeVEPMYgpLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGF 248
Cdd:COG0155 147 PYAEAISQHLL----------------------GHPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGLVGF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 249 NVAIGGGMGMThgdtatyPQLAKVIG-FCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENR-L 326
Cdd:COG0155 203 NVLVGGGLGRT-------PRLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEyL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 327 GWSLEEA-KPYHFDHNGDRYGWVEGIKD-KWHFTLFVEGGRVTDYDdyklMTGLREIAKVH-TGEFRLTANQNLIIANVS 403
Cdd:COG0155 276 GFPLEPApRPLPAFARWDHLGVHEQKQDgLYYVGLSVENGRITDEQ----LRALADLAERYgSGEIRLTPNQNLILADVP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 404 SDKKDEISALIEQYGLTDgkHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEiiDENGLR-DQEITIRMTGCPN 482
Cdd:COG0155 352 EEDLPALEAALRALGLAT--PPSGLRRDSIACPGLPTCKLAIAESKRLAPALADRLEE--DLDGLHdDEPIRIRISGCPN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 483 GCARHALGEIGFIGKAPGK----YNMYLGAAFDG-SRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAG 557
Cdd:COG0155 428 SCGRHYIADIGLVGKAKKGvveaYQLYLGGGLGGdARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVG 507
|
...
gi 1732945831 558 IIK 560
Cdd:COG0155 508 IEP 510
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
170-325 |
1.82e-47 |
|
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: 162.82 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 170 WSKKLSDDLLPRTRAYHEIWLDEERVAGTPE-EVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGF 248
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEdEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEIGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732945831 249 NVAIGGGMGMTHGDTATYPQLakviGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENR 325
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVV----PFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13504 |
PRK13504 |
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit; |
3-569 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
Pssm-ID: 237402 [Multi-domain] Cd Length: 569 Bit Score: 1127.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 3 TKILKAPDGSPSDVERIKEESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRV 82
Cdd:PRK13504 1 HPGPLAVEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 83 RMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSE 162
Cdd:PRK13504 81 RLPGGVITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 163 IHSEVYEWSKKLSDDLLPRTRAYHEIWLDEERVAGTP-EEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVE 241
Cdd:PRK13504 161 LHAEAYEWAKKISDHLLPRTRAYAEIWLDGEKVATFSgTEEEPIYGKTYLPRKFKIAVAVPPDNDVDVYANDLGFVAIAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 242 DGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEE 321
Cdd:PRK13504 241 NGKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTDRKNARLKYTLERVGLDWFKAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 322 LENRLGWSLEEAKPYHFDHNGDRYGWVEGIKDKWHFTLFVEGGRVTDYDDYKLMTGLREIAKVHTGEFRLTANQNLIIAN 401
Cdd:PRK13504 321 VERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLREIAKIHKGDFRLTANQNLIIAN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 402 VSSDKKDEISALIEQYGLTDGKHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGLRDQEITIRMTGCP 481
Cdd:PRK13504 401 VPPSDKAKIEALLREYGLIDGVEESPLRRNSMACVALPTCGLAMAEAERYLPSFIDRIEALLAKHGLSDEHIVIRMTGCP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 482 NGCARHALGEIGFIGKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAGIIKA 561
Cdd:PRK13504 481 NGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREPGEGFGDFVIRAGIIRE 560
|
....*....
gi 1732945831 562 TTDGT-NFH 569
Cdd:PRK13504 561 VLDGArDFH 569
|
|
| CysI |
TIGR02041 |
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ... |
17-559 |
0e+00 |
|
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: 960.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 17 ERIKEESDYLRGTLKEVMLDRISAGIPDDDNRLMKHHGSYLQDDRDLRNERQKQKLEPAYQFMLRVRMPGGVSTPEQWLV 96
Cdd:TIGR02041 1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 97 MDDLSQKYGN-GTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSEIHSEVYEWSKKLS 175
Cdd:TIGR02041 81 IDKFAREYTNyGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 176 DDLLPRTRAYHEIWLDEERVAGTpEEVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGFNVAIGGG 255
Cdd:TIGR02041 161 EHLLPRTRAYAEIWLDQEKVAGT-EEVEPILGPTYLPRKFKTTVVIPPQNDVDVYANDLGFVAIAENGKLVGFNVLIGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 256 MGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENRLGWSLEEAKP 335
Cdd:TIGR02041 240 LSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTKYTIERMGLDTFKAEVERRAGIKFEPARP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 336 YHFDHNGDRYGWVEGIKDKWHFTLFVEGGRVTDYDDYKLMTGLREIAKVHTGEFRLTANQNLIIANVSSDKKDEISALIE 415
Cdd:TIGR02041 320 YEFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIAKIHKGDFRITANQNLIIAGVPEGGKAKIEKLAR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 416 QYGLTDgkHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGLRDQEITIRMTGCPNGCARHALGEIGFI 495
Cdd:TIGR02041 400 QYGLIN--AVTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMAKHGLSDEEIVLRVTGCPNGCGRAMLAEIGLV 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732945831 496 GKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAGII 559
Cdd:TIGR02041 478 GKAPGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLIRAGII 541
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
13-560 |
0e+00 |
|
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: 620.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 13 PSDVERIKEESDYLR-GTLKEVMLDRISAGIPDDDNRL-MKHHGSYLQDDrdlrnerqkqklePAYQFMLRVRMPGGVST 90
Cdd:COG0155 1 LYKYERIKREDVRSRlGTFAEQLGRFLTGEISEDDFRLrLKFHGLYQQRD-------------PDGAFMLRVRIPGGVLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 91 PEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQS--EIHsEVY 168
Cdd:COG0155 68 PEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDpdELF-DVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 169 EWSKKLSDDLLprtrayheiwldeervagtpeeVEPMYgpLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGF 248
Cdd:COG0155 147 PYAEAISQHLL----------------------GHPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGLVGF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 249 NVAIGGGMGMThgdtatyPQLAKVIG-FCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENR-L 326
Cdd:COG0155 203 NVLVGGGLGRT-------PRLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEyL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 327 GWSLEEA-KPYHFDHNGDRYGWVEGIKD-KWHFTLFVEGGRVTDYDdyklMTGLREIAKVH-TGEFRLTANQNLIIANVS 403
Cdd:COG0155 276 GFPLEPApRPLPAFARWDHLGVHEQKQDgLYYVGLSVENGRITDEQ----LRALADLAERYgSGEIRLTPNQNLILADVP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 404 SDKKDEISALIEQYGLTDgkHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEiiDENGLR-DQEITIRMTGCPN 482
Cdd:COG0155 352 EEDLPALEAALRALGLAT--PPSGLRRDSIACPGLPTCKLAIAESKRLAPALADRLEE--DLDGLHdDEPIRIRISGCPN 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 483 GCARHALGEIGFIGKAPGK----YNMYLGAAFDG-SRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFGDFVIRAG 557
Cdd:COG0155 428 SCGRHYIADIGLVGKAKKGvveaYQLYLGGGLGGdARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVG 507
|
...
gi 1732945831 558 IIK 560
Cdd:COG0155 508 IEP 510
|
|
| PLN00178 |
PLN00178 |
sulfite reductase |
14-557 |
7.39e-178 |
|
sulfite reductase
Pssm-ID: 177773 [Multi-domain] Cd Length: 623 Bit Score: 516.23 E-value: 7.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 14 SDVERIKEESDYLRGTLKEVMLDRiSAGIPDDDNRLMKHHGSYLQDDRDLRNERqkqklepAYQFMLRVRMPGGVSTPEQ 93
Cdd:PLN00178 54 SKVEIIKENSNFLRHPLNEELATE-APNINEDAVQLIKFHGSYQQDNREKRGGK-------AYQFMLRTKQPAGKVPNRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 94 WLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSEIHSEVYEWSKK 173
Cdd:PLN00178 126 YLVMDDLADEFGIGTLRLTTRQTFQLHGVLKKDLKTVMSSIIKNMGSTLGACGDVNRNVLAPAAPFARKDYLFAQELAKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 174 LSDDLLPRTRAYHEIWLDEERVAGT-PEEV-----------------EPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLG 235
Cdd:PLN00178 206 IAALLAPQSGAYYDIWVDGEKIMSAePPEVtkarndnshgtnfedspEPIYGTQFLPRKFKIAVTVPGDNSVDILTNDIG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 236 FIAIV-EDGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLG 314
Cdd:PLN00178 286 VVVVSdEAGEPQGYNIYVGGGMGRTHRNETTFPRLADPLGYVPKEDILYAVKAIVATQRDYGRRDDRKQSRMKYLVHSWG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 315 LETVKEELENRLGWSLEEAKP---YHFDhngDRYGWVEGIKDKWHFTLFVEGGRVTDyddyKLMTGLREIAKVHTGEFRL 391
Cdd:PLN00178 366 IEKFRSVVEQYYGKKFEPFRElpeWEFK---SYLGWHEQGDGKLFYGVHVDNGRIKG----EAKKALREVIEKYNLPVRL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 392 TANQNLIIANVSSDKKDEISALIEQYGLTDGKHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGLR-D 470
Cdd:PLN00178 439 TPNQNLILCDIRPAWKEPITAALAAAGLLEPEEVDPLNRTAMACPALPLCPLAITEAERGIPDILKRVRAMFNKVGLKyD 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 471 QEITIRMTGCPNGCARHALGEIGFIGKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYAKERDEGEHFG 550
Cdd:PLN00178 519 ESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPNQTRLAEPFMDKVKVDDLEKVLEPLFYMWKQQRQEKESFG 598
|
....*..
gi 1732945831 551 DFVIRAG 557
Cdd:PLN00178 599 DFTNRVG 605
|
|
| sir |
TIGR02042 |
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ... |
8-557 |
1.83e-160 |
|
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: 470.10 E-value: 1.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 8 APDGSPSDVERIKEESDYLRGTLKEVMLDRiSAGIPDDDNRLMKHHGSYLQDDRDLRNERQkqklEPAYQFMLRVRMPGG 87
Cdd:TIGR02042 1 AKPQKRSKVEILKERSNFLREPLNEQLLEE-ATHFNEDAVQILKFHGSYQQDNRDNRGKGQ----EKDYQFMLRTKNPGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 88 VSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMCASNPYQSEIHsev 167
Cdd:TIGR02042 76 YVPPQLYLTLDDLADEYGNGTLRATTRQTFQLHGILKKNLKTVISTIVKNLGSTLGACGDLNRNVMAPPAPFRKRPE--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 168 YEWSKKLSD---DLL-PRTRAYHEIWLDEERVA-----------------GT--PEEVEPMYGPLYLPRKFKIGIAVPPS 224
Cdd:TIGR02042 153 YEFAREYADniaDLLtPQSGAYYELWLDGEKVMsaepdpevvaarndnshGTnfADSPEPLYGTQYLPRKFKIAVTVPGD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 225 NDIDVFSQDLGFIAIV-EDGKLIGFNVAIGGGMGMTHGDTATYPQLAKVIGFCRPEQLYDIAEKTITIQRDYGNRSVRKN 303
Cdd:TIGR02042 233 NSIDLFTQDIGLVVVSnERGELEGFNIYVGGGMGRTHNKEETFARLADPLGYVPKEDIYYAVKAIVATQRDYGDRDDRRH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 304 ARFKYTVDRLGLETVKEELENRLGWSLE---EAKPYHFDhngDRYGWVEGIKDKWHFTLFVEGGRVTDYDDYKLMTGLRE 380
Cdd:TIGR02042 313 ARMKYLISDWGIEKFREVVEQYFGKKIApvrELPEFEYK---DYLGWHEQGDGKWFLGLHIDSGRVKDDGNWQLKKALRE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 381 IAKVHTGEFRLTANQNLIIANVSSDKKDEISALIEQYGLTDGKHHSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVE 460
Cdd:TIGR02042 390 IVEKYNLPVRLTPNQNIILYDIQPEWKRAITTVLAQRGVLQPEAIDPLNRYAMACPALPTCGLAITESERAIPGILKRIR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 461 EIIDENGLRDQEITIRMTGCPNGCARHALGEIGFIGKAPGKYNMYLGAAFDGSRLSKMYRENIGEEDILSELRVLLSRYA 540
Cdd:TIGR02042 470 ALLEKVGLPDEHFVVRMTGCPNGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLEKVLEPLFVHFK 549
|
570
....*....|....*..
gi 1732945831 541 KERDEGEHFGDFVIRAG 557
Cdd:TIGR02042 550 QSRQSGESFGDFCDRVG 566
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
170-325 |
1.82e-47 |
|
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: 162.82 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 170 WSKKLSDDLLPRTRAYHEIWLDEERVAGTPE-EVEPMYGPLYLPRKFKIGIAVPPSNDIDVFSQDLGFIAIVEDGKLIGF 248
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEdEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEIGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732945831 249 NVAIGGGMGMTHGDTATYPQLakviGFCRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDRLGLETVKEELENR 325
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVV----PFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
77-550 |
1.26e-46 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 170.96 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 77 QFMLRVRMPGGVSTPEQWLVMDDLSQKYG-NGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVmcA 155
Cdd:PRK09566 65 KFMLRLRVPNGILTSEQLRVLASIVQRYGdDGSADITTRQNLQLRGILLEDLPEILNRLKAVGLTSVQSGMDNVRNI--T 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 156 SNPYQSEIHSEVY---EWSKKLSDDLlprtrayheiwldEERVAGTPEEVEpmygplyLPRKFKIGIAVPPSNDIDVFSQ 232
Cdd:PRK09566 143 GSPVAGIDPDELIdtrPLTQKLQDML-------------TNNGEGNPEFSN-------LPRKFNIAIAGGRDNSVHAEIN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 233 DLGFIAIVEDGKLiGFNVAIGGGMGMTHGDTATyPQLAKVigfcRPEQLYDIAEKTITIQRDYGNRSVRKNARFKYTVDR 312
Cdd:PRK09566 203 DIAFVPAYKDGVL-GFNVLVGGFFSSQRCAYAI-PLNAWV----KPDEVVRLCRAILEVYRDNGLRANRQKGRLMWLIDE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 313 LGLETVKEELENRLGWSLEEAKPYHF--DHNGDRYGWVEGIKDKWHFT-LFVEGGRVTDYDDYKLMTglreIAKVH-TGE 388
Cdd:PRK09566 277 WGIEKFRAAVEAQFGPPLLTAAPGDEidWEKRDHIGVHPQKQAGLNYVgLHVPVGRLYAEDMFELAR----LAEVYgSGE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 389 FRLTANQNLIIANVSSDKKDEISA--LIEQYGLtdgkHHSALRRSSMACVALPTCGLAMAEA-ERYLptlldKVEEIIDE 465
Cdd:PRK09566 353 IRLTVEQNVIIPNIPDENLETFLAepLLQKFSL----EPGPLARGLVSCTGNQYCNFALIETkNRAL-----ALAKELDA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 466 NGLRDQEITIRMTGCPNGCARHALGEIGFIG---KAPGK----YNMYLGaafdGS-----RLSKMYRENIGEEDILSELR 533
Cdd:PRK09566 424 ELDLPQPVRIHWTGCPNSCGQPQVADIGLMGtkaRKNGKtvegVDIYMG----GKvgkdaKLGECVQKGIPCEDLKPVLK 499
|
490
....*....|....*..
gi 1732945831 534 VLLSryakerdegEHFG 550
Cdd:PRK09566 500 DLLI---------EQFG 507
|
|
| nirA |
PRK09567 |
NirA family protein; |
78-555 |
1.75e-43 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 163.65 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 78 FMLRVRMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGIlkwnMKKTIQTIHSGLLD----TIAACGDVNRNVm 153
Cdd:PRK09567 117 YMCRLRIPNGILTHWQFAGLADLADRHGGGYSHVTTRANLQLREI----PPEHAVPVLEGLVDlgltARGSGADNIRNV- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 154 cASNPYQSEIHSEVYewskklsdDLLPRTRAYHEiWLDEERVagtpeevepMYGplyLPRKFKI----GIAVPPSNDidv 229
Cdd:PRK09567 192 -TGSPTAGIDPQELL--------DTRPYAREWHH-HILNDRS---------LYG---LPRKFNVafdgGGRIATLED--- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 230 fSQDLGFIAI-VEDGKL----IGFNVAIGGGMGmtHGDTATYpqlAKVIgfCRPEQLYDIAEKTITIQRDYGNRSVRKNA 304
Cdd:PRK09567 247 -TNDIGFQAVrVLEGAGvapgVYFRLVLGGITG--HKDFARD---TGVL--LRPEEATAVADAIVRVFIENGDRTNRKKA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 305 RFKYTVDRLGLETVKEELENRLGWSLEEAKPYHFDHNG--DRYGWVeGIKDKWHFTLFVEG-----GRVTDyddyKLMTG 377
Cdd:PRK09567 319 RLKYVLDAWGFDKFLEAVEEKLGRPLTRVPAEAVAPRPaaDRFAHV-GVHPQKQPGLNWIGvvlpvGRLTT----DQMRG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 378 LREIAKVH-TGEFRLTANQNLIIANVSSDKKDEISALIEQYGLTDGKHHsaLRRSSMACVALPTCGLAMAEAERYLPTLL 456
Cdd:PRK09567 394 LAKIAARYgDGEIRLTVWQNLLISGVPDADVAAVEAAIEALGLTTEASS--IRAGLVACTGNAGCKFAAADTKGHALAIA 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 457 DKVEEIIDenglRDQEITIRMTGCPNGCARHALGEIGFIG-KAPGK-------YNMYLGAAF-DGSRLSKMYRENIGEED 527
Cdd:PRK09567 472 DYCEPRVA----LDQPVNIHLTGCHHSCAQHYIGDIGLIGaKVAVSegdtvegYHIVVGGGFgEDAAIGREVFRDVKAED 547
|
490 500
....*....|....*....|....*....
gi 1732945831 528 ILSELRVLLSRYAKERDE-GEHFGDFVIR 555
Cdd:PRK09567 548 APRLVERLLRAYLAHRQGpDETFQAFTRR 576
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
77-543 |
4.89e-30 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 124.51 E-value: 4.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 77 QFMLRVRMPGGVSTPEQWLVMDDLSQKYG-NGTLKLTTRETFQMHGILKWNMKKTIQTIHSGLLDTIAACGDVNRNVMca 155
Cdd:PLN02431 136 RFMMRLKLPNGVTTSAQTRYLASVIEKYGeDGCADVTTRQNWQIRGVVLPDVPAILKGLEEVGLTSLQSGMDNVRNPV-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 156 SNPYQS----EIhSEVYEWSKKLSDDLLPRTRayheiwldeervaGTPEEVEpmygplyLPRKFKIGIavppSNDIDVFS 231
Cdd:PLN02431 214 GNPLAGidphEI-VDTRPYTNLLSDYITNNGR-------------GNPEITN-------LPRKWNVCV----VGSHDLFE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 232 Q----DLGFIAIVEDGKLiGFNVAIGGGMGMTHGDTATyPQLAKVIGfcrpEQLYDIAEKTITIQRDYGNRSVRKNARFK 307
Cdd:PLN02431 269 HphinDLAYMPATKDGRF-GFNLLVGGFFSPKRCAEAI-PLDAWVPA----DDVVPLCKAILEAFRDLGTRGNRQKTRMM 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 308 YTVDRLGLETVKEELENRL-GWSLEEAKPYHF-DHNGDRYGWV-------EGIKdkwHFTLFVEGGRVTDYDdyklmtgL 378
Cdd:PLN02431 343 WLIDELGVEGFRSEVEKRMpNGELERAASEDLvDKKWERRDYLgvhpqkqEGLS---YVGLHVPVGRLQAAD-------M 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 379 REIAKVH----TGEFRLTANQNLIIANVSSDKKDEISA--LIEQYGLTDGKhhsaLRRSSMACVALPTCGLAMAEAERYL 452
Cdd:PLN02431 413 DELARLAdeygSGELRLTVEQNIIIPNVPNSKVEALLAepLLQRFSPNPGL----LLKGLVACTGNQFCGQAIIETKARA 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 453 PTLLDKVEEIIDenglRDQEITIRMTGCPNGCARHALGEIGFIG----KAPGK----YNMYLGAAF-DGSRLSKMYRENI 523
Cdd:PLN02431 489 LKVTEELERLVE----VPRPVRMHWTGCPNSCGQVQVADIGFMGcmarDENGKavegADIFVGGRVgSDSHLAEEYKKGV 564
|
490 500
....*....|....*....|..
gi 1732945831 524 GEEDILSELR-VLLSRY-AKER 543
Cdd:PLN02431 565 PCDELVPVVAdILIEEFgAKER 586
|
|
| CobG |
TIGR02435 |
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated ... |
79-500 |
5.45e-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: 82.92 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 79 MLRVRMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGILKwNMKKTIQTIHS-GLLDTIAACGDVnRNVMCASn 157
Cdd:TIGR02435 19 LVRVRLPGGRLTPAQAIGLADLAERLGNGIIEVTARGNLQLRGLTA-DHDALSQALLAaGLGAAGAAADDI-RNIEVSP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 158 pyqseihsevyewSKKLSDDLLPRTRAYHEIWLDEERVAGTPEEvepmygplyLPRKFKIGIAVPPSNDIDVFSQDLGFI 237
Cdd:TIGR02435 96 -------------LAGIDPGEIADTRPLAAELRAALENERALLE---------LPPKFSVAIDGGGRLVLLGDTADVRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 238 AiVEDGKLIGFNVAIGGgmgmthgDTATYPQLAKVIGFCRPEQLYDIAEKTITiqrdygnrsVRKNARFKYTVDRLG--- 314
Cdd:TIGR02435 154 A-LTTGAGVAWVVSLAG-------ISTSARSLVTVAPDAAVPVAVALLRVFVE---------LGGAARGRDLDDAFLfal 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 315 -LETVKEELENRLGWSLEEAKPYHFDHNGdRYGWVEGIKDKWHFTLFVEGGRVTdyddYKLMTGLREIAKVH-TGEFRLT 392
Cdd:TIGR02435 217 aLELVEDSRPLIPDAAEGEAPRPAVDAAA-PLGLHPQGDAGVTLGAGLALGQLT----AAQLRGLAQLAQALgDGDLRLT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 393 ANQNLIIANVSSDKKDEISALIEQYGL-TDGkhhSALRRSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDenglrdq 471
Cdd:TIGR02435 292 PWRALLVLGLPPERADAAQRALAALGLvTSA---SDPRARIIACTGAPGCASALADTRADAEALAAYCEPTAP------- 361
|
410 420
....*....|....*....|....*....
gi 1732945831 472 eITIRMTGCPNGCARHALGEIGFIGKAPG 500
Cdd:TIGR02435 362 -ITVHLSGCAKGCAHPGPAAITLVAAGAG 389
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
78-122 |
1.19e-12 |
|
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: 62.93 E-value: 1.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1732945831 78 FMLRVRMPGGVSTPEQWLVMDDLSQKYGNGTLKLTTRETFQMHGI 122
Cdd:pfam03460 8 YMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGV 52
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
354-417 |
2.88e-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: 56.38 E-value: 2.88e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732945831 354 KWHFTLFVEGGRVTdyddYKLMTGLREIAKVH-TGEFRLTANQNLIIANVSSDKKDEISALIEQY 417
Cdd:pfam03460 7 DYMVRVRVPGGRLT----AEQLRALADIAEKYgDGEIRLTTRQNLELHGVPEEDLPELLEELAEA 67
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|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
430-558 |
1.17e-03 |
|
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: 39.56 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732945831 430 RSSMACVALPTCGLAMAEAERYLPTLLDKVEEIIDENGL-RDQEITIrmTGCPNGCARHALGEIGFIG--KAPGK--YNM 504
Cdd:pfam01077 5 RNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLpRKFKIAV--SGCPNNCVAAHANDIGFVGvwKDGGEigFNI 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732945831 505 YLGAAFdGSRLSK----MYRENIGEEDILSELRVLLSRYAKERDEG----EHFGDFVIRAGI 558
Cdd:pfam01077 83 LVGGGL-GRTPGAaatlKVVPFVPEEDVLEVIEAILEVYRDHGDREnrkkERLKYLIERLGL 143
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