|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13504 |
PRK13504 |
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit; |
5-569 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
Pssm-ID: 237402 [Multi-domain] Cd Length: 569 Bit Score: 1132.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 5 HPGPLVVEGKLTDAERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRC 84
Cdd:PRK13504 1 HPGPLAVEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 85 RLPGGVITTKQWQAIDKFAGENTiYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYES 164
Cdd:PRK13504 81 RLPGGVITPQQWLALDKLADEYG-NGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 165 QLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVAT---TDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIA 241
Cdd:PRK13504 160 RLHAEAYEWAKKISDHLLPRTRAYAEIWLDGEKVATfsgTEEEPIYGKTYLPRKFKIAVAVPPDNDVDVYANDLGFVAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 242 ENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKA 321
Cdd:PRK13504 240 ENGKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTDRKNARLKYTLERVGLDWFKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 322 EVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIHKGDFRITANQNLIIA 401
Cdd:PRK13504 320 EVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLREIAKIHKGDFRLTANQNLIIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 402 GVPESEKAKIEKIAKESGLMNAV--TPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGC 479
Cdd:PRK13504 400 NVPPSDKAKIEALLREYGLIDGVeeSPLRRNSMACVALPTCGLAMAEAERYLPSFIDRIEALLAKHGLSDEHIVIRMTGC 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 480 PNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIR 559
Cdd:PRK13504 480 PNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREPGEGFGDFVIRAGIIR 559
|
570
....*....|
gi 447213450 560 PVLDPARDLW 569
Cdd:PRK13504 560 EVLDGARDFH 569
|
|
| CysI |
TIGR02041 |
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ... |
19-558 |
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: 1067.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 19 ERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQA 98
Cdd:TIGR02041 1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 99 IDKFAGENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKIS 178
Cdd:TIGR02041 81 IDKFAREYTNYGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 179 EHLLPRTRAYAEIWLDQEKVATTDE-EPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGL 257
Cdd:TIGR02041 161 EHLLPRTRAYAEIWLDQEKVAGTEEvEPILGPTYLPRKFKTTVVIPPQNDVDVYANDLGFVAIAENGKLVGFNVLIGGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 258 SIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPY 337
Cdd:TIGR02041 241 SMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTKYTIERMGLDTFKAEVERRAGIKFEPARPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 338 EFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKE 417
Cdd:TIGR02041 321 EFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIAKIHKGDFRITANQNLIIAGVPEGGKAKIEKLARQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 418 SGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKA 497
Cdd:TIGR02041 401 YGLINAVTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMAKHGLSDEEIVLRVTGCPNGCGRAMLAEIGLVGKA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447213450 498 PGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGII 558
Cdd:TIGR02041 481 PGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLIRAGII 541
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
15-566 |
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: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 15 LTDAERMKLESNYLR-GTIAEDLNDGLTGGFKGDNF-LLIRFHGMYQQDDrdiraeraeqklePRHAMLLRCRLPGGVIT 92
Cdd:COG0155 1 LYKYERIKREDVRSRlGTFAEQLGRFLTGEISEDDFrLRLKFHGLYQQRD-------------PDGAFMLRVRIPGGVLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 93 TKQWQAIDKFAGENTiYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQL-HAEAY 171
Cdd:COG0155 68 PEQLRALADIAREYG-RGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDPDeLFDVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 172 EWAKKISEHLLprtrayaeiwldqekvattdEEPILgqTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNL 251
Cdd:COG0155 147 PYAEAISQHLL--------------------GHPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGLVGFNV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 252 LVGGGLSIEHgnkktyaRTASEFG-YLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERR-AGI 329
Cdd:COG0155 205 LVGGGLGRTP-------RLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEyLGF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 330 KFEPI-RPYEFTGRGDRIGWVKGI-DDNWHLTLFIENGRILDYPgrplKTGLLEIAKIH-KGDFRITANQNLIIAGVPES 406
Cdd:COG0155 278 PLEPApRPLPAFARWDHLGVHEQKqDGLYYVGLSVENGRITDEQ----LRALADLAERYgSGEIRLTPNQNLILADVPEE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 407 EKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDnlmAKHG--VSDEHIVMRVTGCPNGCG 484
Cdd:COG0155 354 DLPALEAALRALGLATPPSGLRRDSIACPGLPTCKLAIAESKRLAPALADRLE---EDLDglHDDEPIRIRISGCPNSCG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 485 RAMLAEVGLVGKAP-GR---YNLHLGGNRIG-TRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGI-- 557
Cdd:COG0155 431 RHYIADIGLVGKAKkGVveaYQLYLGGGLGGdARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIep 510
|
....*....
gi 447213450 558 IRPVLDPAR 566
Cdd:COG0155 511 LKELLYAAA 519
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
173-326 |
9.97e-48 |
|
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: 163.60 E-value: 9.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 173 WAKKISEHLLPRTRAYAEIWLDQEKVATT---DEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGF 249
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAiedEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEIGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447213450 250 NLLVGGGLSIEHGNKKTYARtaseFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERR 326
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKV----VPFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13504 |
PRK13504 |
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit; |
5-569 |
0e+00 |
|
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
Pssm-ID: 237402 [Multi-domain] Cd Length: 569 Bit Score: 1132.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 5 HPGPLVVEGKLTDAERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRC 84
Cdd:PRK13504 1 HPGPLAVEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 85 RLPGGVITTKQWQAIDKFAGENTiYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYES 164
Cdd:PRK13504 81 RLPGGVITPQQWLALDKLADEYG-NGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 165 QLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVAT---TDEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIA 241
Cdd:PRK13504 160 RLHAEAYEWAKKISDHLLPRTRAYAEIWLDGEKVATfsgTEEEPIYGKTYLPRKFKIAVAVPPDNDVDVYANDLGFVAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 242 ENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKA 321
Cdd:PRK13504 240 ENGKLVGFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTDRKNARLKYTLERVGLDWFKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 322 EVERRAGIKFEPIRPYEFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIHKGDFRITANQNLIIA 401
Cdd:PRK13504 320 EVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLREIAKIHKGDFRLTANQNLIIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 402 GVPESEKAKIEKIAKESGLMNAV--TPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGC 479
Cdd:PRK13504 400 NVPPSDKAKIEALLREYGLIDGVeeSPLRRNSMACVALPTCGLAMAEAERYLPSFIDRIEALLAKHGLSDEHIVIRMTGC 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 480 PNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGIIR 559
Cdd:PRK13504 480 PNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLLGRWAKEREPGEGFGDFVIRAGIIR 559
|
570
....*....|
gi 447213450 560 PVLDPARDLW 569
Cdd:PRK13504 560 EVLDGARDFH 569
|
|
| CysI |
TIGR02041 |
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ... |
19-558 |
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: 1067.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 19 ERMKLESNYLRGTIAEDLNDGLTGGFKGDNFLLIRFHGMYQQDDRDIRAERAEQKLEPRHAMLLRCRLPGGVITTKQWQA 98
Cdd:TIGR02041 1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 99 IDKFAGENTIYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQLHAEAYEWAKKIS 178
Cdd:TIGR02041 81 IDKFAREYTNYGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 179 EHLLPRTRAYAEIWLDQEKVATTDE-EPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNLLVGGGL 257
Cdd:TIGR02041 161 EHLLPRTRAYAEIWLDQEKVAGTEEvEPILGPTYLPRKFKTTVVIPPQNDVDVYANDLGFVAIAENGKLVGFNVLIGGGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 258 SIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERRAGIKFEPIRPY 337
Cdd:TIGR02041 241 SMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTKYTIERMGLDTFKAEVERRAGIKFEPARPY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 338 EFTGRGDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKE 417
Cdd:TIGR02041 321 EFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIAKIHKGDFRITANQNLIIAGVPEGGKAKIEKLARQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 418 SGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAKHGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKA 497
Cdd:TIGR02041 401 YGLINAVTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMAKHGLSDEEIVLRVTGCPNGCGRAMLAEIGLVGKA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447213450 498 PGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGII 558
Cdd:TIGR02041 481 PGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERKPGEGFGDFLIRAGII 541
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
15-566 |
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: 581.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 15 LTDAERMKLESNYLR-GTIAEDLNDGLTGGFKGDNF-LLIRFHGMYQQDDrdiraeraeqklePRHAMLLRCRLPGGVIT 92
Cdd:COG0155 1 LYKYERIKREDVRSRlGTFAEQLGRFLTGEISEDDFrLRLKFHGLYQQRD-------------PDGAFMLRVRIPGGVLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 93 TKQWQAIDKFAGENTiYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSNPYESQL-HAEAY 171
Cdd:COG0155 68 PEQLRALADIAREYG-RGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDPDeLFDVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 172 EWAKKISEHLLprtrayaeiwldqekvattdEEPILgqTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGFNL 251
Cdd:COG0155 147 PYAEAISQHLL--------------------GHPEY--TYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKEDGLVGFNV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 252 LVGGGLSIEHgnkktyaRTASEFG-YLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERR-AGI 329
Cdd:COG0155 205 LVGGGLGRTP-------RLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNRKKARLKYLVDDLGVEKFREEVEEEyLGF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 330 KFEPI-RPYEFTGRGDRIGWVKGI-DDNWHLTLFIENGRILDYPgrplKTGLLEIAKIH-KGDFRITANQNLIIAGVPES 406
Cdd:COG0155 278 PLEPApRPLPAFARWDHLGVHEQKqDGLYYVGLSVENGRITDEQ----LRALADLAERYgSGEIRLTPNQNLILADVPEE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 407 EKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDnlmAKHG--VSDEHIVMRVTGCPNGCG 484
Cdd:COG0155 354 DLPALEAALRALGLATPPSGLRRDSIACPGLPTCKLAIAESKRLAPALADRLE---EDLDglHDDEPIRIRISGCPNSCG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 485 RAMLAEVGLVGKAP-GR---YNLHLGGNRIG-TRIPRMYKENITEPEILASLDELIGRWAKEREAGEGFGDFTVRAGI-- 557
Cdd:COG0155 431 RHYIADIGLVGKAKkGVveaYQLYLGGGLGGdARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIep 510
|
....*....
gi 447213450 558 IRPVLDPAR 566
Cdd:COG0155 511 LKELLYAAA 519
|
|
| PLN00178 |
PLN00178 |
sulfite reductase |
6-556 |
1.29e-154 |
|
sulfite reductase
Pssm-ID: 177773 [Multi-domain] Cd Length: 623 Bit Score: 456.91 E-value: 1.29e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 6 PGPLVVEGKLTDAERMKLESNYLRGTIAEDLNDGLTGgFKGDNFLLIRFHGMYQQDDRDIRAERAEQkleprhaMLLRCR 85
Cdd:PLN00178 44 KKPTTEPPKRSKVEIIKENSNFLRHPLNEELATEAPN-INEDAVQLIKFHGSYQQDNREKRGGKAYQ-------FMLRTK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 86 LPGGVITTKQWQAIDKFAGENTIyGSIRLTNRQTFQFHGILKKNVKPVHQ-MLHSVGlDALATANDMNRNVLCTSNPYES 164
Cdd:PLN00178 116 QPAGKVPNRLYLVMDDLADEFGI-GTLRLTTRQTFQLHGVLKKDLKTVMSsIIKNMG-STLGACGDVNRNVLAPAAPFAR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 165 QLHAEAYEWAKKISEHLLPRTRAYAEIWLDQEKVATTDE--------------------EPILGQTYLPRKFKTTVVIPP 224
Cdd:PLN00178 194 KDYLFAQELAKNIAALLAPQSGAYYDIWVDGEKIMSAEPpevtkarndnshgtnfedspEPIYGTQFLPRKFKIAVTVPG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 225 QNDIDLHANDMNFVAIA-ENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRK 303
Cdd:PLN00178 274 DNSVDILTNDIGVVVVSdEAGEPQGYNIYVGGGMGRTHRNETTFPRLADPLGYVPKEDILYAVKAIVATQRDYGRRDDRK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 304 NAKTKYTLERVGVETFKAEVERRAGIKFEPIRP---YEFTgrgDRIGWVKGIDDNWHLTLFIENGRIldypGRPLKTGLL 380
Cdd:PLN00178 354 QSRMKYLVHSWGIEKFRSVVEQYYGKKFEPFRElpeWEFK---SYLGWHEQGDGKLFYGVHVDNGRI----KGEAKKALR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 381 EIAKIHKGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNA--VTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNI 458
Cdd:PLN00178 427 EVIEKYNLPVRLTPNQNLILCDIRPAWKEPITAALAAAGLLEPeeVDPLNRTAMACPALPLCPLAITEAERGIPDILKRV 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 459 DNLMAKHGVS-DEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGR 537
Cdd:PLN00178 507 RAMFNKVGLKyDESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPNQTRLAEPFMDKVKVDDLEKVLEPLFYM 586
|
570
....*....|....*....
gi 447213450 538 WAKEREAGEGFGDFTVRAG 556
Cdd:PLN00178 587 WKQQRQEKESFGDFTNRVG 605
|
|
| sir |
TIGR02042 |
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ... |
14-556 |
2.58e-144 |
|
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: 428.89 E-value: 2.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 14 KLTDAERMKLESNYLRGTIAEDLNDGLTGgFKGDNFLLIRFHGMYQQDDRDIRAERAEQKleprHAMLLRCRLPGGVITT 93
Cdd:TIGR02042 5 KRSKVEILKERSNFLREPLNEQLLEEATH-FNEDAVQILKFHGSYQQDNRDNRGKGQEKD----YQFMLRTKNPGGYVPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 94 KQWQAIDKFAGENTIyGSIRLTNRQTFQFHGILKKNVKPV-HQMLHSVGlDALATANDMNRNVLCTSNPYESQLHAE-AY 171
Cdd:TIGR02042 80 QLYLTLDDLADEYGN-GTLRATTRQTFQLHGILKKNLKTViSTIVKNLG-STLGACGDLNRNVMAPPAPFRKRPEYEfAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 172 EWAKKISEHLLPRTRAYAEIWLDQEKVATTDE---------------------EPILGQTYLPRKFKTTVVIPPQNDIDL 230
Cdd:TIGR02042 158 EYADNIADLLTPQSGAYYELWLDGEKVMSAEPdpevvaarndnshgtnfadspEPLYGTQYLPRKFKIAVTVPGDNSIDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 231 HANDMNFVAIA-ENGKLVGFNLLVGGGLSIEHGNKKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKY 309
Cdd:TIGR02042 238 FTQDIGLVVVSnERGELEGFNIYVGGGMGRTHNKEETFARLADPLGYVPKEDIYYAVKAIVATQRDYGDRDDRRHARMKY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 310 TLERVGVETFKAEVERRAGIKFEPIR---PYEFTgrgDRIGWVKGIDDNWHLTLFIENGRILDYPGRPLKTGLLEIAKIH 386
Cdd:TIGR02042 318 LISDWGIEKFREVVEQYFGKKIAPVRelpEFEYK---DYLGWHEQGDGKWFLGLHIDSGRVKDDGNWQLKKALREIVEKY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 387 KGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMN--AVTPQRENSMACVSFPTCPLAMAEAERFLPSFIDNIDNLMAK 464
Cdd:TIGR02042 395 NLPVRLTPNQNIILYDIQPEWKRAITTVLAQRGVLQpeAIDPLNRYAMACPALPTCGLAITESERAIPGILKRIRALLEK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 465 HGVSDEHIVMRVTGCPNGCGRAMLAEVGLVGKAPGRYNLHLGGNRIGTRIPRMYKENITEPEILASLDELIGRWAKEREA 544
Cdd:TIGR02042 475 VGLPDEHFVVRMTGCPNGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLEKVLEPLFVHFKQSRQS 554
|
570
....*....|..
gi 447213450 545 GEGFGDFTVRAG 556
Cdd:TIGR02042 555 GESFGDFCDRVG 566
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
173-326 |
9.97e-48 |
|
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: 163.60 E-value: 9.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 173 WAKKISEHLLPRTRAYAEIWLDQEKVATT---DEEPILGQTYLPRKFKTTVVIPPQNDIDLHANDMNFVAIAENGKLVGF 249
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAiedEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKDGGEIGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447213450 250 NLLVGGGLSIEHGNKKTYARtaseFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGVETFKAEVERR 326
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKV----VPFVPEEDVLEVIEAILEVYRDHGDRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
81-543 |
7.80e-35 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 138.76 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 81 LLRCRLPGGVITTKQWQ----AIDKFaGEntiYGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVl 156
Cdd:PLN02431 138 MMRLKLPNGVTTSAQTRylasVIEKY-GE---DGCADVTTRQNWQIRGVVLPDVPAILKGLEEVGLTSLQSGMDNVRNP- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 157 cTSNPYESqlhaeayewakkISEHLLPRTRAYAEIwLDQEKVATTDEEPILgqTYLPRKFKTTVVIPPQNDIDLHANDMN 236
Cdd:PLN02431 213 -VGNPLAG------------IDPHEIVDTRPYTNL-LSDYITNNGRGNPEI--TNLPRKWNVCVVGSHDLFEHPHINDLA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 237 FVAIAENGKlVGFNLLVGGGLSIehgnkKTYARTASEFGYLPLEHTLAVAEAVVTTQRDWGNRTDRKNAKTKYTLERVGV 316
Cdd:PLN02431 277 YMPATKDGR-FGFNLLVGGFFSP-----KRCAEAIPLDAWVPADDVVPLCKAILEAFRDLGTRGNRQKTRMMWLIDELGV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 317 ETFKAEVERRAGikfepirpyefTGRGDRIGWVKGIDDNWHLTLFI------ENGriLDYPGRPLKTGLL------EIAK 384
Cdd:PLN02431 351 EGFRSEVEKRMP-----------NGELERAASEDLVDKKWERRDYLgvhpqkQEG--LSYVGLHVPVGRLqaadmdELAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 385 IH----KGDFRITANQNLIIAGVPESekaKIEKIAKESgLMNAVTPQ----RENSMACVSFPTCPLAMAEAERFLPSFID 456
Cdd:PLN02431 418 LAdeygSGELRLTVEQNIIIPNVPNS---KVEALLAEP-LLQRFSPNpgllLKGLVACTGNQFCGQAIIETKARALKVTE 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 457 NIDNLMAkhgvSDEHIVMRVTGCPNGCGRAMLAEVGLVG--------KAPGRYNLHLGGnRIG--TRIPRMYKENITEPE 526
Cdd:PLN02431 494 ELERLVE----VPRPVRMHWTGCPNSCGQVQVADIGFMGcmardengKAVEGADIFVGG-RVGsdSHLAEEYKKGVPCDE 568
|
490
....*....|....*....
gi 447213450 527 ILASLDE-LIGRW-AKERE 543
Cdd:PLN02431 569 LVPVVADiLIEEFgAKERE 587
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
81-507 |
8.92e-33 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 131.67 E-value: 8.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 81 LLRCRLPGGVITTKQWQAIDKFA---GENtiyGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVlc 157
Cdd:PRK09566 67 MLRLRVPNGILTSEQLRVLASIVqryGDD---GSADITTRQNLQLRGILLEDLPEILNRLKAVGLTSVQSGMDNVRNI-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 158 TSNPYESQLHAEAY---EWAKKISEHLlprtrayaeiwldqekvaTTDEEPILGQTYLPRKFKTTVVIPPQNDIDLHAND 234
Cdd:PRK09566 142 TGSPVAGIDPDELIdtrPLTQKLQDML------------------TNNGEGNPEFSNLPRKFNIAIAGGRDNSVHAEIND 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 235 MNFVAIAENGKLvGFNLLVGGGLSiehGNKKTYArtasefgyLPL------EHTLAVAEAVVTTQRDWGNRTDRKNAKTK 308
Cdd:PRK09566 204 IAFVPAYKDGVL-GFNVLVGGFFS---SQRCAYA--------IPLnawvkpDEVVRLCRAILEVYRDNGLRANRQKGRLM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 309 YTLERVGVETFKAEVERRAGIKFEPIRPyeftgrGDRIGWvkgiDDNWHLTLFIENGRILDY-----P-GRPLKTGLLEI 382
Cdd:PRK09566 272 WLIDEWGIEKFRAAVEAQFGPPLLTAAP------GDEIDW----EKRDHIGVHPQKQAGLNYvglhvPvGRLYAEDMFEL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 383 AKIHK----GDFRITANQNLIIAGVPESekaKIEKIAKESgLMNAVTPQREN----SMACVSFPTCPLAMAEA-ERflps 453
Cdd:PRK09566 342 ARLAEvygsGEIRLTVEQNVIIPNIPDE---NLETFLAEP-LLQKFSLEPGPlargLVSCTGNQYCNFALIETkNR---- 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447213450 454 fidnidNLMAKHGVSDE-----HIVMRVTGCPNGCGRAMLAEVGLVG---KAPGR----YNLHLGG 507
Cdd:PRK09566 414 ------ALALAKELDAEldlpqPVRIHWTGCPNSCGQPQVADIGLMGtkaRKNGKtvegVDIYMGG 473
|
|
| nirA |
PRK09567 |
NirA family protein; |
13-554 |
1.99e-32 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 131.68 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 13 GKLTDAERMKLESNYLrgtiaeDLNDGL-----TGGF-KGDNFLLIRFHGMYQ----QDdrdiraeraeqkleprhAMLL 82
Cdd:PRK09567 63 KKLCDQEKWKREENPF------DAWDRLkaqaaAGAFpKPADNFRWKYHGLFYvapaQD-----------------SYMC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 83 RCRLPGGVITTKQWQAI----DKFAGentiyGSIRLTNRQTFQFHGILKKNVKPVHQMLHSVGLDALATANDMNRNVlcT 158
Cdd:PRK09567 120 RLRIPNGILTHWQFAGLadlaDRHGG-----GYSHVTTRANLQLREIPPEHAVPVLEGLVDLGLTARGSGADNIRNV--T 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 159 SNPyesqlhaeayewAKKISEHLLPRTRAYAEIWldqekvattdEEPILGQ--TY-LPRKFKTTV----VIPPQNDidlh 231
Cdd:PRK09567 193 GSP------------TAGIDPQELLDTRPYAREW----------HHHILNDrsLYgLPRKFNVAFdgggRIATLED---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 232 ANDMNFVA--IAENGKL---VGFNLLVGG--GlsieHgnkKTYARTAsefGY-LPLEHTLAVAEAVVTTQRDWGNRTDRK 303
Cdd:PRK09567 247 TNDIGFQAvrVLEGAGVapgVYFRLVLGGitG----H---KDFARDT---GVlLRPEEATAVADAIVRVFIENGDRTNRK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 304 NAKTKYTLERVGVETFKAEVERRAGIKFEPIRPYEFTGRG--DRIGWV-----KGIDDNWhLTLFIENGRILDYPGRplk 376
Cdd:PRK09567 317 KARLKYVLDAWGFDKFLEAVEEKLGRPLTRVPAEAVAPRPaaDRFAHVgvhpqKQPGLNW-IGVVLPVGRLTTDQMR--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 377 tGLLEIAKIH-KGDFRITANQNLIIAGVPESEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAEAERFLPSFI 455
Cdd:PRK09567 393 -GLAKIAARYgDGEIRLTVWQNLLISGVPDADVAAVEAAIEALGLTTEASSIRAGLVACTGNAGCKFAAADTKGHALAIA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 456 DNIDNLMAkhgvSDEHIVMRVTGCPNGCGRAMLAEVGLVG-KAPGR-------YNLHLGGN-----RIGTRIPRmykeNI 522
Cdd:PRK09567 472 DYCEPRVA----LDQPVNIHLTGCHHSCAQHYIGDIGLIGaKVAVSegdtvegYHIVVGGGfgedaAIGREVFR----DV 543
|
570 580 590
....*....|....*....|....*....|...
gi 447213450 523 TEPEILASLDELIGRWAKEREA-GEGFGDFTVR 554
Cdd:PRK09567 544 KAEDAPRLVERLLRAYLAHRQGpDETFQAFTRR 576
|
|
| CobG |
TIGR02435 |
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated ... |
81-500 |
1.82e-18 |
|
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: 87.54 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 81 LLRCRLPGGVITTKQWQAIDKFAgENTIYGSIRLTNRQTFQFHGIlKKNVKPVHQMLHSVGLDALATANDMNRNVLCTSn 160
Cdd:TIGR02435 19 LVRVRLPGGRLTPAQAIGLADLA-ERLGNGIIEVTARGNLQLRGL-TADHDALSQALLAAGLGAAGAAADDIRNIEVSP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 161 pyesqlhaeayewAKKISEHLLPRTRAYAEIWLdqekvATTDEEPILGQtyLPRKFktTVVIPPQNDIDL--HANDMNFV 238
Cdd:TIGR02435 96 -------------LAGIDPGEIADTRPLAAELR-----AALENERALLE--LPPKF--SVAIDGGGRLVLlgDTADVRLQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 239 AIaENGKLVGFNLLVGGglsiehgnKKTYARTAsefGYLPLEHTLAVAEAVVTTQRDWGNRtdrknAKTKYTLERVGVET 318
Cdd:TIGR02435 154 AL-TTGAGVAWVVSLAG--------ISTSARSL---VTVAPDAAVPVAVALLRVFVELGGA-----ARGRDLDDAFLFAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 319 FKAEVERRAGIKFEPIR---PYEFTGRGDRIGWVKGIDDNWHLTLFIENGRIldyPGRPLKtGLLEIAKIH-KGDFRITA 394
Cdd:TIGR02435 217 ALELVEDSRPLIPDAAEgeaPRPAVDAAAPLGLHPQGDAGVTLGAGLALGQL---TAAQLR-GLAQLAQALgDGDLRLTP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447213450 395 NQNLIIAGVPESEKAKIEKIAKESGLMNAVTPQRENSMACVSFPTCPLAMAE----AERFLPSFIDNIDnlmakhgvsde 470
Cdd:TIGR02435 293 WRALLVLGLPPERADAAQRALAALGLVTSASDPRARIIACTGAPGCASALADtradAEALAAYCEPTAP----------- 361
|
410 420 430
....*....|....*....|....*....|
gi 447213450 471 hIVMRVTGCPNGCGRAMLAEVGLVGKAPGR 500
Cdd:TIGR02435 362 -ITVHLSGCAKGCAHPGPAAITLVAAGAGY 390
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
82-140 |
3.38e-11 |
|
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: 58.69 E-value: 3.38e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447213450 82 LRCRLPGGVITTKQWQAIDKFAGEntiYGS--IRLTNRQTFQFHGILKKNVKPVHQMLHSV 140
Cdd:pfam03460 10 VRVRVPGGRLTAEQLRALADIAEK---YGDgeIRLTTRQNLELHGVPEEDLPELLEELAEA 67
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
353-417 |
6.67e-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: 55.23 E-value: 6.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447213450 353 DDNWHLTLFIENGRIldypGRPLKTGLLEIAKIH-KGDFRITANQNLIIAGVPESEKAKIEKIAKE 417
Cdd:pfam03460 5 DGDYMVRVRVPGGRL----TAEQLRALADIAEKYgDGEIRLTTRQNLELHGVPEEDLPELLEELAE 66
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