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Conserved domains on  [gi|766431898|gb|AJR57019|]
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Met5p [Saccharomyces cerevisiae YJM981]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13504 PRK13504
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
843-1434 0e+00

NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;


:

Pssm-ID: 237402 [Multi-domain]  Cd Length: 569  Bit Score: 871.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  843 DEPKPVTNEDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREIRKSQGLEPYYMFMARARLPGGK 922
Cdd:PRK13504    7 VEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRCRLPGGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  923 TTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIA 1002
Cdd:PRK13504   87 ITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESRLHAEAY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1003 DMGKLISDHFLPKTTAYHEVWLEGpeeqdddpswpsifenrkdgprkkkTLVSGNALVDIEPIYGPTYLPRKFKFNIAVP 1082
Cdd:PRK13504  167 EWAKKISDHLLPRTRAYAEIWLDG-------------------------EKVATFSGTEEEPIYGKTYLPRKFKIAVAVP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1083 PYNDVDVLSIDVGLVAIVnPETQIVeGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKD 1162
Cdd:PRK13504  222 PDNDVDVYANDLGFVAIA-ENGKLV-GFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTD 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1163 RKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRK 1242
Cdd:PRK13504  300 RKNARLKYTLERVGLDWFKAEVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLRE 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1243 VAeymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKL-DNTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDII 1321
Cdd:PRK13504  380 IA----KIHKGDFRLTANQNLIIANVPPSDKAKIEALLREYGLiDGVEESPLRRNSMACVALPTCGLAMAEAERYLPSFI 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1322 TQLEDCLEEYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDYIKPLF 1401
Cdd:PRK13504  456 DRIEALLAKHGLSDEHIVIRMTGCPNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLL 535

                         570       580       590
                  ....*....|....*....|....*....|....
gi 766431898 1402 KRYALEREEGEHFGDFCIRVGIIKPTTEG-KYFH 1434
Cdd:PRK13504  536 GRWAKEREPGEGFGDFVIRAGIIREVLDGaRDFH 569
TPP_enzymes super family cl01629
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 347-664 8.35e-54

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


The actual alignment was detected with superfamily member cd03377:

Pssm-ID: 470272  Cd Length: 365  Bit Score: 192.82  E-value: 8.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  347 EDAYIKVLKQLFSSNLQILNQFSSETI----EPSNP---------------------EFGFGRFLKQEAQREELISLAKT 401
Cdd:cd03377    14 ETPYVKLLTQLFGDRMVIANATGCSSIyggsAPTTPyttnakgrgpawanslfednaEFGLGMRLAVDQRRERARELVQK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  402 SLDpslylSEDANKIVQLLSKWLSfngrDLDEAQLQEANATGLEIfQLLQSNQDsstVLKflKIAPTSDSFIFKSSWLIG 481
Cdd:cd03377    94 LIE-----KIGDEELKTLLNAWLA----TEDDIEESRERVAKLKP-LLAAEKDE---LAK--ELLSLADYLVKKSVWIIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  482 SDAWSYDLGHSGIQQVLSSRKNINVLLIDSEPYD--------------------HRKQNqdRKKDVGLYAMNYYSAYVAS 541
Cdd:cd03377   159 GDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSntggqaskatplgavakfaaAGKRT--GKKDLGMIAMSYGNVYVAQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  542 VAVYASYTQLLTAIIEASKYNGPSIVLAYLP-----YNSENDTPLEvlkETKNAVESGYWPLYRFNPvyDDPSTDKEAFS 616
Cdd:cd03377   237 IALGANDNQTLKAFREAEAYDGPSLIIAYSPciahgIKGGMTKSQE---QQKLAVESGYWPLYRYNP--RLVEEGKNPLQ 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 766431898  617 LDSSVIRKQLQDFLDRENKLTLLTRKDPSLSRNLKQSAGDALTRKQEK 664
Cdd:cd03377   312 LDSKEPDGPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKR 359
CysJ super family cl43121
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 678-874 8.31e-39

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


The actual alignment was detected with superfamily member COG0369:

Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 153.76  E-value: 8.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  678 SGPPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDT 757
Cdd:COG0369    25 AGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFLHSKK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  758 DLDLASLNVAVFGLGDSEYwprkedkHYFNKPSQDLFKRLELLSAKALIPLGlgdDQDADgFQTAYSEWEPKLWEALG-V 836
Cdd:COG0369   105 APKLDGLRYAVLGLGDSSY-------ETFCQTGKDFDARLEELGATRLLPRV---DCDVD-YEEAAEAWLAAVLAALAeA 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 766431898  837 SGAAVDDEPKPVTNEDIKRESNFLRGTISENLKDTSSG 874
Cdd:COG0369   174 LGAAAAAAAAAAAAAPAYSRKNPFPATVLENRELTGRG 211
 
Name Accession Description Interval E-value
PRK13504 PRK13504
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
843-1434 0e+00

NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;


Pssm-ID: 237402 [Multi-domain]  Cd Length: 569  Bit Score: 871.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  843 DEPKPVTNEDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREIRKSQGLEPYYMFMARARLPGGK 922
Cdd:PRK13504    7 VEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRCRLPGGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  923 TTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIA 1002
Cdd:PRK13504   87 ITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESRLHAEAY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1003 DMGKLISDHFLPKTTAYHEVWLEGpeeqdddpswpsifenrkdgprkkkTLVSGNALVDIEPIYGPTYLPRKFKFNIAVP 1082
Cdd:PRK13504  167 EWAKKISDHLLPRTRAYAEIWLDG-------------------------EKVATFSGTEEEPIYGKTYLPRKFKIAVAVP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1083 PYNDVDVLSIDVGLVAIVnPETQIVeGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKD 1162
Cdd:PRK13504  222 PDNDVDVYANDLGFVAIA-ENGKLV-GFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTD 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1163 RKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRK 1242
Cdd:PRK13504  300 RKNARLKYTLERVGLDWFKAEVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLRE 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1243 VAeymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKL-DNTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDII 1321
Cdd:PRK13504  380 IA----KIHKGDFRLTANQNLIIANVPPSDKAKIEALLREYGLiDGVEESPLRRNSMACVALPTCGLAMAEAERYLPSFI 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1322 TQLEDCLEEYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDYIKPLF 1401
Cdd:PRK13504  456 DRIEALLAKHGLSDEHIVIRMTGCPNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLL 535

                         570       580       590
                  ....*....|....*....|....*....|....
gi 766431898 1402 KRYALEREEGEHFGDFCIRVGIIKPTTEG-KYFH 1434
Cdd:PRK13504  536 GRWAKEREPGEGFGDFVIRAGIIREVLDGaRDFH 569
CysI TIGR02041
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ...
 851-1424 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: 699.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   851 EDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREIRKSQGLEPYYMFMARARLPGGKTTPQQWLA 930
Cdd:TIGR02041    1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   931 LDHLSDTSGN-GTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIADMGKLIS 1009
Cdd:TIGR02041   81 IDKFAREYTNyGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1010 DHFLPKTTAYHEVWLEGpeeqdddpswpsifenrkdgprkkKTLVSGNalvDIEPIYGPTYLPRKFKFNIAVPPYNDVDV 1089
Cdd:TIGR02041  161 EHLLPRTRAYAEIWLDQ------------------------EKVAGTE---EVEPILGPTYLPRKFKTTVVIPPQNDVDV 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1090 LSIDVGLVAIVNPETQIveGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKDRKHARLK 1169
Cdd:TIGR02041  214 YANDLGFVAIAENGKLV--GFNVLIGGGLSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTK 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1170 YTVDDMGVEGFKQKVEEYWGKKFEPERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRKVAeymlK 1249
Cdd:TIGR02041  292 YTIERMGLDTFKAEVERRAGIKFEPARPYEFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIA----K 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1250 TNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDNTdFSGLRLSSSSCVGLPTCGLAFAESERFLPDIITQLEDCLE 1329
Cdd:TIGR02041  368 IHKGDFRITANQNLIIAGVPEGGKAKIEKLARQYGLINA-VTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMA 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1330 EYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDYIKPLFKRYALERE 1409
Cdd:TIGR02041  447 KHGLSDEEIVLRVTGCPNGCGRAMLAEIGLVGKAPGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERK 526

                          570
                   ....*....|....*
gi 766431898  1410 EGEHFGDFCIRVGII 1424
Cdd:TIGR02041  527 PGEGFGDFLIRAGII 541
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 850-1428 2.10e-178

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: 540.86  E-value: 2.10e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  850 NEDIKRESNFLR-GTISENLKDTSSGGVTHAN-EQLMKFHGIYTQDDRDireirksqglepyYMFMARARLPGGKTTPQQ 927
Cdd:COG0155     4 YERIKREDVRSRlGTFAEQLGRFLTGEISEDDfRLRLKFHGLYQQRDPD-------------GAFMLRVRIPGGVLTPEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  928 WLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKvhQQIADM--- 1004
Cdd:COG0155    71 LRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDP--DELFDVrpy 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1005 GKLISDHFLpkttayhevwlegpeeqdddpswpsifenrkdgprkkktlvsgnalvdIEPIYgpTYLPRKFKFNIAVPPY 1084
Cdd:COG0155   149 AEAISQHLL------------------------------------------------GHPEY--TYLPRKFKIAFSGPPE 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1085 NDVDVLSIDVGLVAIVNPETQIveGYNVFVGGGMGTThnnkktyPRLGSCLG-FVKTEDIIPPLEGIVIVQRDHGDRKDR 1163
Cdd:COG0155   179 DDADVEINDLGFIAVVKEDGLV--GFNVLVGGGLGRT-------PRLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNR 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1164 KHARLKYTVDDMGVEGFKQKVEEYW-GKKFEPE-RPFEFKSNIDYFGWIKDET-GLNHFTAFIENGRVEDTpdlpQKTGI 1240
Cdd:COG0155   250 KKARLKYLVDDLGVEKFREEVEEEYlGFPLEPApRPLPAFARWDHLGVHEQKQdGLYYVGLSVENGRITDE----QLRAL 325

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1241 RKVAEymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDnTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDI 1320
Cdd:COG0155   326 ADLAE---RYGSGEIRLTPNQNLILADVPEEDLPALEAALRALGLA-TPPSGLRRDSIACPGLPTCKLAIAESKRLAPAL 401

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1321 ITQLEDCLEEYGLRHDsIIMRMTGCPNGCSRPWLGELALVGKAPH----TYNLMLGGGYLG-QRLNKLYKANVKDEEIVD 1395
Cdd:COG0155   402 ADRLEEDLDGLHDDEP-IRIRISGCPNSCGRHYIADIGLVGKAKKgvveAYQLYLGGGLGGdARLGRKYGPKVPADEIPD 480

                         570       580       590
                  ....*....|....*....|....*....|...
gi 766431898 1396 YIKPLFKRYALEREEGEHFGDFCIRVGIIKPTT 1428
Cdd:COG0155   481 ALERLLEAYLAEREEGESFGDFVRRVGIEPLKE 513
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 347-664 8.35e-54

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 192.82  E-value: 8.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  347 EDAYIKVLKQLFSSNLQILNQFSSETI----EPSNP---------------------EFGFGRFLKQEAQREELISLAKT 401
Cdd:cd03377    14 ETPYVKLLTQLFGDRMVIANATGCSSIyggsAPTTPyttnakgrgpawanslfednaEFGLGMRLAVDQRRERARELVQK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  402 SLDpslylSEDANKIVQLLSKWLSfngrDLDEAQLQEANATGLEIfQLLQSNQDsstVLKflKIAPTSDSFIFKSSWLIG 481
Cdd:cd03377    94 LIE-----KIGDEELKTLLNAWLA----TEDDIEESRERVAKLKP-LLAAEKDE---LAK--ELLSLADYLVKKSVWIIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  482 SDAWSYDLGHSGIQQVLSSRKNINVLLIDSEPYD--------------------HRKQNqdRKKDVGLYAMNYYSAYVAS 541
Cdd:cd03377   159 GDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSntggqaskatplgavakfaaAGKRT--GKKDLGMIAMSYGNVYVAQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  542 VAVYASYTQLLTAIIEASKYNGPSIVLAYLP-----YNSENDTPLEvlkETKNAVESGYWPLYRFNPvyDDPSTDKEAFS 616
Cdd:cd03377   237 IALGANDNQTLKAFREAEAYDGPSLIIAYSPciahgIKGGMTKSQE---QQKLAVESGYWPLYRYNP--RLVEEGKNPLQ 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 766431898  617 LDSSVIRKQLQDFLDRENKLTLLTRKDPSLSRNLKQSAGDALTRKQEK 664
Cdd:cd03377   312 LDSKEPDGPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKR 359
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 1004-1187 3.26e-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: 165.91  E-value: 3.26e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1004 MGKLISDHFLPKTTAYHEVWLegpeeqdDDPSWPSIFENRkdgprkkktlvsgnalvdIEPIYGPTYLPRKFKFNIAVPP 1083
Cdd:pfam01077    1 GDNVRNVTLCPGAGLCPEELL-------DTRPLAKAIEDE------------------FEPDYGFPYLPRKFKIAVSGCP 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1084 YNDVDVLSIDVGLVAIVNPETQIveGYNVFVGGGMGTTHNNKKTYPRLGsclgFVKTEDIIPPLEGIVIVQRDHGDRKDR 1163
Cdd:pfam01077   56 NNCVAAHANDIGFVGVWKDGGEI--GFNILVGGGLGRTPGAAATLKVVP----FVPEEDVLEVIEAILEVYRDHGDRENR 129

                          170       180
                   ....*....|....*....|....
gi 766431898  1164 KHARLKYTVDDMGVEGFKQKVEEY 1187
Cdd:pfam01077  130 KKERLKYLIERLGLEKFREEVEER 153
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 678-874 8.31e-39

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 153.76  E-value: 8.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  678 SGPPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDT 757
Cdd:COG0369    25 AGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFLHSKK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  758 DLDLASLNVAVFGLGDSEYwprkedkHYFNKPSQDLFKRLELLSAKALIPLGlgdDQDADgFQTAYSEWEPKLWEALG-V 836
Cdd:COG0369   105 APKLDGLRYAVLGLGDSSY-------ETFCQTGKDFDARLEELGATRLLPRV---DCDVD-YEEAAEAWLAAVLAALAeA 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 766431898  837 SGAAVDDEPKPVTNEDIKRESNFLRGTISENLKDTSSG 874
Cdd:COG0369   174 LGAAAAAAAAAAAAAPAYSRKNPFPATVLENRELTGRG 211
Flavodoxin_1 pfam00258
Flavodoxin;
684-826 1.18e-31

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 120.94  E-value: 1.18e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   684 VYYASDGGNAANLAKRLAARASARGLKATVLSMD--DIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDTDL-- 759
Cdd:pfam00258    1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDdvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLed 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766431898   760 -DLASLNVAVFGLGDSEYWPrkedkhyFNKPSQDLFKRLELLSAKALIPLGLGDDQDA-DGFQTAYSEW 826
Cdd:pfam00258   81 gDLSGLKYAVFGLGDSGYEG-------FCGAAKKLDEKLSELGASRVGPLGEGDEDPQeDGLEEAFEAW 142
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
680-834 3.25e-09

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 61.27  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  680 PPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDTDL 759
Cdd:PRK10953   62 PGITLISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAP 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 766431898  760 DLASLNVAVFGLGDSEYwprkedkHYFNKPSQDLFKRLELLSAKALIplglgDDQDAD-GFQTAYSEWEPKLWEAL 834
Cdd:PRK10953  142 KLENTAFAVFGLGDTSY-------EFFCQAGKDFDSKLAELGAERLL-----DRVDADvEYQAAASEWRARVVDAL 205
 
Name Accession Description Interval E-value
PRK13504 PRK13504
NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;
843-1434 0e+00

NADPH-dependent assimilatory sulfite reductase hemoprotein subunit;


Pssm-ID: 237402 [Multi-domain]  Cd Length: 569  Bit Score: 871.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  843 DEPKPVTNEDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREIRKSQGLEPYYMFMARARLPGGK 922
Cdd:PRK13504    7 VEGKLSDVERIKLESNYLRGTIAEELNDGLTGGFSEDDFQLLKFHGSYQQDDRDIRAERAEQKLEPAYQFMLRCRLPGGV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  923 TTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIA 1002
Cdd:PRK13504   87 ITPQQWLALDKLADEYGNGTLRLTTRQTFQFHGILKKNLKPVIQTINSVLLDTLAACGDVNRNVMCTPNPYESRLHAEAY 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1003 DMGKLISDHFLPKTTAYHEVWLEGpeeqdddpswpsifenrkdgprkkkTLVSGNALVDIEPIYGPTYLPRKFKFNIAVP 1082
Cdd:PRK13504  167 EWAKKISDHLLPRTRAYAEIWLDG-------------------------EKVATFSGTEEEPIYGKTYLPRKFKIAVAVP 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1083 PYNDVDVLSIDVGLVAIVnPETQIVeGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKD 1162
Cdd:PRK13504  222 PDNDVDVYANDLGFVAIA-ENGKLV-GFNVLVGGGMGMTHGDKETYPRLADELGYVPPEDVLDVAEAVVTTQRDYGNRTD 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1163 RKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRK 1242
Cdd:PRK13504  300 RKNARLKYTLERVGLDWFKAEVERRAGKKLEPARPYEFTGRGDRLGWVEGIDGKWHLTLFIENGRIKDYPGRPLKTGLRE 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1243 VAeymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKL-DNTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDII 1321
Cdd:PRK13504  380 IA----KIHKGDFRLTANQNLIIANVPPSDKAKIEALLREYGLiDGVEESPLRRNSMACVALPTCGLAMAEAERYLPSFI 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1322 TQLEDCLEEYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDYIKPLF 1401
Cdd:PRK13504  456 DRIEALLAKHGLSDEHIVIRMTGCPNGCARPYLAEIGLVGKAPGRYNLYLGGSFNGTRLPKMYRENITEEEILATLDPLL 535

                         570       580       590
                  ....*....|....*....|....*....|....
gi 766431898 1402 KRYALEREEGEHFGDFCIRVGIIKPTTEG-KYFH 1434
Cdd:PRK13504  536 GRWAKEREPGEGFGDFVIRAGIIREVLDGaRDFH 569
CysI TIGR02041
sulfite reductase (NADPH) hemoprotein, beta-component; Sulfite reductase (NADPH) catalyzes a ...
 851-1424 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: 699.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   851 EDIKRESNFLRGTISENLKDTSSGGVTHANEQLMKFHGIYTQDDRDIREIRKSQGLEPYYMFMARARLPGGKTTPQQWLA 930
Cdd:TIGR02041    1 ERIKEESNYLRGTILEDLADPLTGGFKGDNFQLIRFHGMYQQDDRDLRAERAEQKLEPRYAMMLRCRLPGGVITPKQWLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   931 LDHLSDTSGN-GTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIADMGKLIS 1009
Cdd:TIGR02041   81 IDKFAREYTNyGSIRLTNRQTFQFHGILKKNLKPVHQMLHSVGLDSLATAGDVNRNVLCTSNPYESELHAEAYEWAKKIS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1010 DHFLPKTTAYHEVWLEGpeeqdddpswpsifenrkdgprkkKTLVSGNalvDIEPIYGPTYLPRKFKFNIAVPPYNDVDV 1089
Cdd:TIGR02041  161 EHLLPRTRAYAEIWLDQ------------------------EKVAGTE---EVEPILGPTYLPRKFKTTVVIPPQNDVDV 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1090 LSIDVGLVAIVNPETQIveGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKDRKHARLK 1169
Cdd:TIGR02041  214 YANDLGFVAIAENGKLV--GFNVLIGGGLSMEHGNKKTYPRLASEIGFIPPEHTLAVAEAVVTTQRDFGNRTDRKNARTK 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1170 YTVDDMGVEGFKQKVEEYWGKKFEPERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQKTGIRKVAeymlK 1249
Cdd:TIGR02041  292 YTIERMGLDTFKAEVERRAGIKFEPARPYEFTGRGDRIGWVKGIDGNWHLTLFIENGRILDYPDKPLKTGLLEIA----K 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1250 TNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDNTdFSGLRLSSSSCVGLPTCGLAFAESERFLPDIITQLEDCLE 1329
Cdd:TIGR02041  368 IHKGDFRITANQNLIIAGVPEGGKAKIEKLARQYGLINA-VTALRENSMACVSFPTCPLAMAEAERYLPDFIDKLDNIMA 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1330 EYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDYIKPLFKRYALERE 1409
Cdd:TIGR02041  447 KHGLSDEEIVLRVTGCPNGCGRAMLAEIGLVGKAPGRYNLHLGGNRIGTRIPRLYKENITEPEILAELDELIGRWAKERK 526

                          570
                   ....*....|....*
gi 766431898  1410 EGEHFGDFCIRVGII 1424
Cdd:TIGR02041  527 PGEGFGDFLIRAGII 541
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 850-1428 2.10e-178

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: 540.86  E-value: 2.10e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  850 NEDIKRESNFLR-GTISENLKDTSSGGVTHAN-EQLMKFHGIYTQDDRDireirksqglepyYMFMARARLPGGKTTPQQ 927
Cdd:COG0155     4 YERIKREDVRSRlGTFAEQLGRFLTGEISEDDfRLRLKFHGLYQQRDPD-------------GAFMLRVRIPGGVLTPEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  928 WLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKvhQQIADM--- 1004
Cdd:COG0155    71 LRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGLTTIGACGDVVRNVTASPLAGVDP--DELFDVrpy 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1005 GKLISDHFLpkttayhevwlegpeeqdddpswpsifenrkdgprkkktlvsgnalvdIEPIYgpTYLPRKFKFNIAVPPY 1084
Cdd:COG0155   149 AEAISQHLL------------------------------------------------GHPEY--TYLPRKFKIAFSGPPE 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1085 NDVDVLSIDVGLVAIVNPETQIveGYNVFVGGGMGTThnnkktyPRLGSCLG-FVKTEDIIPPLEGIVIVQRDHGDRKDR 1163
Cdd:COG0155   179 DDADVEINDLGFIAVVKEDGLV--GFNVLVGGGLGRT-------PRLADVLGeFVPPEDLLDVAEAVVRVFRDYGDRDNR 249

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1164 KHARLKYTVDDMGVEGFKQKVEEYW-GKKFEPE-RPFEFKSNIDYFGWIKDET-GLNHFTAFIENGRVEDTpdlpQKTGI 1240
Cdd:COG0155   250 KKARLKYLVDDLGVEKFREEVEEEYlGFPLEPApRPLPAFARWDHLGVHEQKQdGLYYVGLSVENGRITDE----QLRAL 325

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1241 RKVAEymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDnTDFSGLRLSSSSCVGLPTCGLAFAESERFLPDI 1320
Cdd:COG0155   326 ADLAE---RYGSGEIRLTPNQNLILADVPEEDLPALEAALRALGLA-TPPSGLRRDSIACPGLPTCKLAIAESKRLAPAL 401

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1321 ITQLEDCLEEYGLRHDsIIMRMTGCPNGCSRPWLGELALVGKAPH----TYNLMLGGGYLG-QRLNKLYKANVKDEEIVD 1395
Cdd:COG0155   402 ADRLEEDLDGLHDDEP-IRIRISGCPNSCGRHYIADIGLVGKAKKgvveAYQLYLGGGLGGdARLGRKYGPKVPADEIPD 480

                         570       580       590
                  ....*....|....*....|....*....|...
gi 766431898 1396 YIKPLFKRYALEREEGEHFGDFCIRVGIIKPTT 1428
Cdd:COG0155   481 ALERLLEAYLAEREEGESFGDFVRRVGIEPLKE 513
PLN00178 PLN00178
sulfite reductase
 844-1422 1.65e-162

sulfite reductase


Pssm-ID: 177773 [Multi-domain]  Cd Length: 623  Bit Score: 503.13  E-value: 1.65e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  844 EPKPVTNEDIKRESNFLRGTISENLKdTSSGGVTHANEQLMKFHGIYTQDDRDIREIRksqglepYYMFMARARLPGGKT 923
Cdd:PLN00178   50 PPKRSKVEIIKENSNFLRHPLNEELA-TEAPNINEDAVQLIKFHGSYQQDNREKRGGK-------AYQFMLRTKQPAGKV 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  924 TPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQIAD 1003
Cdd:PLN00178  122 PNRLYLVMDDLADEFGIGTLRLTTRQTFQLHGVLKKDLKTVMSSIIKNMGSTLGACGDVNRNVLAPAAPFARKDYLFAQE 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1004 MGKLISDHFLPKTTAYHEVWLEGPEEQDDDPswPSIFENRKDGPRkkktlvsGNALVD-IEPIYGPTYLPRKFKFNIAVP 1082
Cdd:PLN00178  202 LAKNIAALLAPQSGAYYDIWVDGEKIMSAEP--PEVTKARNDNSH-------GTNFEDsPEPIYGTQFLPRKFKIAVTVP 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1083 PYNDVDVLSIDVGLVAIVNpETQIVEGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGDRKD 1162
Cdd:PLN00178  273 GDNSVDILTNDIGVVVVSD-EAGEPQGYNIYVGGGMGRTHRNETTFPRLADPLGYVPKEDILYAVKAIVATQRDYGRRDD 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1163 RKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERP---FEFKSnidYFGWIKDETGLNHFTAFIENGRVEDTpdlpQKTG 1239
Cdd:PLN00178  352 RKQSRMKYLVHSWGIEKFRSVVEQYYGKKFEPFRElpeWEFKS---YLGWHEQGDGKLFYGVHVDNGRIKGE----AKKA 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1240 IRKVAE-YMLktnsgHFRLTGNQHLVISNITDEHVAGIKSILKTYKL-DNTDFSGLRLSSSSCVGLPTCGLAFAESERFL 1317
Cdd:PLN00178  425 LREVIEkYNL-----PVRLTPNQNLILCDIRPAWKEPITAALAAAGLlEPEEVDPLNRTAMACPALPLCPLAITEAERGI 499

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1318 PDIITQLEDCLEEYGLR-HDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIVDY 1396
Cdd:PLN00178  500 PDILKRVRAMFNKVGLKyDESVVVRMTGCPNGCARPYMAELGFVGDGPNSYQIWLGGTPNQTRLAEPFMDKVKVDDLEKV 579

                         570       580
                  ....*....|....*....|....*.
gi 766431898 1397 IKPLFKRYALEREEGEHFGDFCIRVG 1422
Cdd:PLN00178  580 LEPLFYMWKQQRQEKESFGDFTNRVG 605
sir TIGR02042
ferredoxin-sulfite reductase; Distantly related to the iron-sulfur hemoprotein of sulfite ...
 845-1422 6.38e-161

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: 497.07  E-value: 6.38e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   845 PKPVTNEDIKRESNFLRGTISENLKDTSsggvTHANE---QLMKFHGIYTQDDRDIReirkSQGLEPYYMFMARARLPGG 921
Cdd:TIGR02042    4 QKRSKVEILKERSNFLREPLNEQLLEEA----THFNEdavQILKFHGSYQQDNRDNR----GKGQEKDYQFMLRTKNPGG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   922 KTTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSALPTNAKVHQQI 1001
Cdd:TIGR02042   76 YVPPQLYLTLDDLADEYGNGTLRATTRQTFQLHGILKKNLKTVISTIVKNLGSTLGACGDLNRNVMAPPAPFRKRPEYEF 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1002 A-DMGKLISDHFLPKTTAYHEVWLEGPEEQDDDPSwPSIFENRKDGPRkkktlvsGNALVD-IEPIYGPTYLPRKFKFNI 1079
Cdd:TIGR02042  156 ArEYADNIADLLTPQSGAYYELWLDGEKVMSAEPD-PEVVAARNDNSH-------GTNFADsPEPLYGTQYLPRKFKIAV 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1080 AVPPYNDVDVLSIDVGLVAIVNPETQIvEGYNVFVGGGMGTTHNNKKTYPRLGSCLGFVKTEDIIPPLEGIVIVQRDHGD 1159
Cdd:TIGR02042  228 TVPGDNSIDLFTQDIGLVVVSNERGEL-EGFNIYVGGGMGRTHNKEETFARLADPLGYVPKEDIYYAVKAIVATQRDYGD 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1160 RKDRKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPER---PFEFKsniDYFGWIKDETGLNHFTAFIENGRVEDTPDLPQ 1236
Cdd:TIGR02042  307 RDDRRHARMKYLISDWGIEKFREVVEQYFGKKIAPVRelpEFEYK---DYLGWHEQGDGKWFLGLHIDSGRVKDDGNWQL 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1237 KTGIRKVAE-YMLKtnsghFRLTGNQHLVISNITDEHVAGIKSILKTYKLDNTDF-SGLRLSSSSCVGLPTCGLAFAESE 1314
Cdd:TIGR02042  384 KKALREIVEkYNLP-----VRLTPNQNIILYDIQPEWKRAITTVLAQRGVLQPEAiDPLNRYAMACPALPTCGLAITESE 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1315 RFLPDIITQLEDCLEEYGLRHDSIIMRMTGCPNGCSRPWLGELALVGKAPHTYNLMLGGGYLGQRLNKLYKANVKDEEIV 1394
Cdd:TIGR02042  459 RAIPGILKRIRALLEKVGLPDEHFVVRMTGCPNGCARPYMAELGFVGSAPNSYQVWLGGSPNQTRLARPFIDKLKDGDLE 538

                          570       580
                   ....*....|....*....|....*...
gi 766431898  1395 DYIKPLFKRYALEREEGEHFGDFCIRVG 1422
Cdd:TIGR02042  539 KVLEPLFVHFKQSRQSGESFGDFCDRVG 566
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 347-664 8.35e-54

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 192.82  E-value: 8.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  347 EDAYIKVLKQLFSSNLQILNQFSSETI----EPSNP---------------------EFGFGRFLKQEAQREELISLAKT 401
Cdd:cd03377    14 ETPYVKLLTQLFGDRMVIANATGCSSIyggsAPTTPyttnakgrgpawanslfednaEFGLGMRLAVDQRRERARELVQK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  402 SLDpslylSEDANKIVQLLSKWLSfngrDLDEAQLQEANATGLEIfQLLQSNQDsstVLKflKIAPTSDSFIFKSSWLIG 481
Cdd:cd03377    94 LIE-----KIGDEELKTLLNAWLA----TEDDIEESRERVAKLKP-LLAAEKDE---LAK--ELLSLADYLVKKSVWIIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  482 SDAWSYDLGHSGIQQVLSSRKNINVLLIDSEPYD--------------------HRKQNqdRKKDVGLYAMNYYSAYVAS 541
Cdd:cd03377   159 GDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSntggqaskatplgavakfaaAGKRT--GKKDLGMIAMSYGNVYVAQ 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  542 VAVYASYTQLLTAIIEASKYNGPSIVLAYLP-----YNSENDTPLEvlkETKNAVESGYWPLYRFNPvyDDPSTDKEAFS 616
Cdd:cd03377   237 IALGANDNQTLKAFREAEAYDGPSLIIAYSPciahgIKGGMTKSQE---QQKLAVESGYWPLYRYNP--RLVEEGKNPLQ 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 766431898  617 LDSSVIRKQLQDFLDRENKLTLLTRKDPSLSRNLKQSAGDALTRKQEK 664
Cdd:cd03377   312 LDSKEPDGPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKR 359
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 1004-1187 3.26e-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: 165.91  E-value: 3.26e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1004 MGKLISDHFLPKTTAYHEVWLegpeeqdDDPSWPSIFENRkdgprkkktlvsgnalvdIEPIYGPTYLPRKFKFNIAVPP 1083
Cdd:pfam01077    1 GDNVRNVTLCPGAGLCPEELL-------DTRPLAKAIEDE------------------FEPDYGFPYLPRKFKIAVSGCP 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1084 YNDVDVLSIDVGLVAIVNPETQIveGYNVFVGGGMGTTHNNKKTYPRLGsclgFVKTEDIIPPLEGIVIVQRDHGDRKDR 1163
Cdd:pfam01077   56 NNCVAAHANDIGFVGVWKDGGEI--GFNILVGGGLGRTPGAAATLKVVP----FVPEEDVLEVIEAILEVYRDHGDRENR 129

                          170       180
                   ....*....|....*....|....
gi 766431898  1164 KHARLKYTVDDMGVEGFKQKVEEY 1187
Cdd:pfam01077  130 KKERLKYLIERLGLEKFREEVEER 153
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
 678-874 8.31e-39

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 153.76  E-value: 8.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  678 SGPPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDT 757
Cdd:COG0369    25 AGTPLTILYGSQTGNAEGLAEQLAERAKAAGLAVTLASLDDYKPKDLAKEGLLLIVTSTYGEGEPPDNARAFYEFLHSKK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  758 DLDLASLNVAVFGLGDSEYwprkedkHYFNKPSQDLFKRLELLSAKALIPLGlgdDQDADgFQTAYSEWEPKLWEALG-V 836
Cdd:COG0369   105 APKLDGLRYAVLGLGDSSY-------ETFCQTGKDFDARLEELGATRLLPRV---DCDVD-YEEAAEAWLAAVLAALAeA 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 766431898  837 SGAAVDDEPKPVTNEDIKRESNFLRGTISENLKDTSSG 874
Cdd:COG0369   174 LGAAAAAAAAAAAAAPAYSRKNPFPATVLENRELTGRG 211
Flavodoxin_1 pfam00258
Flavodoxin;
684-826 1.18e-31

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 120.94  E-value: 1.18e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   684 VYYASDGGNAANLAKRLAARASARGLKATVLSMD--DIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDTDL-- 759
Cdd:pfam00258    1 IFYGSQTGNTEKLAEAIAEGLGEAGFEVDVVDLDdvDETLSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLed 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766431898   760 -DLASLNVAVFGLGDSEYWPrkedkhyFNKPSQDLFKRLELLSAKALIPLGLGDDQDA-DGFQTAYSEW 826
Cdd:pfam00258   81 gDLSGLKYAVFGLGDSGYEG-------FCGAAKKLDEKLSELGASRVGPLGEGDEDPQeDGLEEAFEAW 142
nirA PRK09567
NirA family protein;
851-1420 1.81e-30

NirA family protein;


Pssm-ID: 236573 [Multi-domain]  Cd Length: 593  Bit Score: 128.98  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  851 EDIKRESNFLrgTISENLKDTSSGGVT--HANEQLMKFHGIY----TQDDrdireirksqglepyymFMARARLPGGKTT 924
Cdd:PRK09567   69 EKWKREENPF--DAWDRLKAQAAAGAFpkPADNFRWKYHGLFyvapAQDS-----------------YMCRLRIPNGILT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  925 PQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSalPTNAKVHQQIADM 1004
Cdd:PRK09567  130 HWQFAGLADLADRHGGGYSHVTTRANLQLREIPPEHAVPVLEGLVDLGLTARGSGADNIRNVTGS--PTAGIDPQELLDT 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1005 gklisdhfLPKTTAYHEvwlegpeeqdddpswpSIFENRKdgprkkktlvsgnalvdiepIYGptyLPRKFkfNIA---- 1080
Cdd:PRK09567  208 --------RPYAREWHH----------------HILNDRS--------------------LYG---LPRKF--NVAfdgg 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1081 --VPPYNDVDvlsiDVGLVAIvnpetQIVEGYNVFVGggmgtthnnkkTYPRLgsCLG-------FVK-TEDIIPPLE-- 1148
Cdd:PRK09567  239 grIATLEDTN----DIGFQAV-----RVLEGAGVAPG-----------VYFRL--VLGgitghkdFARdTGVLLRPEEat 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1149 ----GIVIVQRDHGDRKDRKHARLKYTVDDMGVEGFKQKVEEYWGKKF--------EPERPFefksniDYFGWI----KD 1212
Cdd:PRK09567  297 avadAIVRVFIENGDRTNRKKARLKYVLDAWGFDKFLEAVEEKLGRPLtrvpaeavAPRPAA------DRFAHVgvhpQK 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1213 ETGLNHFTAFIENGRVedTPDlpQKTGIRKVAEymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDnTDFSG 1292
Cdd:PRK09567  371 QPGLNWIGVVLPVGRL--TTD--QMRGLAKIAA---RYGDGEIRLTVWQNLLISGVPDADVAAVEAAIEALGLT-TEASS 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1293 LRLSSSSCVGLPTCGLAFAESERFLPDIITQLEDCLEEyglrhDSII-MRMTGCPNGCSRPWLGELALVG-KAPHT---- 1366
Cdd:PRK09567  443 IRAGLVACTGNAGCKFAAADTKGHALAIADYCEPRVAL-----DQPVnIHLTGCHHSCAQHYIGDIGLIGaKVAVSegdt 517

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 766431898 1367 ---YNLMLGGGY-----LGQRLNKlykaNVKDEEIVDYIKPLFKRYALEREE-GEHFGDFCIR 1420
Cdd:PRK09567  518 vegYHIVVGGGFgedaaIGREVFR----DVKAEDAPRLVERLLRAYLAHRQGpDETFQAFTRR 576
PLN02431 PLN02431
ferredoxin--nitrite reductase
 891-1409 2.22e-29

ferredoxin--nitrite reductase


Pssm-ID: 178050 [Multi-domain]  Cd Length: 587  Bit Score: 125.28  E-value: 2.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  891 TQDDRDIR-------EIRKSQglepYYMFMARARLPGGKTTPQQ--WLAlDHLSDTSGNGTLKLTTRATFQIHGVLKKNL 961
Cdd:PLN02431  113 SKDDIDVRlkwlglfHRRKHQ----YGRFMMRLKLPNGVTTSAQtrYLA-SVIEKYGEDGCADVTTRQNWQIRGVVLPDV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  962 KHTLRGMNAVLMDTLAAAGDVNRNVMVSALptnAKVH-QQIAD---MGKLISDHflpkttayhevwlegpeeqdddpswp 1037
Cdd:PLN02431  188 PAILKGLEEVGLTSLQSGMDNVRNPVGNPL---AGIDpHEIVDtrpYTNLLSDY-------------------------- 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1038 sIFENRKdgprkkktlvsGNALVdiepiygpTYLPRKFkfNIAVPPYNDvDVLSIDVGLVAIVNPETQIVEGYNVFVGGG 1117
Cdd:PLN02431  239 -ITNNGR-----------GNPEI--------TNLPRKW--NVCVVGSHD-LFEHPHINDLAYMPATKDGRFGFNLLVGGF 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1118 MGTTHNNKKTyprlgSCLGFVKTEDIIPPLEGIVIVQRDHGDRKDRKHARLKYTVDDMGVEGFKQKVEEYW-GKKFE--- 1193
Cdd:PLN02431  296 FSPKRCAEAI-----PLDAWVPADDVVPLCKAILEAFRDLGTRGNRQKTRMMWLIDELGVEGFRSEVEKRMpNGELEraa 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1194 ----PERPFEFKsniDYFGWIKD-ETGLNHFTAFIENGRVedtpdlpQKTGIRKVAEYMLKTNSGHFRLTGNQHLVISNI 1268
Cdd:PLN02431  371 sedlVDKKWERR---DYLGVHPQkQEGLSYVGLHVPVGRL-------QAADMDELARLADEYGSGELRLTVEQNIIIPNV 440

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1269 TDEHVAGIKS--ILKTYKLdntdFSGLRLSS-SSCVGLPTCGLAFAESERFLPDIITQLEDCLEeyglRHDSIIMRMTGC 1345
Cdd:PLN02431  441 PNSKVEALLAepLLQRFSP----NPGLLLKGlVACTGNQFCGQAIIETKARALKVTEELERLVE----VPRPVRMHWTGC 512

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766431898 1346 PNGCSRPWLGELALVG--------KAPHTYNLMLGG-----GYLGQrlnkLYKANVKDEEIVDYIKP-LFKRY-ALERE 1409
Cdd:PLN02431  513 PNSCGQVQVADIGFMGcmardengKAVEGADIFVGGrvgsdSHLAE----EYKKGVPCDELVPVVADiLIEEFgAKERE 587
nirA PRK09566
ferredoxin-nitrite reductase; Reviewed
 912-1373 1.70e-28

ferredoxin-nitrite reductase; Reviewed


Pssm-ID: 236572 [Multi-domain]  Cd Length: 513  Bit Score: 121.65  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  912 FMARARLPGGKTTPQQWLALDHLSDTSG-NGTLKLTTRATFQIHGVLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSa 990
Cdd:PRK09566   66 FMLRLRVPNGILTSEQLRVLASIVQRYGdDGSADITTRQNLQLRGILLEDLPEILNRLKAVGLTSVQSGMDNVRNITGS- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  991 lPTNAKVHQQIADMGKLISdhflpkttayhevwlegpEEQDDdpswpsIFENRKdgprkkktlvsGNalvdiepiYGPTY 1070
Cdd:PRK09566  145 -PVAGIDPDELIDTRPLTQ------------------KLQDM------LTNNGE-----------GN--------PEFSN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1071 LPRKFkfNIAVPPYNDVDVLSiDVGLVAIVNPETQIVEGYNVFVGGGMGTTHN------NkktyprlgsclGFVKTEDII 1144
Cdd:PRK09566  181 LPRKF--NIAIAGGRDNSVHA-EINDIAFVPAYKDGVLGFNVLVGGFFSSQRCayaiplN-----------AWVKPDEVV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1145 PPLEGIVIVQRDHGDRKDRKHARLKYTVDDMGVEGFKQKVEEYWGKKFEPERPfefKSNI-----DYFG-WIKDETGLNH 1218
Cdd:PRK09566  247 RLCRAILEVYRDNGLRANRQKGRLMWLIDEWGIEKFRAAVEAQFGPPLLTAAP---GDEIdwekrDHIGvHPQKQAGLNY 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1219 FTAFIENGRV--EDTPDLpqktgirkvAEYMLKTNSGHFRLTGNQHLVISNITDEHVAGIKS--ILKTYKLDNtdfSGLR 1294
Cdd:PRK09566  324 VGLHVPVGRLyaEDMFEL---------ARLAEVYGSGEIRLTVEQNVIIPNIPDENLETFLAepLLQKFSLEP---GPLA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898 1295 LSSSSCVGLPTCGLAFAES-ERFLpDIITQLEDCLEeyglRHDSIIMRMTGCPNGCSRPWLGELALVG-------KAPHT 1366
Cdd:PRK09566  392 RGLVSCTGNQYCNFALIETkNRAL-ALAKELDAELD----LPQPVRIHWTGCPNSCGQPQVADIGLMGtkarkngKTVEG 466


                  ....*..
gi 766431898 1367 YNLMLGG 1373
Cdd:PRK09566  467 VDIYMGG 473
CobG TIGR02435
precorrin-3B synthase; An iron-sulfur protein. An oxygen atom from dioxygen is incorporated ...
 913-1364 8.03e-19

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: 90.62  E-value: 8.03e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   913 MARARLPGGKTTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGvLKKNLKHTLRGMNAVLMDTLAAAGDVNRNVMVSalP 992
Cdd:TIGR02435   19 LVRVRLPGGRLTPAQAIGLADLAERLGNGIIEVTARGNLQLRG-LTADHDALSQALLAAGLGAAGAAADDIRNIEVS--P 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898   993 TNAKVHQQIADmgklisdhflpkTTAYHEVWLEGPEEQdddpswPSIFEnrkdgprkkktlvsgnalvdiepiygptyLP 1072
Cdd:TIGR02435   96 LAGIDPGEIAD------------TRPLAAELRAALENE------RALLE-----------------------------LP 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1073 RKFKFNIAVPPYNDVDVLSIDVGLVAivnpeTQIVEGYNVFVGGGMGTTHNnkktyprlgSCLGFVKTEDIIPPLEGIVI 1152
Cdd:TIGR02435  129 PKFSVAIDGGGRLVLLGDTADVRLQA-----LTTGAGVAWVVSLAGISTSA---------RSLVTVAPDAAVPVAVALLR 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1153 VQRDHGDrkdrkHARLKYTVDDMGVEGFKQKVEEYWGKKFEP---ERPFEFKSNIDYFGWIKDETGLNHFTAFIENGRVe 1229
Cdd:TIGR02435  195 VFVELGG-----AARGRDLDDAFLFALALELVEDSRPLIPDAaegEAPRPAVDAAAPLGLHPQGDAGVTLGAGLALGQL- 268

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  1230 dTPDLpqktgIRKVAEYMLKTNSGHFRLTGNQHLVISNITDEHVAGIKSILKTYKLDnTDFSGLRLSSSSCVGLPTCGLA 1309
Cdd:TIGR02435  269 -TAAQ-----LRGLAQLAQALGDGDLRLTPWRALLVLGLPPERADAAQRALAALGLV-TSASDPRARIIACTGAPGCASA 341

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 766431898  1310 FAESERFLPDIITQLEDCLEeyGLRHdsiimrMTGCPNGCSRPWLGELALVGKAP 1364
Cdd:TIGR02435  342 LADTRADAEALAAYCEPTAP--ITVH------LSGCAKGCAHPGPAAITLVAAGA 388
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 454-603 2.42e-14

Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238976 [Multi-domain]  Cd Length: 237  Bit Score: 74.06  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  454 QDSSTVLKFLKIAPT------SDSFIFKSSWLIGSDAWSYDLGHSGIQQVLSSRKNINVLLIDSEPYDH----------R 517
Cdd:cd02018    61 EDANAVASGLKRGLKarfpkdRELDKKKDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNtggqrsgatpL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  518 KQN--------QDRKKDVGLYAMNYYSAYVASVAVyASYTQLLTAIIEA-SKYNGPSIVLAYLPYNSENDTPL-EVLKET 587
Cdd:cd02018   141 GADskmapagkKEDKKDLVLIAATHGCVYVARLSP-ALKKHFLKVVKEAiSRTDGPTFIHAYTPCITEWGIGSgKSLELA 219

                         170
                  ....*....|....*.
gi 766431898  588 KNAVESGYWPLYRFNP 603
Cdd:cd02018   220 RKAVKSRMFPLFEYDP 235
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 912-962 1.23e-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: 64.09  E-value: 1.23e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 766431898   912 FMARARLPGGKTTPQQWLALDHLSDTSGNGTLKLTTRATFQIHGVLKKNLK 962
Cdd:pfam03460    8 YMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLP 58
FldA COG0716
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ...
 684-775 8.70e-12

Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440480 [Multi-domain]  Cd Length: 135  Bit Score: 64.15  E-value: 8.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  684 VYYASDGGNAANLAKRLAARASARGlkATVLSMDDIILEELPGEENVVFITSTAGqGEFPQDGKSFWEALKNDtdldLAS 763
Cdd:COG0716     3 IVYGSTTGNTEKVAEAIAEALGAAG--VDLFEIEDADLDDLEDYDLLILGTPTWA-GELPDDWEDFLEELKED----LSG 75

                          90
                  ....*....|..
gi 766431898  764 LNVAVFGLGDSE 775
Cdd:COG0716    76 KKVALFGTGDSS 87
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 1210-1281 1.58e-09

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: 1.58e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 766431898  1210 IKDETGLNHFTAFIENGRVedTPDlpQKTGIRKVAEymlKTNSGHFRLTGNQHLVISNITDEHVAGIKSILK 1281
Cdd:pfam03460    1 HPQKDGDYMVRVRVPGGRL--TAE--QLRALADIAE---KYGDGEIRLTTRQNLELHGVPEEDLPELLEELA 65
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
680-834 3.25e-09

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 61.27  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  680 PPLHVYYASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNDTDL 759
Cdd:PRK10953   62 PGITLISASQTGNARRVAEQLRDDLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAP 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 766431898  760 DLASLNVAVFGLGDSEYwprkedkHYFNKPSQDLFKRLELLSAKALIplglgDDQDAD-GFQTAYSEWEPKLWEAL 834
Cdd:PRK10953  142 KLENTAFAVFGLGDTSY-------EFFCQAGKDFDSKLAELGAERLL-----DRVDADvEYQAAASEWRARVVDAL 205
PRK06703 PRK06703
flavodoxin; Provisional
 686-776 8.62e-09

flavodoxin; Provisional


Pssm-ID: 235854 [Multi-domain]  Cd Length: 151  Bit Score: 55.92  E-value: 8.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  686 YASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKNdtdLDLASLN 765
Cdd:PRK06703    8 YASMSGNTEDIADLIKVSLDAFDHEVVLQEMDGMDAEELLAYDGIILGSYTWGDGDLPYEAEDFHEDLEN---IDLSGKK 84

                          90
                  ....*....|.
gi 766431898  766 VAVFGLGDSEY 776
Cdd:PRK06703   85 VAVFGSGDTAY 95
PRK09267 PRK09267
flavodoxin FldA; Validated
 684-775 8.15e-08

flavodoxin FldA; Validated


Pssm-ID: 236439 [Multi-domain]  Cd Length: 169  Bit Score: 53.30  E-value: 8.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  684 VYYASDGGNAANLAKRLAARASARGlkATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKndtDLDLAS 763
Cdd:PRK09267    6 IFFGSDTGNTEDIAKMIQKKLGKDV--ADVVDIAKASKEDFEAYDLLILGIPTWGYGELQCDWDDFLPELE---EIDFSG 80

                          90
                  ....*....|..
gi 766431898  764 LNVAVFGLGDSE 775
Cdd:PRK09267   81 KKVALFGLGDQE 92
PRK09004 PRK09004
FMN-binding protein MioC; Provisional
 691-776 8.44e-07

FMN-binding protein MioC; Provisional


Pssm-ID: 181608 [Multi-domain]  Cd Length: 146  Bit Score: 49.83  E-value: 8.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  691 GNAANLAKRLAARASARGLKATVL---SMDDIILEELpgeenVVFITSTAGQGEFPQDGKSFWEALKNdTDLDLASLNVA 767
Cdd:PRK09004   13 GGAEYVADHLAEKLEEAGFSTETLhgpLLDDLSASGL-----WLIVTSTHGAGDLPDNLQPFFEELQE-QKPDLSQVRFA 86


                  ....*....
gi 766431898  768 VFGLGDSEY 776
Cdd:PRK09004   87 AIGIGSSEY 95
PRK08105 PRK08105
flavodoxin; Provisional
 691-776 8.76e-06

flavodoxin; Provisional


Pssm-ID: 181230 [Multi-domain]  Cd Length: 149  Bit Score: 47.19  E-value: 8.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  691 GNAANLAKRLAARASARGLKATVLSMDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKnDTDLDLASLNVAVFG 770
Cdd:PRK08105   13 GNALLVAEEAEAILTAQGHEVTLFEDPELSDWQPYQDELVLVVTSTTGQGDLPDSIVPLFQALK-DTAGYQPNLRYGVIA 91


                  ....*.
gi 766431898  771 LGDSEY 776
Cdd:PRK08105   92 LGDSSY 97
PRK09271 PRK09271
flavodoxin; Provisional
 686-799 2.88e-03

flavodoxin; Provisional


Pssm-ID: 181744  Cd Length: 160  Bit Score: 40.17  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  686 YASDGGNAANLAKRLAARASARGLKATVLSMDDIILEELP--GEENVVFI--TSTAGQGEFPQDGKSFWEALkndTDLDL 761
Cdd:PRK09271    7 YASLSGNTREVAREIEERCEEAGHEVDWVETDVQTLAEYPldPEDYDLYLlgTWTDNAGRTPPEMKRFIAEL---AETIG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 766431898  762 ASLNVAVFGLGDS----EYWPRKEDK--HYFNKPsqdlFKRLEL 799
Cdd:PRK09271   84 KPPNVAVFGTGETqwgeEYYCGAVHRmaRFFGSS----YPRLKI 123
PRK06756 PRK06756
flavodoxin; Provisional
 686-776 4.31e-03

flavodoxin; Provisional


Pssm-ID: 168663 [Multi-domain]  Cd Length: 148  Bit Score: 39.48  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431898  686 YASDGGNAANLAKRLAARASARGLKATVLS-MDDIILEELPGEENVVFITSTAGQGEFPQDGKSFWEALKndtDLDLASL 764
Cdd:PRK06756    8 FASMSGNTEEMADHIAGVIRETENEIEVIDiMDSPEASILEQYDGIILGAYTWGDGDLPDDFLDFYDAMD---SIDLTGK 84

                          90
                  ....*....|..
gi 766431898  765 NVAVFGLGDSEY 776
Cdd:PRK06756   85 KAAVFGSCDSAY 96
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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