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Conserved domains on  [gi|446550804|ref|WP_000628150|]
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MULTISPECIES: pyruvate:ferredoxin (flavodoxin) oxidoreductase [Enterobacteriaceae]

Protein Classification

pyruvate:ferredoxin (flavodoxin) oxidoreductase( domain architecture ID 1000199)

pyruvate:ferredoxin (flavodoxin) oxidoreductase catalyzes the interconversion of pyruvate and acetyl-CoA, the electron acceptor being either ferredoxin or flavodoxin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pyruv_ox_red super family cl31176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
1-1166 0e+00

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


The actual alignment was detected with superfamily member TIGR02176:

Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 1605.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804     1 MITIDGNGAVASVAFRTSEVIAIYPITPSSTMAEQADAWAGNGLKNVWGDTPRVVEMQSEAGAIATVHGALQTGALSTSF 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    81 TSSQGLLLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   161 VPFIHFFDGFRTSHEINKIVPLADDTILDLMPQAEIDAHRARALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGSVRSV 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   321 AVLDRTKEPGAQAEPLYLDVMTALAEAFnngerETLPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKARFTVGIYDDV 400
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYEMG-----EAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   401 TNLSLPLPEN-TLPNSAKLEALFYGLGSDGSVSATKNNIKIIGNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAY 479
Cdd:TIGR02176  396 TGTSLPVDEFfDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTY 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   480 LISQADFVGCHQLQFIDKYQMAERLKPGGIFLLNTPYSADEVWSRLPQEVQAVLNQKKARFYVINAAKIARECGLAARIN 559
Cdd:TIGR02176  476 LVTEADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRIN 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   560 TVMQMAFFHLTQILPGDSALAELQGAIAKSYSSKGQDLVERNWQALALARESVEEVPLQPVNPHSANRPPVVSDAAPDFV 639
Cdd:TIGR02176  556 TIMQTAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFV 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   640 KTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIAEEIPIWKEELCTQCNHCVAACPHSAIRAKVVPPEAMENAPA 719
Cdd:TIGR02176  636 KNVVRPINAQEGDDLPVSAFPADGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPA 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   720 SLHSLDVKSRDMRGQKYVLQVAPEDCTGCNLCVEVCPAKDrqnpeiKAINMMSRLEHVEEEKINYDFFLNLPEIDRsKLE 799
Cdd:TIGR02176  716 GFKSLDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKE------KALVMQPLAEQREAQVANWEFAINIPEKDN-KLN 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   800 RIDIRTSQLITPLFEYSGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYTTDANGRGPAWANSLFEDN 879
Cdd:TIGR02176  789 IDTVKGSQFQRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDN 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   880 AEFGLGFRLTVDQHRVRVLRLLDQFADKIPAE------LLTALKSDATPEVRREQVAALRQQL--NDVAEAHELLRDADA 951
Cdd:TIGR02176  869 AEFGYGMRLSMDKRRERLAELAAKALESDIASgdlkaaLNGWLAGKNDIEKSKERVAKLKKLLagEKDDLLKEIYAVSDL 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   952 LVEKSIWLIGGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMM 1031
Cdd:TIGR02176  949 FVKKSVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMT 1028
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  1032 YGHVYVAQISLGAQLNQTVKAIQEAEAYPGPSLIIAYSPCEEHGYDLALSHDQMRQLTA--TGFWPLYRFDPRRADEGKL 1109
Cdd:TIGR02176 1029 YGYVYVAQVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAveSGYWPLYRYNPRLAEQGKN 1108
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 446550804  1110 PLALDSRPPSVALEETLLHEQRFRRLNSQQPEVAEQLWKDAAADLQKRYDFLAQMAG 1166
Cdd:TIGR02176 1109 PFQLDSKEPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
 
Name Accession Description Interval E-value
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
1-1166 0e+00

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 1605.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804     1 MITIDGNGAVASVAFRTSEVIAIYPITPSSTMAEQADAWAGNGLKNVWGDTPRVVEMQSEAGAIATVHGALQTGALSTSF 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    81 TSSQGLLLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   161 VPFIHFFDGFRTSHEINKIVPLADDTILDLMPQAEIDAHRARALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGSVRSV 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   321 AVLDRTKEPGAQAEPLYLDVMTALAEAFnngerETLPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKARFTVGIYDDV 400
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYEMG-----EAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   401 TNLSLPLPEN-TLPNSAKLEALFYGLGSDGSVSATKNNIKIIGNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAY 479
Cdd:TIGR02176  396 TGTSLPVDEFfDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTY 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   480 LISQADFVGCHQLQFIDKYQMAERLKPGGIFLLNTPYSADEVWSRLPQEVQAVLNQKKARFYVINAAKIARECGLAARIN 559
Cdd:TIGR02176  476 LVTEADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRIN 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   560 TVMQMAFFHLTQILPGDSALAELQGAIAKSYSSKGQDLVERNWQALALARESVEEVPLQPVNPHSANRPPVVSDAAPDFV 639
Cdd:TIGR02176  556 TIMQTAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFV 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   640 KTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIAEEIPIWKEELCTQCNHCVAACPHSAIRAKVVPPEAMENAPA 719
Cdd:TIGR02176  636 KNVVRPINAQEGDDLPVSAFPADGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPA 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   720 SLHSLDVKSRDMRGQKYVLQVAPEDCTGCNLCVEVCPAKDrqnpeiKAINMMSRLEHVEEEKINYDFFLNLPEIDRsKLE 799
Cdd:TIGR02176  716 GFKSLDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKE------KALVMQPLAEQREAQVANWEFAINIPEKDN-KLN 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   800 RIDIRTSQLITPLFEYSGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYTTDANGRGPAWANSLFEDN 879
Cdd:TIGR02176  789 IDTVKGSQFQRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDN 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   880 AEFGLGFRLTVDQHRVRVLRLLDQFADKIPAE------LLTALKSDATPEVRREQVAALRQQL--NDVAEAHELLRDADA 951
Cdd:TIGR02176  869 AEFGYGMRLSMDKRRERLAELAAKALESDIASgdlkaaLNGWLAGKNDIEKSKERVAKLKKLLagEKDDLLKEIYAVSDL 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   952 LVEKSIWLIGGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMM 1031
Cdd:TIGR02176  949 FVKKSVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMT 1028
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  1032 YGHVYVAQISLGAQLNQTVKAIQEAEAYPGPSLIIAYSPCEEHGYDLALSHDQMRQLTA--TGFWPLYRFDPRRADEGKL 1109
Cdd:TIGR02176 1029 YGYVYVAQVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAveSGYWPLYRYNPRLAEQGKN 1108
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 446550804  1110 PLALDSRPPSVALEETLLHEQRFRRLNSQQPEVAEQLWKDAAADLQKRYDFLAQMAG 1166
Cdd:TIGR02176 1109 PFQLDSKEPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
811-1166 0e+00

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: 636.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  811 PLFEYSGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYTTDANGRGPAWANSLFEDNAEFGLGFRLTV 890
Cdd:cd03377     1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  891 DQHRVRVLRLLDQFADKI-PAELLTALKSDATPEV----RREQVAALRQQLNDV--AEAHELLRDADALVEKSIWLIGGD 963
Cdd:cd03377    81 DQRRERARELVQKLIEKIgDEELKTLLNAWLATEDdieeSRERVAKLKPLLAAEkdELAKELLSLADYLVKKSVWIIGGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  964 GWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQISLG 1043
Cdd:cd03377   161 GWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQIALG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1044 AQLNQTVKAIQEAEAYPGPSLIIAYSPCEEHGY--DLALSHDQMRQLTATGFWPLYRFDPRRADEGKLPLALDSRPPSVA 1121
Cdd:cd03377   241 ANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIkgGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEPDGP 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 446550804 1122 LEETLLHEQRFRRLNSQQPEVAEQLWKDAAADLQKRYDFLAQMAG 1166
Cdd:cd03377   321 VEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
1-394 3.50e-127

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440438 [Multi-domain]  Cd Length: 372  Bit Score: 394.45  E-value: 3.50e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    1 MITIDGNGAVA-SVAFRTSEVIAIYPITPSSTMAEQADAWAGNglKNVwgdtpRVVEMQSEAGAIATVHGALQTGALSTS 79
Cdd:COG0674     3 RVLMDGNEAVAlGAIAAGCRVIAAYPITPSTEIAEYLAEWLAE--LGG-----VVVQAESEIAAIGAVIGASAAGARAMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   80 FTSSQGLLLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAV-----RQTGCAMLCAANVQEAQDFALISHI 154
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  155 ATLKSRVPFIHFFDGFRTSHEINkiVPLADDTILDLMPQAEidAHRARALNpEHPVIRGTSANPDTYFQS---REATNPw 231
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEEP--VELPDDEEVKILPRPE--EYRPYALD-EDPRAIPGTAQPDVYFTGlehDETEDP- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  232 yDAVYDHVEQAMNDFSAATgRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQ 311
Cdd:COG0674   230 -ENAEKMVEKRMRKFEKIR-DELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEALRE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  312 ALpGSVRSVAVLDRTKEpGaqaePLYLDVMTALAeafnngeretLPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKar 391
Cdd:COG0674   308 AL-KGVKKVAVVERNKS-G----QLALDVRAALG----------ADRVVGGIYGLGGRPFTPEEILAVIEELLKGAPK-- 369

                  ...
gi 446550804  392 FTV 394
Cdd:COG0674   370 FTL 372
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
13-244 1.54e-99

Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 396432  Cd Length: 230  Bit Score: 314.97  E-value: 1.54e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    13 VAFRTS-EVIAIYPITPSSTMAEQADAWAGNGLKNVwgdtPRVVEMQSEAGAIATVHGALQTGALSTSFTSSQGLLLMIP 91
Cdd:pfam01855    1 AAIAAGvDVIAAYPITPSSEIAEEAAEWAANGEKGD----VVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    92 TLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSRVPFIHFFDGFR 171
Cdd:pfam01855   77 NLGKAAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446550804   172 TSHEINKIVPLADDTILDLMPQAEIDAHRAR-ALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVEQAMN 244
Cdd:pfam01855  157 TSHEREKVELPPDEDEKDLIDEFLPPYKRKRyGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVMK 230
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
5-396 2.00e-53

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 192.67  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    5 DGNGAvASVAFRTSE--VIAIYPITPSSTMAEQADAWAGNGLknVWGDtprVVEMQSEAGAIATVHGALQTGALSTSFTS 82
Cdd:PRK09622   14 DGNTA-ASNALRQAQidVVAAYPITPSTPIVQNYGSFKANGY--VDGE---FVMVESEHAAMSACVGAAAAGGRVATATS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   83 SQGLLLMIPTLYKLAGELTPFVLHVAARTVAThALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALIS-HIAT-LKSR 160
Cdd:PRK09622   88 SQGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFTLMAfKIAEdQKVR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  161 VPFIHFFDGFRTSHEINKIVPLADDTILDLMpqAEIDAHRArALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:PRK09622  167 LPVIVNQDGFLCSHTAQNVRPLSDEVAYQFV--GEYQTKNS-MLDFDKPVTYGAQTEEDWHFEHKAQLHHALMSSSSVIE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGsVRSV 320
Cdd:PRK09622  244 EVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKN-LKAL 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446550804  321 AVLDRTKePGAQAEPLYLDVMTALaeaFNNGERETlPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKARFTVGI 396
Cdd:PRK09622  323 AILDRSS-PAGAMGALFNEVTSAV---YQTQGTKH-PVVSNYIYGLGGRDMTIAHLCEIFEELNENALAGKLTHPT 393
EKR smart00890
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
627-679 3.59e-25

Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) and the 4Fe-4S binding domain Fer4. It contains a characteristic EKR sequence motif. The exact function of this domain is not known.


Pssm-ID: 197958 [Multi-domain]  Cd Length: 57  Bit Score: 99.23  E-value: 3.59e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 446550804    627 RPPVVSDAAPDFVKTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIAE 679
Cdd:smart00890    5 EPPPVPEEAPEFVKNVVAPMNAGEGDDLPVSAFPEDGTFPTGTAAYEKRGIAV 57
 
Name Accession Description Interval E-value
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
1-1166 0e+00

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 1605.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804     1 MITIDGNGAVASVAFRTSEVIAIYPITPSSTMAEQADAWAGNGLKNVWGDTPRVVEMQSEAGAIATVHGALQTGALSTSF 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    81 TSSQGLLLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   161 VPFIHFFDGFRTSHEINKIVPLADDTILDLMPQAEIDAHRARALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGSVRSV 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   321 AVLDRTKEPGAQAEPLYLDVMTALAEAFnngerETLPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKARFTVGIYDDV 400
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYEMG-----EAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDV 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   401 TNLSLPLPEN-TLPNSAKLEALFYGLGSDGSVSATKNNIKIIGNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAY 479
Cdd:TIGR02176  396 TGTSLPVDEFfDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTY 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   480 LISQADFVGCHQLQFIDKYQMAERLKPGGIFLLNTPYSADEVWSRLPQEVQAVLNQKKARFYVINAAKIARECGLAARIN 559
Cdd:TIGR02176  476 LVTEADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRIN 555
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   560 TVMQMAFFHLTQILPGDSALAELQGAIAKSYSSKGQDLVERNWQALALARESVEEVPLQPVNPHSANRPPVVSDAAPDFV 639
Cdd:TIGR02176  556 TIMQTAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFV 635
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   640 KTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIAEEIPIWKEELCTQCNHCVAACPHSAIRAKVVPPEAMENAPA 719
Cdd:TIGR02176  636 KNVVRPINAQEGDDLPVSAFPADGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPA 715
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   720 SLHSLDVKSRDMRGQKYVLQVAPEDCTGCNLCVEVCPAKDrqnpeiKAINMMSRLEHVEEEKINYDFFLNLPEIDRsKLE 799
Cdd:TIGR02176  716 GFKSLDAKGKELEGMKFRIQISPLDCTGCGNCVDICPAKE------KALVMQPLAEQREAQVANWEFAINIPEKDN-KLN 788
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   800 RIDIRTSQLITPLFEYSGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYTTDANGRGPAWANSLFEDN 879
Cdd:TIGR02176  789 IDTVKGSQFQRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDN 868
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   880 AEFGLGFRLTVDQHRVRVLRLLDQFADKIPAE------LLTALKSDATPEVRREQVAALRQQL--NDVAEAHELLRDADA 951
Cdd:TIGR02176  869 AEFGYGMRLSMDKRRERLAELAAKALESDIASgdlkaaLNGWLAGKNDIEKSKERVAKLKKLLagEKDDLLKEIYAVSDL 948
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   952 LVEKSIWLIGGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMM 1031
Cdd:TIGR02176  949 FVKKSVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMT 1028
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  1032 YGHVYVAQISLGAQLNQTVKAIQEAEAYPGPSLIIAYSPCEEHGYDLALSHDQMRQLTA--TGFWPLYRFDPRRADEGKL 1109
Cdd:TIGR02176 1029 YGYVYVAQVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAveSGYWPLYRYNPRLAEQGKN 1108
                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 446550804  1110 PLALDSRPPSVALEETLLHEQRFRRLNSQQPEVAEQLWKDAAADLQKRYDFLAQMAG 1166
Cdd:TIGR02176 1109 PFQLDSKEPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
811-1166 0e+00

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: 636.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  811 PLFEYSGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYTTDANGRGPAWANSLFEDNAEFGLGFRLTV 890
Cdd:cd03377     1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  891 DQHRVRVLRLLDQFADKI-PAELLTALKSDATPEV----RREQVAALRQQLNDV--AEAHELLRDADALVEKSIWLIGGD 963
Cdd:cd03377    81 DQRRERARELVQKLIEKIgDEELKTLLNAWLATEDdieeSRERVAKLKPLLAAEkdELAKELLSLADYLVKKSVWIIGGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  964 GWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQISLG 1043
Cdd:cd03377   161 GWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQIALG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1044 AQLNQTVKAIQEAEAYPGPSLIIAYSPCEEHGY--DLALSHDQMRQLTATGFWPLYRFDPRRADEGKLPLALDSRPPSVA 1121
Cdd:cd03377   241 ANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIkgGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEPDGP 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 446550804 1122 LEETLLHEQRFRRLNSQQPEVAEQLWKDAAADLQKRYDFLAQMAG 1166
Cdd:cd03377   321 VEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
1-394 3.50e-127

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440438 [Multi-domain]  Cd Length: 372  Bit Score: 394.45  E-value: 3.50e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    1 MITIDGNGAVA-SVAFRTSEVIAIYPITPSSTMAEQADAWAGNglKNVwgdtpRVVEMQSEAGAIATVHGALQTGALSTS 79
Cdd:COG0674     3 RVLMDGNEAVAlGAIAAGCRVIAAYPITPSTEIAEYLAEWLAE--LGG-----VVVQAESEIAAIGAVIGASAAGARAMT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   80 FTSSQGLLLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAV-----RQTGCAMLCAANVQEAQDFALISHI 154
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  155 ATLKSRVPFIHFFDGFRTSHEINkiVPLADDTILDLMPQAEidAHRARALNpEHPVIRGTSANPDTYFQS---REATNPw 231
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEEP--VELPDDEEVKILPRPE--EYRPYALD-EDPRAIPGTAQPDVYFTGlehDETEDP- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  232 yDAVYDHVEQAMNDFSAATgRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQ 311
Cdd:COG0674   230 -ENAEKMVEKRMRKFEKIR-DELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEALRE 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  312 ALpGSVRSVAVLDRTKEpGaqaePLYLDVMTALAeafnngeretLPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKar 391
Cdd:COG0674   308 AL-KGVKKVAVVERNKS-G----QLALDVRAALG----------ADRVVGGIYGLGGRPFTPEEILAVIEELLKGAPK-- 369

                  ...
gi 446550804  392 FTV 394
Cdd:COG0674   370 FTL 372
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
13-244 1.54e-99

Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N terminal structural domain of the pyruvate ferredoxin oxidoreductase. This domain binds thiamine diphosphate, and along with domains II and IV, is involved in inter subunit contacts. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 396432  Cd Length: 230  Bit Score: 314.97  E-value: 1.54e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    13 VAFRTS-EVIAIYPITPSSTMAEQADAWAGNGLKNVwgdtPRVVEMQSEAGAIATVHGALQTGALSTSFTSSQGLLLMIP 91
Cdd:pfam01855    1 AAIAAGvDVIAAYPITPSSEIAEEAAEWAANGEKGD----VVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    92 TLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSRVPFIHFFDGFR 171
Cdd:pfam01855   77 NLGKAAGERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446550804   172 TSHEINKIVPLADDTILDLMPQAEIDAHRAR-ALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVEQAMN 244
Cdd:pfam01855  157 TSHEREKVELPPDEDEKDLIDEFLPPYKRKRyGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVMK 230
PorG COG1014
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ...
417-854 4.30e-71

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440638 [Multi-domain]  Cd Length: 424  Bit Score: 244.21  E-value: 4.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  417 KLEALFYGLGSDGSVSATKNNIKIIGNsTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAyLISQADFVGCHQLQFID 496
Cdd:COG1014     4 DLEIRIAGVGGQGVVTAGKILAKAAMR-EGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSP-LIDEADVLIALDPEELD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  497 KYqmAERLKPGGIFLLNTPYSADEVWsRLPQEvqaVLNQKKARFYVINAAKIARE-CGLAARINTVMQMAFFHLTQIlpg 575
Cdd:COG1014    82 RV--LDGLKPGGVLIVNSSLVPPEVW-RLPQE---ALERKDIRVYVIDATKIAKElLGNARVANTVMLGALAALLGL--- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  576 dsALAELQGAIAKSYSSKGQDLVERNWQALALARESVEEVPLQPvnphsANRPPVVSDAAPDFVKTVTAAMLAGLGDALP 655
Cdd:COG1014   153 --PLEALEEAIEETFGKKGEKVVELNLKAFEAGYEAAKEVFALA-----AAPAPLVLLAGNAAAALGAAAGGAAFAAAYP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  656 VSALPPDGTWPMGTTRWEKRNIAEEIPIWKEELCTQCNHCVAACPHSAIRAKVVPPEAMENAPASLHSLDVKSRDMRGQK 735
Cdd:COG1014   226 ITPSTSLIEAAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGGAALATEGLGLAGMTETPVVAVAAPRPG 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  736 YVLQVAPEDCTGCNLCVEVCPAKDRQNPEIKAINMMSRLEHVEEEKINYDFFLNLPEIDRSKLERIDIRTSQLITPLFEY 815
Cdd:COG1014   306 PGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLLLLQLLVLLLTDLLLLLLDLLR 385
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 446550804  816 SGACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGN 854
Cdd:COG1014   386 RRAGLGAEEAEARRKLLAAEGRAARAAGGGGGGGGGGGL 424
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
812-1103 6.26e-67

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: 225.44  E-value: 6.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  812 LFEYSGACSGCGETPYIKLLTQLYG--DRMLIANATGCSSIYGGNLPSTPYttdangrGPAWANSLFEDNAEFGLGFRlt 889
Cdd:cd02018     1 LTEEHGACAGCGEVTAVRVVLAALPapEDTVIANSTGCSSVYASTAPFNSW-------AVPWVNSLFEDANAVASGLK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  890 vdqhrvrvlrlldqfadkipaELLTALksdaTPEvrreqvaalrqqlndvaeahellrDADALVEKSIWLIGGDGWAYDI 969
Cdd:cd02018    72 ---------------------RGLKAR----FPK------------------------DRELDKKKDVVVIGGDGATYDI 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  970 GFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQISLGAQlNQT 1049
Cdd:cd02018   103 GFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAATHGCVYVARLSPALK-KHF 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446550804 1050 VKAIQEAEAY-PGPSLIIAYSPCE-EHGYDLALSHDQMRQLTATGFWPLYRFDPRR 1103
Cdd:cd02018   182 LKVVKEAISRtDGPTFIHAYTPCItEWGIGSGKSLELARKAVKSRMFPLFEYDPRE 237
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
5-396 2.00e-53

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 192.67  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    5 DGNGAvASVAFRTSE--VIAIYPITPSSTMAEQADAWAGNGLknVWGDtprVVEMQSEAGAIATVHGALQTGALSTSFTS 82
Cdd:PRK09622   14 DGNTA-ASNALRQAQidVVAAYPITPSTPIVQNYGSFKANGY--VDGE---FVMVESEHAAMSACVGAAAAGGRVATATS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   83 SQGLLLMIPTLYKLAGELTPFVLHVAARTVAThALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALIS-HIAT-LKSR 160
Cdd:PRK09622   88 SQGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFTLMAfKIAEdQKVR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  161 VPFIHFFDGFRTSHEINKIVPLADDTILDLMpqAEIDAHRArALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:PRK09622  167 LPVIVNQDGFLCSHTAQNVRPLSDEVAYQFV--GEYQTKNS-MLDFDKPVTYGAQTEEDWHFEHKAQLHHALMSSSSVIE 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGsVRSV 320
Cdd:PRK09622  244 EVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKN-LKAL 322
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446550804  321 AVLDRTKePGAQAEPLYLDVMTALaeaFNNGERETlPRVIGGRYGLSSKEFGPDCVLAVFAELNAAKPKARFTVGI 396
Cdd:PRK09622  323 AILDRSS-PAGAMGALFNEVTSAV---YQTQGTKH-PVVSNYIYGLGGRDMTIAHLCEIFEELNENALAGKLTHPT 393
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
816-1142 7.92e-53

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440637 [Multi-domain]  Cd Length: 262  Bit Score: 186.12  E-value: 7.92e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  816 SGACSGCGETPYIKLLTQ-----LYGDRMLIANATGCSSIYGGnlpstPYTTDangrgpaWANSLFEDNAEFGLGFRLtv 890
Cdd:COG1013    13 HRWCPGCGHGIILRLLLKaldelLDGDKTVVVSGIGCSSVAPG-----YFNVP-------GFHTLHGRAAAVATGIKL-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  891 dqhrvrvlrlldqfadkipaelltalksdatpevrreqvaalrqqlndvaeahellrdadALVEKSIWLIGGDGWAYDIG 970
Cdd:COG1013    79 ------------------------------------------------------------ANPDLTVIVFGGDGDTYDIG 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  971 FGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQISLGaQLNQTV 1050
Cdd:COG1013    99 GNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVARASVG-DPKDLK 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1051 KAIQEAEAYPGPSLIIAYSPCEEH-GYDLALSHDQMRqltaTGFWPLYRFDPRradeGKLPLALDSRPPsVALEETLLHE 1129
Cdd:COG1013   178 KKIKKAIEHKGFSFIEVLSPCPTGwGRDPSKTIEWAK----EGMWPLYEYDPG----EKLRLTYEPKDK-IPVGEFLKNQ 248
                         330
                  ....*....|....
gi 446550804 1130 QRFR-RLNSQQPEV 1142
Cdd:COG1013   249 GRFEeLIEEIQKPV 262
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
6-169 7.60e-51

Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase alpha subunit (IOR-alpha), and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain, of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit (IOR-alpha), and related proteins, subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzyme Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit. This subfamily includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate.


Pssm-ID: 132917 [Multi-domain]  Cd Length: 160  Bit Score: 176.54  E-value: 7.60e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    6 GNGAVASVAFRTS-EVIAIYPITPSSTMAEQADAWAgnglknVWGDTPRVVEMQSEAGAIATVHGALQTGALSTSFTSSQ 84
Cdd:cd07034     1 GNEAVARGALAAGvDVVAAYPITPSTEIAETLAKAV------LGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   85 GLLLMIPTLYKLAGELTPFVLHVAARTVATHALsIFGDHSDVMAVRQTG--CAMLCAANVQEAQDFALISHIATLKSRVP 162
Cdd:cd07034    75 GLNLMAEALYLAAGAELPLVIVVAQRPGPSTGL-PKPDQSDLMAARYGGhpWPVLAPSSVQEAFDLALEAFELAEKYRLP 153

                  ....*..
gi 446550804  163 FIHFFDG 169
Cdd:cd07034   154 VIVLSDG 160
vorA PRK08366
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
4-363 1.78e-36

2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 169406 [Multi-domain]  Cd Length: 390  Bit Score: 142.83  E-value: 1.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    4 IDGNGAVASVAFRTS-EVIAIYPITPSSTMAEQADAWAGNGLKNVwgdtpRVVEMQSEAGAIATVHGALQTGALSTSFTS 82
Cdd:PRK08366    6 VSGNYAAAYAALHARvQVVAAYPITPQTSIIEKIAEFIANGEADI-----QYVPVESEHSAMAACIGASAAGARAFTATS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   83 SQGLLLMIPTLYKLAGELTPFVLHVAARTVAThALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSRVP 162
Cdd:PRK08366   81 AQGLALMHEMLHWAAGARLPIVMVDVNRAMAP-PWSVWDDQTDSLAQRDTGWMQFYAENNQEVYDGVLMAFKVAETVNLP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  163 FIHFFDGFRTSHEINkivpladdtILDLMPQAEIDAHraraLNP----------EHPVIRGTSANPDTYFQSREATNPWY 232
Cdd:PRK08366  160 AMVVESAFILSHTYD---------VVEMIPQELVDEF----LPPrkplysladfDNPISVGALATPADYYEFRYKIAKAM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  233 DAVYDHVEQAMNDFSAATGRQY-QPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQ 311
Cdd:PRK08366  227 EEAKKVIKEVGKEFGERFGRDYsQMIETYYTDDADFVFMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPFPKEELYE 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446550804  312 aLPGSVRSVAVLDRTKEPGaQAEPLYLDVMTALaeaFNNGERETLPRVI---GGR 363
Cdd:PRK08366  307 -IAESVKGIAVLDRNFSFG-QEGILFTEAKGAL---YNTDARPIMKNYIvglGGR 356
porA PRK08367
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed
4-363 4.87e-36

pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 181403 [Multi-domain]  Cd Length: 394  Bit Score: 141.56  E-value: 4.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    4 IDGNGAVASVA-FRTSEVIAIYPITPSSTMAEQADAWAGNGLKNVwgdtpRVVEMQSEAGAIATVHGALQTGALSTSFTS 82
Cdd:PRK08367    7 MKANEAAAWAAkLAKPKVIAAFPITPSTLVPEKISEFVANGELDA-----EFIKVESEHSAISACVGASAAGVRTFTATA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   83 SQGLLLMIPTLYKLAGELTPFVLHVAARTVAThALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSRV- 161
Cdd:PRK08367   82 SQGLALMHEVLFIAAGMRLPIVMAIGNRALSA-PINIWNDWQDTISQRDTGWMQFYAENNQEALDLILIAFKVAEDERVl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  162 -PFIHFFDGFRTSHEINKiVPLADDTILDLMpQAEIDAHRArALNPEHPVIRGTSANPDTYFQSREATNPWYDAVYDHVE 240
Cdd:PRK08367  161 lPAMVGFDAFILTHTVEP-VEIPDQEVVDEF-LGEYEPKHA-YLDPARPITQGALAFPAHYMEARYTVWEAMENAKKVID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  241 QAMNDFSAATGRQYQPFEYYGHPQAERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHlLQALPGSVRSV 320
Cdd:PRK08367  238 EAFAEFEKKFGRKYQKIEEYRTEDAEIIFVTMGSLAGTLKEFVDKLREEGYKVGAAKLTVYRPFPVEE-IRALAKKAKVL 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 446550804  321 AVLDRTKEPGaqaepLYLDVMTALAEAFNNgERETlPRVI------GGR 363
Cdd:PRK08367  317 AFLEKNISFG-----LGGAVFADASAALVN-ESEK-PKILdfiiglGGR 358
POR pfam01558
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ...
426-610 6.49e-35

Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large protein pyruvate-flavodoxin oxidoreductase and the whole pyruvate ferredoxin oxidoreductase gamma subunit protein. It is not known whether the gamma subunit has a catalytic or regulatory role. Pyruvate oxidoreductase (POR) catalyzes the final step in the fermentation of carbohydrates in anaerobic microorganizms. This involves the oxidative decarboxylation of pyruvate with the participation of thiamine followed by the transfer of an acetyl moiety to coenzyme A for the synthesis of acetyl-CoA. The family also includes pyruvate flavodoxin oxidoreductase as encoded by the nifJ gene in cyanobacterium which is required for growth on molecular nitrogen when iron is limited.


Pssm-ID: 426323 [Multi-domain]  Cd Length: 172  Bit Score: 131.27  E-value: 6.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   426 GSDGSVSATKNNIKIIgNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGCHQLQFIDKYqmAERLK 505
Cdd:pfam01558    1 GGQGVVTAGKILAKAA-ARAGYYVQATPEYGSEIRGGPVVSHVRISDEPIVPAIPVGEADLLVALDPETLDRH--LDGLK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   506 PGGIFLLNTPYSADE-VWSRLPQEVQAvlnqkkARFYVINAAKIARECGLAAR-INTVMQMAFFHLTQiLPGDSALAelq 583
Cdd:pfam01558   78 PGGIIIYNSSEVPPElLEKDLPAYPRL------ARVYGVPATEIAKEAGGNSRaANTVMLGALAALLG-LPLEALEE--- 147
                          170       180
                   ....*....|....*....|....*..
gi 446550804   584 gAIAKSYSSKgQDLVERNWQALALARE 610
Cdd:pfam01558  148 -AIKKRFPGK-AKVIELNLKAFRAGYE 172
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
817-1100 9.72e-29

Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. 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. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.


Pssm-ID: 239471 [Multi-domain]  Cd Length: 235  Bit Score: 115.80  E-value: 9.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  817 GACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYttdangRGPaWANSLFEDNAEFGLGFRltvdqhrvr 896
Cdd:cd03376     6 RACAGCGAALALRHVLKALGPDTVVVNPTGCLEVITTPYPYTAW------RVP-WIHVAFENAAAVASGIE--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  897 vlrlldqfadkipaelltalksdatpevrreqvAALRQQLNDvaeahellRDADALVeksiwlIGGDGWAYDIGFGGLDH 976
Cdd:cd03376    70 ---------------------------------AALKALGRG--------KDITVVA------FAGDGGTADIGFQALSG 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  977 VLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKF---GEH--GKRKARKDLGVSMMMYGHVYVAQISlGAQLNQTVK 1051
Cdd:cd03376   103 AAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTtpvGKVsfGKKQPKKDLPLIMAAHNIPYVATAS-VAYPEDLYK 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 446550804 1052 AIQEAEAYPGPSLIIAYSPC-EEHGYDLALSHDQMRQLTATGFWPLYRFD 1100
Cdd:cd03376   182 KVKKALSIEGPAYIHILSPCpTGWRFDPSKTIEIARLAVETGFWPLYEYE 231
EKR pfam10371
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
626-678 1.57e-27

Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) pfam01558 and the 4Fe-4S binding domain Fer4 pfam00037. It contains a characteriztic EKR sequence motif. The exact function of this domain is not known.


Pssm-ID: 431238 [Multi-domain]  Cd Length: 54  Bit Score: 105.63  E-value: 1.57e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 446550804   626 NRPPVVSDAAPDFVKTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIA 678
Cdd:pfam10371    2 ELPPPVPEDAPEFVKNVLAPMNAGEGDELPVSAFPEDGTFPTGTSAYEKRGIA 54
NapF COG1145
Ferredoxin [Energy production and conversion];
510-776 1.12e-26

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 110.20  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  510 FLLNTPYSADEVWSRLPQEVQAVLNQKKARFYVINAAKIARECGLAARINTVMQMAFFHLTQILPGDSALAELQGAIAKS 589
Cdd:COG1145     3 LLLDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGEIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  590 YSSKGQDLVERNWQALALARESVEEVPLQPVNPHSANRPPVVSDAAPDFVKTVTAAMLAGLGDALPVSALPPDGTWPMGT 669
Cdd:COG1145    83 RVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  670 TRWEKRNIAEEIPIWK--EELCTQCNHCVAACPHSAIRakvvppeamenapaslhsldvksrdMRGQKYVLQVAPEDCTG 747
Cdd:COG1145   163 KIEEELKIAIKKAKAVidAEKCIGCGLCVKVCPTGAIR-------------------------LKDGKPQIVVDPDKCIG 217
                         250       260
                  ....*....|....*....|....*....
gi 446550804  748 CNLCVEVCPAkdrqnpeiKAINMMSRLEH 776
Cdd:COG1145   218 CGACVKVCPV--------GAISLEPKEIE 238
EKR smart00890
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
627-679 3.59e-25

Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some lower eukaryotic species which lies between a POR (pyruvate ferredoxin/flavodoxin oxidoreductase) and the 4Fe-4S binding domain Fer4. It contains a characteristic EKR sequence motif. The exact function of this domain is not known.


Pssm-ID: 197958 [Multi-domain]  Cd Length: 57  Bit Score: 99.23  E-value: 3.59e-25
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 446550804    627 RPPVVSDAAPDFVKTVTAAMLAGLGDALPVSALPPDGTWPMGTTRWEKRNIAE 679
Cdd:smart00890    5 EPPPVPEEAPEFVKNVVAPMNAGEGDDLPVSAFPEDGTFPTGTAAYEKRGIAV 57
PRK11865 PRK11865
pyruvate synthase subunit beta;
818-1148 1.38e-24

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 105.57  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  818 ACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPYttdangRGPaWANSLFEDNAEFGLGFRltvdqhrvrv 897
Cdd:PRK11865   20 ACAGCGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAW------NVP-WIHVAFENAAAVASGIE---------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  898 lrlldqfadkipaelltalksdatpevrreqvAALRQQLNDVaeahellrdadalvekSIWLIGGDGWAYDIGFGGLDHV 977
Cdd:PRK11865   83 --------------------------------RAVKALGKKV----------------NVVAIGGDGGTADIGFQSLSGA 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  978 LSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGK-----RKARKDLGVSMMMYGHVYVAQISLGaQLNQTVKA 1052
Cdd:PRK11865  115 MERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKysrgeDRPKKNMPLIMAAHGIPYVATASIG-YPEDFMEK 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1053 IQEAEAYPGPSLIIAYSPCEEH-GYDLALSHDQMRQLTATGFWPLYRF---DPRRADEGkLPLALDSRPPsvaLEETLLH 1128
Cdd:PRK11865  194 VKKAKEVEGPAYIQVLQPCPTGwGFPPEKTIEIGRLAVETGYWPLFEIengKFKITYEP-LHLDRRTRKP---IEEYLKV 269
                         330       340
                  ....*....|....*....|....
gi 446550804 1129 EQRFRRLNSQQPEVAEQ----LWK 1148
Cdd:PRK11865  270 QGRFKHLTEEDIEILQKyideKWK 293
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
664-781 3.72e-22

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 91.65  E-value: 3.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  664 TWPMGTTRWEKRNIAEEIPIWKEELCTQCNHCVAACPHSAIRakvvppeamenapaslhsldvksrdMRGQKYVlQVAPE 743
Cdd:COG1144     7 TEPGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIR-------------------------VDDGKYY-GIDYD 60
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446550804  744 DCTGCNLCVEVCPAkdrqnpeiKAINMmsrlehVEEEK 781
Cdd:COG1144    61 YCKGCGICAEVCPV--------KAIEM------VPEEK 84
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
9-169 5.87e-21

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.


Pssm-ID: 132915 [Multi-domain]  Cd Length: 154  Bit Score: 90.48  E-value: 5.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804    9 AVASVAFRTS-EVIAIYPITPSSTMAEQADAwagnglknvwGDTPRVVEMQSEAGAIATVHG-ALQTGALSTSFTSSQGL 86
Cdd:cd06586     2 AFAEVLTAWGvRHVFGYPGDEISSLLDALRE----------GDKRIIDTVIHELGAAGAAAGyARAGGPPVVIVTSGTGL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   87 LLMIPTLYKLAGELTPFVLHVAARTVATHALSIFGDHSDVMAVRQTGCAMLCAANVQEAQDFALISHIATLKSRVPFIHF 166
Cdd:cd06586    72 LNAINGLADAAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVR 151

                  ...
gi 446550804  167 FDG 169
Cdd:cd06586   152 LPR 154
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
265-344 1.94e-18

Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic enzyme pyruvate:ferredoxin oxidoreductase and is necessary for inter subunit contacts in conjunction with domains I and IV.


Pssm-ID: 407280 [Multi-domain]  Cd Length: 102  Bit Score: 81.54  E-value: 1.94e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   265 AERVIILMGSAIGTCEEVVDELLIRGEKVGVLKVRLYRPFSAKHLLQALPGsVRSVAVLDRTKEPGAQAePLYLDVMTAL 344
Cdd:pfam17147    1 AEVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEELKELLAG-VKKVVVLDRNISFGSPG-QLGTEVKAAL 78
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
818-1145 2.24e-18

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 87.07  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  818 ACSGCGETPYIKLLTQLYGDRMLIANATGCSSIYGGNLPSTPytTDANgrgpaWANSLFEDNAEFGLGfrltvdqhrvrv 897
Cdd:PRK11864   20 ACPGCGAPLGLRYLLKALGEKTVLVIPASCSTVIQGDTPKSP--LTVP-----VLHTAFAATAAVASG------------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  898 lrlldqfadkipaelltalksdatpevrreqvaalrqqlndVAEAHELLRDADALVekSIWliGGDGWAYDIGFGGLDHV 977
Cdd:PRK11864   81 -----------------------------------------IEEALKARGEKGVIV--VGW--AGDGGTADIGFQALSGA 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  978 LSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQISLgAQLNQTVKAIQEAE 1057
Cdd:PRK11864  116 AERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVATASI-AYPEDFIRKLKKAK 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1058 AYPGPSLIIAYSPCEEhG--YDLALSHDQMRQLTATGFWPLYRFdprraDEGKLPLALDSRPPS-----VALEETLLHEQ 1130
Cdd:PRK11864  195 EIRGFKFIHLLAPCPP-GwrFDPDKTIEIARLAVETGVWPLFEY-----ENGKFKLNSPSKTLLdkkkrKPVEEYLKLQG 268
                         330
                  ....*....|....*
gi 446550804 1131 RFRRLNSQQPEVAEQ 1145
Cdd:PRK11864  269 RFKHLTEEEIKGLQE 283
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
417-756 3.88e-16

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 80.81  E-value: 3.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  417 KLEALFYGLGSDGSVSATKnnikIIGNST---PWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGCHQLQ 493
Cdd:PRK14028    2 RIETVWLGRGGQGIVTATY----IIANAAvidGFYAIANPEFGAERRGAPVKAFLTISKNPIEDQEPVKTPDVAVIFDDK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  494 FIDKYQMA-ERLKPGGIFLLNTpysadevwSRLPQEVQAVLNQKKARFYVINAAKIAREcglaarintvmqmaffHLTQI 572
Cdd:PRK14028   78 LIDPMRFAiDAVKPGGYVILNT--------GKQPEEARKLVGRDDVYIVVLDAIGIARK----------------HLKLD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  573 LPGD---SALAELQG-----AIAKSYSSKGQDLVERNWQALALARESVEEVPLQPVNphsanrppvvSDAAPDFVKTVTA 644
Cdd:PRK14028  134 VPNGplaGAFSKVMGfpsleSIRTAFETQLGKAVEENFAATKEAYEVAVVIPPEKVD----------ASAKPKGIISTTS 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  645 AMLAGLGDAL------PVSALPPDGTWPMGTTRWEKrniaeEIPIWKEELCTQCNHCVAACPHSAIrakvvpPEAMENAP 718
Cdd:PRK14028  204 AFLTGPYELVgwqevnKAGAVFPGSSFPYLTGGWRI-----DKPVIDHSKCIMCRKCWLYCPDDAI------IEAWREAE 272
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 446550804  719 ASlhsldvksrdmRGQKYVLQVAPED---CTGCNLCVEVCP 756
Cdd:PRK14028  273 GP-----------RGRKFRMKMIDFDyqyCKGCGVCAEVCP 302
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
954-1071 2.22e-14

Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.


Pssm-ID: 239470 [Multi-domain]  Cd Length: 193  Bit Score: 72.94  E-value: 2.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  954 EKSIWLIGGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYG 1033
Cdd:cd03375    69 DLTVIVVSGDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAG 148
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446550804 1034 HVYVAQISLGaQLNQTVKAIQEAEAYPGPSLIIAYSPC 1071
Cdd:cd03375   149 ATFVARGFSG-DIKQLKEIIKKAIQHKGFSFVEVLSPC 185
PorC_KorC TIGR02175
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ...
418-612 2.14e-13

2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins (H. pylori) used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes the gamma subunit. In Pyrococcus furious, enzymes active on pyruvate and 2-ketoisovalerate share a common gamma subunit.


Pssm-ID: 274014 [Multi-domain]  Cd Length: 177  Bit Score: 69.69  E-value: 2.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   418 LEALFYGLGSDGSVSATKNNIKIIGNSTPwYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGCHQLQFIDK 497
Cdd:TIGR02175    2 IEIRFHGRGGQGAVTASQLLAEAAFLEGK-YAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQIYEPDYVVVLDPTLLKT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   498 YQMAERLKPGGIFLLNTPYSADEVWsrlpqevqavlnqKKARFYVINAAKIARECGLAARINTVMQMAFFHLTQILPGDS 577
Cdd:TIGR02175   81 VNVTAGLKEDGILIVNTKKDPEELR-------------KELKVYTVDATKIALVVLGRPIVNTPMLGAFAKVTGLVSLES 147
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 446550804   578 alaeLQGAIAKSYSSKgqdLVERNWQALALARESV 612
Cdd:TIGR02175  148 ----LEKAIEESFPGK---LAEANAKAVERAYEEV 175
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
677-773 4.73e-13

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 65.13  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  677 IAEEIPIWKEELCTQCNHCVAACPHSAIRAKvvppeamenapaslhsldvksrdmRGQKYVlqVAPEDCTGCNLCVEVCP 756
Cdd:COG1149     1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKLD------------------------DGGAPV--VDPDLCTGCGACVGVCP 54
                          90
                  ....*....|....*..
gi 446550804  757 AkdrqnpeiKAINMMSR 773
Cdd:COG1149    55 T--------GAITLEER 63
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
686-781 8.10e-13

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 64.38  E-value: 8.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  686 EELCTQCNHCVAACPHSAIRakvvppeaMENAPAslhsldvksrdmrgqKYVLQVAPEDCTGCNLCVEVCPAkdrqnpei 765
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAIT--------IEDGEP---------------GKVYVIDPDKCIGCGLCVEVCPT-------- 49
                          90
                  ....*....|....*.
gi 446550804  766 KAINmMSRLEHVEEEK 781
Cdd:COG1143    50 GAIS-MTPFELAVEDR 64
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
956-1148 1.37e-12

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 69.49  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  956 SIWLIGGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTK---FG--EHGKRKARKDLGVsmm 1030
Cdd:PRK11867   89 TVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKttpYGsiEPPFNPVELALGA--- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804 1031 myGHVYVAQiSLGAQLNQTVKAIQEAEAYPGPSLIIAYSPC------------EEHGYDLalsHDqmrqltATGFWPLYR 1098
Cdd:PRK11867  166 --GATFVAR-GFDSDVKQLTELIKAAINHKGFSFVEILQPCptfnnvntfdwfKERLVKV---HD------AEGYDPTNA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446550804 1099 FDPRRADEGKLPLAL-----DSRPPSvaleETLLHEQRFRRLNSQQPEVAEQLWK 1148
Cdd:PRK11867  234 LAAMKTLEEGDPIPTgifyqVERPTY----EEAVRAQIEGPLALQDLLMGGDTWT 284
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
689-758 2.86e-10

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 57.11  E-value: 2.86e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   689 CTQCNHCVAACPHSAIRAkvvpPEAMENAPASLHSLDVKSRDMRGQKYVLQVApEDCTGCNLCVEVCPAK 758
Cdd:pfam13484    1 CGSCGKCIDACPTGAIVG----PEGVLDARRCISYLTIEKKGLIPDELRCLLG-NRCYGCDICQDVCPWN 65
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
686-756 2.94e-10

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 57.03  E-value: 2.94e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804  686 EELCTQCNHCVAACPHsairakvvppeamenapaslhslDVKSRDMRGQKyVLQVAPEDCTGCNLCVEVCP 756
Cdd:COG1146     7 TDKCIGCGACVEVCPV-----------------------DVLELDEEGKK-ALVINPEECIGCGACELVCP 53
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
682-774 3.98e-10

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 57.05  E-value: 3.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  682 PIWKEELCTQCNHCVAACPHSAIRakvvppeaMENAPASLHsldvksrdmrgqkyvlqvaPEDCTGCNLCVEVCPAKDRQ 761
Cdd:COG2768     6 PYVDEEKCIGCGACVKVCPVGAIS--------IEDGKAVID-------------------PEKCIGCGACIEVCPVGAIK 58
                          90
                  ....*....|...
gi 446550804  762 NPEIKAINMMSRL 774
Cdd:COG2768    59 IEWEEDEEFQEKM 71
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
960-1071 5.86e-10

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 61.82  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  960 IGGDGWAYDIGFGGLDHVLSltENVNILVL--DTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYV 1037
Cdd:PRK05778   94 VGGDGDLASIGGGHFIHAGR--RNIDITVIveNNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFV 171
                          90       100       110
                  ....*....|....*....|....*....|....
gi 446550804 1038 AQiSLGAQLNQTVKAIQEAEAYPGPSLIIAYSPC 1071
Cdd:PRK05778  172 AR-SFAGDVKQLVELIKKAISHKGFAFIDVLSPC 204
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
685-770 7.58e-10

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 55.75  E-value: 7.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   685 KEELCTQCNHCVAACPHSAIRAKVVPPEAMenapaslhsldvksrdmrgqkyvLQVAPEDCTGCNLCVEVCPAKDrqnpe 764
Cdd:pfam14697    4 DEDTCIGCGKCYIACPDTSHQAIVGDGKRH-----------------------HTVIEDECTGCNLCVSVCPVDD----- 55

                   ....*.
gi 446550804   765 ikAINM 770
Cdd:pfam14697   56 --CITM 59
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
689-758 1.00e-09

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 55.23  E-value: 1.00e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   689 CTQCNHCVAACPHSAIRAKvvppeamenapaslhsldvKSRDMRGQKYVlQVAPEDCTGCNLCVEVCPAK 758
Cdd:pfam12838    1 CIGCGACVAACPVGAITLD-------------------EVGEKKGTKTV-VIDPERCVGCGACVAVCPTG 50
PRK06853 PRK06853
indolepyruvate oxidoreductase subunit beta; Reviewed
455-614 3.74e-09

indolepyruvate oxidoreductase subunit beta; Reviewed


Pssm-ID: 180732 [Multi-domain]  Cd Length: 197  Bit Score: 57.57  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  455 YDSKKA--------GGLTVSHLRVSEqPIRSAyLIS--QADFVgchqLQF--IDKYQMAERLKPGGIFLLNT----PYSA 518
Cdd:PRK06853   32 YDVKVSevhgmsqrGGSVVSHVRFGD-EVYSP-LIPegKADLL----LAFepLEALRYLPYLKKGGKVVVNTqpivPVPV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  519 DEVWSRLP--QEVQAVLNQKKARFYVINAAKIARECGLAARINTVMQMAffhLTQILPGDSalAELQGAIAKSYSSKgqd 596
Cdd:PRK06853  106 SLGLAKYPedEEILEELKKLGIKVYVIDAEKIAKEAGNIKAANVVLLGA---LAKFLPIDE--ETLEEAIKERVPPK--- 177
                         170
                  ....*....|....*...
gi 446550804  597 LVERNWQALALARESVEE 614
Cdd:PRK06853  178 FVEVNLKAFEAGREAAEK 195
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
677-758 1.08e-08

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 52.75  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  677 IAEEIPIWKEELCTQCNHCVAACPHSAIRakvvppeamenapaslhsldvksrdMRGQKYVlqVAPEDCTGCNLCVEVCP 756
Cdd:COG2221     5 IGTWPPKIDEEKCIGCGLCVAVCPTGAIS-------------------------LDDGKLV--IDEEKCIGCGACIRVCP 57

                  ..
gi 446550804  757 AK 758
Cdd:COG2221    58 TG 59
PRK08534 PRK08534
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed
419-615 1.48e-08

pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed


Pssm-ID: 181460 [Multi-domain]  Cd Length: 181  Bit Score: 55.82  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  419 EALFYGLGSDGSVSATKNnIKIIGNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGCHQLQFIDKY 498
Cdd:PRK08534    3 EIRFHGRGGQGAVTAAEI-LAKAAFEDGKFSQAFPFFGVERRGAPVMAFTRIDDKPIRLRSQIYEPDYVIVQDPTLLDSV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  499 QMAERLKPGGIFLLNTPYSADEVWSrlpqevqavlnQKKARFYVINAAKIARECGLAARINTVMQMAFFHLTQILPGDSa 578
Cdd:PRK08534   82 DVTSGLKKDGIIIINTTKDPEDLKY-----------DTKAKVYTIDATKIALDVLGVPIVNTTMLGAFAGATGEVSLES- 149
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446550804  579 laeLQGAIAKSYSSKgqdLVERNWQALALARESVEEV 615
Cdd:PRK08534  150 ---LKKAILERFPGK---LGEKNAEAVEKAYNLMKEE 180
PRK14029 PRK14029
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
418-614 1.58e-08

pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional


Pssm-ID: 172523 [Multi-domain]  Cd Length: 185  Bit Score: 55.80  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  418 LEALFYGLGSDGSVSATkNNIKIIGNSTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGCHQLQFIDK 497
Cdd:PRK14029    2 IEIRFHGRGGQGAVTAA-NILAEAAFLEGKYVQAFPFFGVERRGAPVTAFTRIDEKPIRIKTQIYEPDVVVVLDPSLLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  498 YQMAERLKPGGIFLLNTPYSADEVWSRlpqevqavLNQKKARFYVINAAKIARECGLAARINTVMQMAFFHLTQILpgds 577
Cdd:PRK14029   81 VDVTAGLKDGGIVIVNTEKSKEEVLEK--------LKKKPKKLALVDATTIALEILGLPITNTAILGAVAKATGLV---- 148
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 446550804  578 ALAELQGAIAKSYSSkgqDLVERNWQAlalARESVEE 614
Cdd:PRK14029  149 KIESVEEAIKDTFSG---ELGEKNAKA---AREAFEK 179
Fer4_9 pfam13187
4Fe-4S dicluster domain;
689-756 1.74e-08

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 51.79  E-value: 1.74e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446550804   689 CTQCNHCVAACPHSAIRAKVVppeamenapaslhsldvksrdmrGQKYVLQVAPEDCTGCNLCVEVCP 756
Cdd:pfam13187    2 CTGCGACVAACPAGAIVPDLV-----------------------GQTIRGDIAGLACIGCGACVDACP 46
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
682-756 2.05e-08

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 53.94  E-value: 2.05e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446550804  682 PIWKEELCTQCNHCVAACPHSAIraKVVPPEAMENAPaslhsldvksrdmrgqkyvlQVAPEDCTGCNLCVEVCP 756
Cdd:cd10549     1 LKYDPEKCIGCGICVKACPTDAI--ELGPNGAIARGP--------------------EIDEDKCVFCGACVEVCP 53
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
686-756 2.20e-08

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 51.48  E-value: 2.20e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804   686 EELCTQCNHCVAACPHSAIRAkVVPPEAMENAPASlhsldvksrdmrgqkyvlqVAPEDCTGCNLCVEVCP 756
Cdd:pfam13237    6 PDKCIGCGRCTAACPAGLTRV-GAIVERLEGEAVR-------------------IGVWKCIGCGACVEACP 56
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
664-780 6.44e-08

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 52.44  E-value: 6.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  664 TWPMGTTRWEKrniaeeiPIWKEELCTQCNHCVAACPHSAIRAkvvppeamenapaslhsldvKSRDMRGQKYVLqvape 743
Cdd:PRK09625   43 TTSVAHWRVEK-------PVHNNEICINCFNCWVYCPDAAILS--------------------RDKKLKGVDYSH----- 90
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446550804  744 dCTGCNLCVEVCPAkdrqNPeiKAINMMSrlEHVEEE 780
Cdd:PRK09625   91 -CKGCGVCVEVCPT----NP--KSLLMFE--EQIENE 118
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
689-757 2.63e-07

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 51.09  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  689 CTQCNHCVAACPHSAIRAKVVPPEAMENAPA----SLHSLDVKS------------RDMRGQKYVLQVAPEDCTGCNLCV 752
Cdd:cd10564    47 CTFCGACAEACPEGALDPAREAPWPLRAEIGdsclALQGVECRScqdacptqairfRPRLGGIALPELDADACTGCGACV 126

                  ....*
gi 446550804  753 EVCPA 757
Cdd:cd10564   127 SVCPV 131
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
686-758 4.07e-07

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 48.50  E-value: 4.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446550804  686 EELCTQCNHCVAACPHSAIrakvvppeamenapaslhsldvksrDMRGQKYVlqVAPEDCTGCNLCVEVCPAK 758
Cdd:COG4231    21 EDKCTGCGACVKVCPADAI-------------------------EEGDGKAV--IDPDLCIGCGSCVQVCPVD 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
686-797 9.04e-07

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 49.32  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  686 EELCTQCNHCVAACPHSAIRAKVVPPEAMEnapaslhsldvksrdmRGQKYVLQvaPEDCTGCNLCVEVCPAkdrqnpei 765
Cdd:cd10549    39 EDKCVFCGACVEVCPTGAIELTPEGKEYVP----------------KEKEAEID--EEKCIGCGLCVKVCPV-------- 92
                          90       100       110
                  ....*....|....*....|....*....|..
gi 446550804  766 KAInmmsrleHVEEEKinydfflnLPEIDRSK 797
Cdd:cd10549    93 DAI-------TLEDEL--------EIVIDKEK 109
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
951-1067 1.18e-06

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 49.51  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   951 ALVEKSIWLIGGDGWAYDIGfGGLDHVLSLTENVNILVLDTQCYSNTGGQAskaTPLGAVTKFGEHGKRKARKDLGVSMM 1030
Cdd:pfam02775   43 ARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQQ---TPFGGGRYSGPSGKILPPVDFAKLAE 118
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 446550804  1031 MYGhVYVAQISLGAQLnqtVKAIQEAEAYPGPSLIIA 1067
Cdd:pfam02775  119 AYG-AKGARVESPEEL---EEALKEALEHDGPALIDV 151
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
961-1077 1.42e-06

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 51.30  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  961 GGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSMMMYGHVYVAQi 1040
Cdd:PRK11866   84 GGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVAR- 162
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446550804 1041 SLGAQLNQTVKAIQEAEAYPGPSLIIAYSPC----EEHGYD 1077
Cdd:PRK11866  163 GFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCvtfnKLNTYD 203
PRK13795 PRK13795
hypothetical protein; Provisional
688-764 3.39e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.15  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  688 LCTQCNHCVAACPHSAIRakvvppeamenapaslhsldvksrdMRGQKYVLQVAPEDCTGCNLCVEVCPA---KDRQNPE 764
Cdd:PRK13795  582 ECVGCGVCVGACPTGAIR-------------------------IEEGKRKISVDEEKCIHCGKCTEVCPVvkyKDKRNGS 636
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
683-756 5.24e-06

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 47.00  E-value: 5.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446550804  683 IWKEELCTQCN--HCVAACPHSAIrakvvppeamenapaslhsldvkSRDMRGqkyVLQVAPEDCTGCNLCVEVCP 756
Cdd:cd04410    44 AFLPVSCMHCEdpPCVKACPTGAI-----------------------YKDEDG---IVLIDEDKCIGCGSCVEACP 93
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
689-758 7.28e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 44.61  E-value: 7.28e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446550804   689 CTQCNHCVAACPHSAIRA--KVVPPEAMENAPASLHSLDVKSRDmrgqkyvlqvAPEDCTGCNLCVEVCPAK 758
Cdd:pfam13183    2 CIRCGACLAACPVYLVTGgrFPGDPRGGAAALLGRLEALEGLAE----------GLWLCTLCGACTEVCPVG 63
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
686-756 1.05e-05

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 47.10  E-value: 1.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804   686 EELCTQCNHCVAACPHSAIrakVVPPEAMenapaslHSldvksrdmrgqkyvlqVAPEDCTGCNLCVEVCP 756
Cdd:TIGR01944  112 EDNCIGCTKCIQACPVDAI---VGAAKAM-------HT----------------VIADECTGCDLCVEPCP 156
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
673-768 1.27e-05

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.47  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  673 EKRNIAEE--IPIWKEELCTQCNHCVAACPHSAIRAKvvppeamenapaslhsldvksrdmrgQKYVLQVAPEDCTGCNL 750
Cdd:COG1148   480 SKGELGVEpsVAEVDPEKCTGCGRCVEVCPYGAISID--------------------------EKGVAEVNPALCKGCGT 533
                          90       100
                  ....*....|....*....|....*..
gi 446550804  751 CVEVCPAK--------DRQ-NPEIKAI 768
Cdd:COG1148   534 CAAACPSGaislkgftDDQiLAQIDAL 560
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
651-768 1.54e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 46.09  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  651 GDALPVSALPP----DGTWPMGTTRWEKRN-IAeeipiWKEElcTQCNHCVAACPHSAIrakvvppeAMenapaslhsld 725
Cdd:cd16373    63 VEVCPTGALRPldleEQKVKMGVAVIDKDRcLA-----WQGG--TDCGVCVEACPTEAI--------AI----------- 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446550804  726 vksrDMRGQKYVLQVAPEDCTGCNLCVEVCPAKDrqnpeIKAI 768
Cdd:cd16373   117 ----VLEDDVLRPVVDEDKCVGCGLCEYVCPVEP-----PKAI 150
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
686-756 1.66e-05

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 47.68  E-value: 1.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804  686 EELCTQCNHCVAACPHSAIRakvvppeaMenAPASLHsldvksrdmrgqkyvlQVAPEDCTGCNLCVEVCP 756
Cdd:COG2878   136 EYGCIGCGDCIKACPFDAIV--------G--AAKGMH----------------TVDEDKCTGCGLCVEACP 180
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
688-773 3.28e-05

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 45.03  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  688 LCTQCNH--CVAACPHSAIRakvvppeamenapaslhsldvksrdmRGQKYVlQVAPEDCTGCNLCVEVCPakdrqnpeI 765
Cdd:COG1142    51 QCRHCEDapCAEVCPVGAIT--------------------------RDDGAV-VVDEEKCIGCGLCVLACP--------F 95

                  ....*...
gi 446550804  766 KAINMMSR 773
Cdd:COG1142    96 GAITMVGE 103
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
679-756 3.71e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 44.49  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  679 EEIPIWKEELCTQCNH--CVAACPHSAIrakvvppeamenapaslhsldvkSRDmrGQKYVLQVAPEDCTGCNLCVEVCP 756
Cdd:cd10550    39 EPEGLDVPVVCRQCEDapCVEACPVGAI-----------------------SRD--EETGAVVVDEDKCIGCGMCVEACP 93
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
686-759 6.17e-05

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 46.86  E-value: 6.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446550804  686 EELCTQCNHCVAAC---PHSAIrakvvppeamenapaslHSLDVKSRdmrgqkyVLQVAPEDCTGCNLCVEVCPAKD 759
Cdd:PRK08318  341 QDKCIGCGRCYIACedtSHQAI-----------------EWDEDGTR-------TPEVIEEECVGCNLCAHVCPVEG 393
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
686-756 8.13e-05

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 44.94  E-value: 8.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804  686 EELCTQCNHCVAACPHSAIrakVVPPEAMenapaslHSldvksrdmrgqkyvlqVAPEDCTGCNLCVEVCP 756
Cdd:PRK05113  113 EDNCIGCTKCIQACPVDAI---VGATKAM-------HT----------------VISDLCTGCDLCVAPCP 157
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
687-756 1.03e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 43.42  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  687 ELCTQCNHCVAAC-----PHSAIRAKVVPPEAM--------ENAP-------ASLHsldvksRDMRGQKYVlqvAPEDCT 746
Cdd:cd16374     6 ERCIGCRACEIACarehsGKPRISVEVVEDLASvpvrcrhcEDAPcmevcptGAIY------RDEDGAVLV---DPDKCI 76
                          90
                  ....*....|
gi 446550804  747 GCNLCVEVCP 756
Cdd:cd16374    77 GCGMCAMACP 86
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
690-756 1.75e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 42.93  E-value: 1.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446550804  690 TQCNHC-----VAACPHSAIRakvvppeamenapaslhsldvKSRDmrGqkyVLQVAPEDCTGCNLCVEVCP 756
Cdd:cd16371    52 MSCNHCenpacVKVCPTGAIT---------------------KRED--G---IVVVDQDKCIGCGYCVWACP 97
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
678-756 1.77e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 44.74  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  678 AEEIPIWKEELCTQCNHCVAACPHSAIRAKVVPPEAMENApaslHSLDVKSRDMRGQK--YVLQVAPEDCTGCNLCVEVC 755
Cdd:PRK12576  143 EDQKELWKFAQCIWCGLCVSACPVVAIDPEFLGPAAHAKG----YRFLADPRDTITEErmKILIDSSWRCTYCYSCSNVC 218

                  .
gi 446550804  756 P 756
Cdd:PRK12576  219 P 219
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
689-758 1.94e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.54  E-value: 1.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  689 CTQCNHCVAACPHSAIRakvvppeaMENAPASlhsldvksrdmrgqkyvlqVAPEDCTGCNLCVEVCPAK 758
Cdd:PRK07118  215 CIGCGKCVKACPAGAIT--------MENNLAV-------------------IDQEKCTSCGKCVEKCPTK 257
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
666-703 2.27e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 40.20  E-value: 2.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 446550804   666 PMGTTRWEKRNIAEEIPIWK--EELCTQCNHCVAACPHSA 703
Cdd:pfam12838   12 PVGAITLDEVGEKKGTKTVVidPERCVGCGACVAVCPTGA 51
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
689-850 2.35e-04

Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.


Pssm-ID: 238897 [Multi-domain]  Cd Length: 731  Bit Score: 45.48  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  689 CTQCNHCVAACPHSaIRAkvvpPEAMENApaslhsldvKSRDMRGqkyvLQVAPEDCTGCNLCVEVCPAkdrqnpEIKAI 768
Cdd:cd01916   367 CTDCGWCTRACPNS-LRI----KEAMEAA---------KEGDFSG----LADLFDQCVGCGRCEQECPK------EIPII 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  769 NMMsrlehveeEKINYDFFLNLP---EIDRSKLERIDIRTSQLITPLFEYSG--ACSGCGETPY----IKLLTQLYGDRM 839
Cdd:cd01916   423 NMI--------EKAARERIKEEKgkmRAGRGPIKDTEIRKVGAPIVLGDIPGviALVGCSNYPNgtkdVYKIAEEFLERN 494
                         170
                  ....*....|.
gi 446550804  840 LIANATGCSSI 850
Cdd:cd01916   495 YIVVTTGCMAM 505
PRK06991 PRK06991
electron transport complex subunit RsxB;
686-756 2.36e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 44.40  E-value: 2.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446550804  686 EELCTQCNHCVAACPHSAIRAkvvppeamenAPASLHSldvksrdmrgqkyvlqVAPEDCTGCNLCVEVCP 756
Cdd:PRK06991   84 EQLCIGCTLCMQACPVDAIVG----------APKQMHT----------------VLADLCTGCDLCVPPCP 128
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
681-704 3.67e-04

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 38.75  E-value: 3.67e-04
                           10        20
                   ....*....|....*....|....
gi 446550804   681 IPIWKEELCTQCNHCVAACPHSAI 704
Cdd:pfam12837    1 VVEVDPDKCIGCGRCVVVCPYGAI 24
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
689-756 4.73e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.17  E-value: 4.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446550804  689 CTQCNHCVAACPHSAIrakvvppeamenapaslhsldvkSRDMRGqkyVLQVAPEDCTGCNLCVEVCP 756
Cdd:cd16372    49 CNQCGECIDVCPTGAI-----------------------TRDANG---VVMINKKLCVGCLMCVGFCP 90
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
659-773 4.85e-04

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 43.20  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  659 LPPDGTWPmgttrwekrniAEEIPIWKEEL--------CTQCNHCVAACPHSAIRAKVVPPEAMENApaslHSLDVKSRD 730
Cdd:COG0479   117 LSPDGPAP-----------DNERLQSPEDRekaddlaeCILCGACVAACPNVWANPDFLGPAALAQA----YRFALDPRD 181
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 446550804  731 MRGQKYVLQVAPE----DCTGCNLCVEVCPAkdrqnpEI---KAINMMSR 773
Cdd:COG0479   182 EETEERLEALEDEegvwRCTTCGNCTEVCPK------GIpptKAIAKLKR 225
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
689-776 5.71e-04

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 42.80  E-value: 5.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804   689 CTQCNHCVAACPHSAIRAKVVPPEAMenapASLHSLDVKSRDM----RGQKYVLQVAPEDCTGCNLCVEVCPakdrqnpe 764
Cdd:TIGR00384  140 CILCGCCYSSCPAFWWNPEFLGPAAL----TAAYRFLIDSRDHatkdRLEGLNDKNGVWRCTTCMNCSEVCP-------- 207
                           90
                   ....*....|..
gi 446550804   765 iKAINMMSRLEH 776
Cdd:TIGR00384  208 -KGVNPARAIEK 218
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
682-705 6.46e-04

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 38.00  E-value: 6.46e-04
                           10        20
                   ....*....|....*....|....
gi 446550804   682 PIWKEELCTQCNHCVAACPHSAIR 705
Cdd:pfam00037    1 VVIDEEKCIGCGACVEVCPVGAIT 24
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
677-707 9.88e-04

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.88  E-value: 9.88e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446550804  677 IAEEIPIWKEELCTQCNHCVAACPHSAIRAK 707
Cdd:COG2221    34 LDDGKLVIDEEKCIGCGACIRVCPTGAIKGE 64
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
742-756 1.15e-03

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 37.23  E-value: 1.15e-03
                           10
                   ....*....|....*
gi 446550804   742 PEDCTGCNLCVEVCP 756
Cdd:pfam00037    5 EEKCIGCGACVEVCP 19
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
726-758 1.21e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 38.87  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446550804  726 VKSRDMRGQKYVLQVAPEDCTGCNLCVEVCPAK 758
Cdd:COG4231     5 VKILDNRTTAMRYVIDEDKCTGCGACVKVCPAD 37
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
742-786 1.64e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 39.69  E-value: 1.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446550804  742 PEDCTGCNLCVEVCPAkdrqnpeiKAINMMSRLEHVEEEKINYDF 786
Cdd:cd10549     5 PEKCIGCGICVKACPT--------DAIELGPNGAIARGPEIDEDK 41
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
983-1071 1.97e-03

Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.


Pssm-ID: 238966 [Multi-domain]  Cd Length: 178  Bit Score: 40.34  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  983 NVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGKRKARKDLGVSmmmyghvyVAQISLGAQLNQTVKAIQEAEAYPGP 1062
Cdd:cd02008    98 NITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVIDIEALVRAIGVK--------RVVVVDPYDLKAIREELKEALAVPGV 169

                  ....*....
gi 446550804 1063 SLIIAYSPC 1071
Cdd:cd02008   170 SVIIAKRPC 178
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
660-756 1.99e-03

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 40.08  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  660 PPDGTWPMGTT-RWEKRNIAEEIPIW--KEELCTQCNH--CVAACPHSAIrakvvppeamenapaslhsldvkSRDMRGQ 734
Cdd:cd16366    38 PPDLTAHTWTLvRFYEVEKPGGDLSWlfRKDQCMHCTDagCLAACPTGAI-----------------------IRTETGT 94
                          90       100
                  ....*....|....*....|..
gi 446550804  735 KYVlqvAPEDCTGCNLCVEVCP 756
Cdd:cd16366    95 VVV---DPETCIGCGYCVNACP 113
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
740-758 2.14e-03

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.77  E-value: 2.14e-03
                          10
                  ....*....|....*....
gi 446550804  740 VAPEDCTGCNLCVEVCPAK 758
Cdd:COG1146     5 IDTDKCIGCGACVEVCPVD 23
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
679-756 2.23e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 38.93  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446550804  679 EEIPIWKEE-LCTQCNHCVAACPhsairAKVVppeAMENAPASLhsldvksrdmRGQKyVLQVAPEDCTGCNLCVEVCP 756
Cdd:PRK09626    7 DNTPVWVDEsRCKACDICVSVCP-----AGVL---AMRIDPHAV----------LGKM-IKVVHPESCIGCRECELHCP 66
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
686-712 2.45e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.71  E-value: 2.45e-03
                          10        20
                  ....*....|....*....|....*..
gi 446550804  686 EELCTQCNHCVAACPHSAIRAKVVPPE 712
Cdd:COG4231    50 PDLCIGCGSCVQVCPVDAIKLEKRVPE 76
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
685-714 2.71e-03

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.38  E-value: 2.71e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 446550804  685 KEELCTQCNHCVAACPHSAIRAKVVPPEAM 714
Cdd:COG1146    38 NPEECIGCGACELVCPVGAITVEDDEPEEQ 67
Fer4_9 pfam13187
4Fe-4S dicluster domain;
684-704 3.13e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 36.76  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|.
gi 446550804   684 WKEELCTQCNHCVAACPHSAI 704
Cdd:pfam13187   30 IAGLACIGCGACVDACPRGAI 50
PRK12385 PRK12385
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
689-756 4.30e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183490 [Multi-domain]  Cd Length: 244  Bit Score: 40.07  E-value: 4.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446550804  689 CTQCNHCVAACPHSAIRAKVVPPEAMenapASLHSLDVKSRDMRGQKYVLQVAPED----CTGCNLCVEVCP 756
Cdd:PRK12385  149 CINCGLCYAACPQFGLNPEFIGPAAI----TLAHRYNLDSRDHGKKERMKQLNGQNgvwsCTFVGYCSEVCP 216
PRK05844 PRK05844
pyruvate flavodoxin oxidoreductase subunit gamma; Validated
429-612 4.79e-03

pyruvate flavodoxin oxidoreductase subunit gamma; Validated


Pssm-ID: 180284 [Multi-domain]  Cd Length: 186  Bit Score: 39.37  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  429 GSVSATKNNIKIIGNsTPWYAQGYFVYDSKKAGGLTVSHLRVSEQPIRSAYLISQADFVGC--HQLQFIDKYQMAErlKP 506
Cdd:PRK05844   13 GAVTGAKGLADVIAK-TGKEVQAFAFYGSAKRGAAMTAYNRIDDEPILNHEKFMQPDYVLVidPGLVFIENIFANE--KE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  507 GGIFLLNTPYSADEVWSRLPQevqavLNQKKArfYVINAAKIARECGLAARINTVMQMAFFHLTQILPGDSALAELQGAI 586
Cdd:PRK05844   90 DTKYIITTHLSKEELIEKKPE-----LKGKKV--FLVDCIKISMETIGRPIPNTPMLGALMKVSGMLEIDAFKEAFKKVL 162
                         170       180
                  ....*....|....*....|....*.
gi 446550804  587 AKSYSskgQDLVERNWQALALARESV 612
Cdd:PRK05844  163 GKKLP---QKVIDANMLAIQRAYEEV 185
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
686-769 6.17e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 39.98  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  686 EELCTQCNHCVAACPHSAIRakvvppeaMENAPASLHsldVKSRDMrgQKYVLQVApeDCTGCnLCVEVCPAKDRQNPEI 765
Cdd:COG2878   166 EDKCTGCGLCVEACPVDCIE--------MVPVSPTVV---VSSWDK--GKAVRKVV--GCIGL-CCKKCCPAAAITVNNL 229

                  ....
gi 446550804  766 KAIN 769
Cdd:COG2878   230 AAII 233
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
686-705 8.62e-03

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 37.99  E-value: 8.62e-03
                          10        20
                  ....*....|....*....|
gi 446550804  686 EELCTQCNHCVAACPHSAIR 705
Cdd:cd10564   116 ADACTGCGACVSVCPVGAIT 135
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
666-705 8.75e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.88  E-value: 8.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 446550804  666 PMGTTRWEKRNIAEEIPIWkEELCTQCNHCVAACPHSAIR 705
Cdd:COG1143    15 PVDAITIEDGEPGKVYVID-PDKCIGCGLCVEVCPTGAIS 53
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
961-1071 9.00e-03

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 39.38  E-value: 9.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  961 GGDGWAYDIGFGGLDHVLSLTENVNILVLDTQCYSNTGGQASKATPLGAVTKFGEHGK-RKARKDLGVSMMMyGHVYVAQ 1039
Cdd:PRK11869   85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVfEEPFNPIALAIAL-DASFVAR 163
                          90       100       110
                  ....*....|....*....|....*....|..
gi 446550804 1040 ISLGaQLNQTVKAIQEAEAYPGPSLIIAYSPC 1071
Cdd:PRK11869  164 TFSG-DIEETKEILKEAIKHKGLAIVDIFQPC 194
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
690-768 9.21e-03

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 38.77  E-value: 9.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446550804  690 TQCNHCV-AACphsairAKVVPPEAMenapaslhsldVKSRDmrGqkyVLQVAPEDCTGCNLCVEVCPAKDRQ-NPEIKA 767
Cdd:COG0437    58 VLCNHCDdPPC------VKVCPTGAT-----------YKRED--G---IVLVDYDKCIGCRYCVAACPYGAPRfNPETGV 115

                  .
gi 446550804  768 I 768
Cdd:COG0437   116 V 116
 
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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