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Conserved domains on  [gi|575523317|gb|AHG98009|]
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NifJ [Cloning vector pCV_cistron14]

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

CATH:  3.40.920.10|3.40.50.920|3.40.50.970|4.10.780.10|3.30.70.20
EC:  1.2.7.1
Gene Ontology:  GO:0005506|GO:0022900|GO:0030976|GO:0051539|GO:0019164|GO:0016903
SCOP:  4000021|3001790|4000649

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 ...
 1-1165 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: 1859.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317     1 MKTMDGNAAAAWISYAFTEVAAIYPITPSTPMAENVDEWAAQGKKNLFGQPVRLMEMQSEAGAAGAVHGALQAGALTTTY 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    81 TASQGLLLMIPNMYKIAGELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   161 IPFVNFFDGFRTSHEIQKIEVLEYEQLATLLDRPALDSFRRNALHPDHPVIRGTAQNPDIYFQEREAGNRFYQALPDIVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   241 SYMTQISALTGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFAQLPKTVQRI 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   321 AVLDRTKEPGAQAEPLCLDVKNAFY-HHDDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPLPMDGFTLGIVDDVTFTSL 399
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYeMGEAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSL 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   400 pPAQQTLAVSHDGITACKFWGMGSDGTVGANKSAIKIIGDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHR 479
Cdd:TIGR02176  401 -PVDEFFDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   480 ADFISCSQQSYVERYDLLDGLKPGGTFLLNCSWSDAELEQHLPVGFKRYLARENIHFYTLNAVDIARELGLGGRFNMLMQ 559
Cdd:TIGR02176  480 ADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQ 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   560 AAFFKLAAIIDPQTAADYLKQAVEKSYGSKGAAVIEMNQRAIELGMASLHQVTIPAHWATLDEPAAQASAMMPDFIRDIL 639
Cdd:TIGR02176  560 TAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFVKNVV 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   640 QPMNRQCGDQLPVSAFVGmeDGTFPSGTAAWEKRGIALEVPVWQPEGCTQCNQCAFICPHAAIRPALLNGEEHDAAPVGL 719
Cdd:TIGR02176  640 RPINAQEGDDLPVSAFPA--DGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPAGF 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   720 LSKPAQG--AKEYHYHLAISPLDCSGCGNCVDICPARGKALKMQSLDSQR-QMAPVWDYALALTPKSNPFRKTTVKGSQF 796
Cdd:TIGR02176  718 KSLDAKGkeLEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQReAQVANWEFAINIPEKDNKLNIDTVKGSQF 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   797 ETPLLEFSGACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPSIPYTTNHRGHGPAWANSLFEDNAEFGLGMML 876
Cdd:TIGR02176  798 QRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRL 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   877 GGQAVRQQIADDMTAALALPV-SDELSDAMRQWLAKQDEGEGTRERADRLSERLAAEKEgvPLLEQLWQNRDYFVRRSQW 955
Cdd:TIGR02176  878 SMDKRRERLAELAAKALESDIaSGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKD--DLLKEIYAVSDLFVKKSVW 955

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   956 IFGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVA 1035
Cdd:TIGR02176  956 IIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVA 1035

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  1036 QVAMGADKDQTLRAIAEAEAWPGPSLVIAYAACINHGLKAGMRCSQREAKRAVEAGYWHLWRYHPQREAEGKTPFMLDSE 1115
Cdd:TIGR02176 1036 QVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSK 1115

                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|
gi 575523317  1116 EPEESFRDFLLGEVRYASLHKTTPHLADALFSRTEEDARARFAQYRRLAG 1165
Cdd:TIGR02176 1116 EPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
 
Name Accession Description Interval E-value
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 1-1165 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: 1859.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317     1 MKTMDGNAAAAWISYAFTEVAAIYPITPSTPMAENVDEWAAQGKKNLFGQPVRLMEMQSEAGAAGAVHGALQAGALTTTY 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    81 TASQGLLLMIPNMYKIAGELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   161 IPFVNFFDGFRTSHEIQKIEVLEYEQLATLLDRPALDSFRRNALHPDHPVIRGTAQNPDIYFQEREAGNRFYQALPDIVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   241 SYMTQISALTGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFAQLPKTVQRI 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   321 AVLDRTKEPGAQAEPLCLDVKNAFY-HHDDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPLPMDGFTLGIVDDVTFTSL 399
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYeMGEAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSL 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   400 pPAQQTLAVSHDGITACKFWGMGSDGTVGANKSAIKIIGDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHR 479
Cdd:TIGR02176  401 -PVDEFFDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   480 ADFISCSQQSYVERYDLLDGLKPGGTFLLNCSWSDAELEQHLPVGFKRYLARENIHFYTLNAVDIARELGLGGRFNMLMQ 559
Cdd:TIGR02176  480 ADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQ 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   560 AAFFKLAAIIDPQTAADYLKQAVEKSYGSKGAAVIEMNQRAIELGMASLHQVTIPAHWATLDEPAAQASAMMPDFIRDIL 639
Cdd:TIGR02176  560 TAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFVKNVV 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   640 QPMNRQCGDQLPVSAFVGmeDGTFPSGTAAWEKRGIALEVPVWQPEGCTQCNQCAFICPHAAIRPALLNGEEHDAAPVGL 719
Cdd:TIGR02176  640 RPINAQEGDDLPVSAFPA--DGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPAGF 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   720 LSKPAQG--AKEYHYHLAISPLDCSGCGNCVDICPARGKALKMQSLDSQR-QMAPVWDYALALTPKSNPFRKTTVKGSQF 796
Cdd:TIGR02176  718 KSLDAKGkeLEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQReAQVANWEFAINIPEKDNKLNIDTVKGSQF 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   797 ETPLLEFSGACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPSIPYTTNHRGHGPAWANSLFEDNAEFGLGMML 876
Cdd:TIGR02176  798 QRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRL 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   877 GGQAVRQQIADDMTAALALPV-SDELSDAMRQWLAKQDEGEGTRERADRLSERLAAEKEgvPLLEQLWQNRDYFVRRSQW 955
Cdd:TIGR02176  878 SMDKRRERLAELAAKALESDIaSGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKD--DLLKEIYAVSDLFVKKSVW 955

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   956 IFGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVA 1035
Cdd:TIGR02176  956 IIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVA 1035

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  1036 QVAMGADKDQTLRAIAEAEAWPGPSLVIAYAACINHGLKAGMRCSQREAKRAVEAGYWHLWRYHPQREAEGKTPFMLDSE 1115
Cdd:TIGR02176 1036 QVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSK 1115

                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|
gi 575523317  1116 EPEESFRDFLLGEVRYASLHKTTPHLADALFSRTEEDARARFAQYRRLAG 1165
Cdd:TIGR02176 1116 EPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 799-1165 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: 667.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  799 PLLEFSGACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPSIPYTTNHRGHGPAWANSLFEDNAEFGLGMMLGG 878
Cdd:cd03377     1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  879 QAVRQQIADDMTAALALPVSDELSDAMRQWLAKQDEGEGTRERADRLSERLAAEKegVPLLEQLWQNRDYFVRRSQWIFG 958
Cdd:cd03377    81 DQRRERARELVQKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEK--DELAKELLSLADYLVKKSVWIIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  959 GDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQVA 1038
Cdd:cd03377   159 GDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQIA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317 1039 MGADKDQTLRAIAEAEAWPGPSLVIAYAACINHGLKAGMRCSQREAKRAVEAGYWHLWRYHPQREAEGKTPFMLDSEEPE 1118
Cdd:cd03377   239 LGANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIKGGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEPD 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 575523317 1119 ESFRDFLLGEVRYASLHKTTPHLADALFSRTEEDARARFAQYRRLAG 1165
Cdd:cd03377   319 GPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
 1-388 4.88e-119

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: 372.49  E-value: 4.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    1 MKTMDGNAAAAW-ISYAFTEVAAIYPITPSTPMAENVDEWAAqgKKNlfgqpVRLMEMQSEAGAAGAVHGALQAGALTTT 79
Cdd:COG0674     3 RVLMDGNEAVALgAIAAGCRVIAAYPITPSTEIAEYLAEWLA--ELG-----GVVVQAESEIAAIGAVIGASAAGARAMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   80 YTASQGLLLMIPNMYKIAGELLPGVFHVSARALATNSLNIFGDHQDVMAV-----RQTGCAMLAENNVQQVMDLSAVAHL 154
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIAFN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  155 AAIKGRIPFVNFFDGFRTSHEIqKIEVLEYEQLATlLDRPalDSFRRNALHpDHPVIR-GTAQnPDIYF---QEREAGNR 230
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEE-PVELPDDEEVKI-LPRP--EEYRPYALD-EDPRAIpGTAQ-PDVYFtglEHDETEDP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  231 fyQALPDIVESYMTQISALTgREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFF 310
Cdd:COG0674   230 --ENAEKMVEKRMRKFEKIR-DELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEALR 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575523317  311 AQLpKTVQRIAVLDRTKEpGaqaePLCLDVKNAFyhhdDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPLPmdGFTL 388
Cdd:COG0674   307 EAL-KGVKKVAVVERNKS-G----QLALDVRAAL----GADRVVGGIYGLGGRPFTPEEILAVIEELLKGAP--KFTL 372
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
 19-243 1.21e-87

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: 282.61  E-value: 1.21e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    19 EVAAIYPITPSTPMAENVDEWAAQGKKNlfgqPVRLMEMQSEAGAAGAVHGALQAGALTTTYTASQGLLLMIPNMYKIAG 98
Cdd:pfam01855    8 DVIAAYPITPSSEIAEEAAEWAANGEKG----DVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGKAAG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    99 ELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGRIPFVNFFDGFRTSHEIQK 178
Cdd:pfam01855   84 ERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFRTSHEREK 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317   179 IEVLEYEQLATLLDRPALDSFR-RNALHPDHPVIRGTAQNPDIYFQEREAGNRFYQALPDIVESYM 243
Cdd:pfam01855  164 VELPPDEDEKDLIDEFLPPYKRkRYGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVM 229
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
5-379 1.10e-45

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 170.33  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    5 DGNAAAAW-ISYAFTEVAAIYPITPSTPMAENVDEWAAQGKKNlfGQPVRLmemQSEAGAAGAVHGALQAGALTTTYTAS 83
Cdd:PRK09622   14 DGNTAASNaLRQAQIDVVAAYPITPSTPIVQNYGSFKANGYVD--GEFVMV---ESEHAAMSACVGAAAAGGRVATATSS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   84 QGLLLMIPNMYKIAGELLPGVFHVSARALATnSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAA--IKGRI 161
Cdd:PRK09622   89 QGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFTLMAFKIAedQKVRL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  162 PFVNFFDGFRTSHEIQKIEVL----------EYEQLATLLDRpaldsfrrnalhpDHPVIRGTAQNPDIYFQEREagnRF 231
Cdd:PRK09622  168 PVIVNQDGFLCSHTAQNVRPLsdevayqfvgEYQTKNSMLDF-------------DKPVTYGAQTEEDWHFEHKA---QL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  232 YQALPD---IVESYMTQISALTGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAH 308
Cdd:PRK09622  232 HHALMSsssVIEEVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYER 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575523317  309 fFAQLPKTVQRIAVLDRTKePGAQAEPLCLDVKNAFYHHDDA--PLIVGGRYALGGKDVLPNDIAAVFDNLNK 379
Cdd:PRK09622  312 -LGQALKNLKALAILDRSS-PAGAMGALFNEVTSAVYQTQGTkhPVVSNYIYGLGGRDMTIAHLCEIFEELNE 382
EKR smart00890
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
 618-677 1.02e-21

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: 89.21  E-value: 1.02e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    618 ATLDEPAAQASAMmPDFIRDILQPMNRQCGDQLPVSAFVgmEDGTFPSGTAAWEKRGIAL 677
Cdd:smart00890    1 SELDEPPPVPEEA-PEFVKNVVAPMNAGEGDDLPVSAFP--EDGTFPTGTAAYEKRGIAV 57
 
Name Accession Description Interval E-value
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 1-1165 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: 1859.44  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317     1 MKTMDGNAAAAWISYAFTEVAAIYPITPSTPMAENVDEWAAQGKKNLFGQPVRLMEMQSEAGAAGAVHGALQAGALTTTY 80
Cdd:TIGR02176    1 MKTMDGNTAAAHVAYAFSEVAAIYPITPSSTMGEYVDDWAAQGRKNIFGQTVKVVEMQSEAGAAGAVHGALQTGALTTTF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    81 TASQGLLLMIPNMYKIAGELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGR 160
Cdd:TIGR02176   81 TASQGLLLMIPNMYKIAGELLPCVFHVSARAIAAHALSIFGDHQDVMAARQTGFAMLASSSVQEVMDLALVAHLATIEAR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   161 IPFVNFFDGFRTSHEIQKIEVLEYEQLATLLDRPALDSFRRNALHPDHPVIRGTAQNPDIYFQEREAGNRFYQALPDIVE 240
Cdd:TIGR02176  161 VPFMHFFDGFRTSHEIQKIEVLDYEDMASLVNQELVAAFRKRSMNPEHPHVRGTAQNPDIYFQGREAVNPYYLAVPGIVQ 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   241 SYMTQISALTGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFAQLPKTVQRI 320
Cdd:TIGR02176  241 KYMDKIAKLTGRSYHLFDYYGAPDAERVIIAMGSVAETIEETVDYLNAKGEKVGLLKVRLYRPFSAETFFAALPKSVKRI 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   321 AVLDRTKEPGAQAEPLCLDVKNAFY-HHDDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPLPMDGFTLGIVDDVTFTSL 399
Cdd:TIGR02176  321 AVLDRTKEPGAAGEPLYLDVVSAFYeMGEAMPVILGGRYGLGSKEFTPAMVKAVFDNLSGEAPKNHFTVGIEDDVTGTSL 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   400 pPAQQTLAVSHDGITACKFWGMGSDGTVGANKSAIKIIGDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHR 479
Cdd:TIGR02176  401 -PVDEFFDTTPKGTIQAKFYGLGSDGTVGANKNAIKIIGDNTDNYAQGYFSYDSKKSGGITISHLRFGEKPIRSTYLVTE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   480 ADFISCSQQSYVERYDLLDGLKPGGTFLLNCSWSDAELEQHLPVGFKRYLARENIHFYTLNAVDIARELGLGGRFNMLMQ 559
Cdd:TIGR02176  480 ADFVACHNPAYLEMYDVLKGLKKGGTFLLNSPWAPEDLDKHLPNGVKRYIADKEIKFYTIDAVKIAQEVGLGGRINTIMQ 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   560 AAFFKLAAIIDPQTAADYLKQAVEKSYGSKGAAVIEMNQRAIELGMASLHQVTIPAHWATLDEPAAQASAMMPDFIRDIL 639
Cdd:TIGR02176  560 TAFFKLAGVLPFEKAVDLLKKSIEKSYGKKGEKIVQKNIKAVDQAVESLHEVKVPAEWKDAPAEPKAIEGDAPEFVKNVV 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   640 QPMNRQCGDQLPVSAFVGmeDGTFPSGTAAWEKRGIALEVPVWQPEGCTQCNQCAFICPHAAIRPALLNGEEHDAAPVGL 719
Cdd:TIGR02176  640 RPINAQEGDDLPVSAFPA--DGTFPLGTTAFEKRGVAINVPVWVPDNCIQCNQCAFVCPHAAIRPKLADEEELENAPAGF 717

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   720 LSKPAQG--AKEYHYHLAISPLDCSGCGNCVDICPARGKALKMQSLDSQR-QMAPVWDYALALTPKSNPFRKTTVKGSQF 796
Cdd:TIGR02176  718 KSLDAKGkeLEGMKFRIQISPLDCTGCGNCVDICPAKEKALVMQPLAEQReAQVANWEFAINIPEKDNKLNIDTVKGSQF 797

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   797 ETPLLEFSGACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPSIPYTTNHRGHGPAWANSLFEDNAEFGLGMML 876
Cdd:TIGR02176  798 QRPLFEFSGACSGCGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRL 877

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   877 GGQAVRQQIADDMTAALALPV-SDELSDAMRQWLAKQDEGEGTRERADRLSERLAAEKEgvPLLEQLWQNRDYFVRRSQW 955
Cdd:TIGR02176  878 SMDKRRERLAELAAKALESDIaSGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKD--DLLKEIYAVSDLFVKKSVW 955

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   956 IFGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVA 1035
Cdd:TIGR02176  956 IIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYGYVYVA 1035

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  1036 QVAMGADKDQTLRAIAEAEAWPGPSLVIAYAACINHGLKAGMRCSQREAKRAVEAGYWHLWRYHPQREAEGKTPFMLDSE 1115
Cdd:TIGR02176 1036 QVSMGANMQQTLKAFREAEAYDGPSIVIAYSPCINHGIKKGMGKSQAEQKTAVESGYWPLYRYNPRLAEQGKNPFQLDSK 1115

                         1130      1140      1150      1160      1170
                   ....*....|....*....|....*....|....*....|....*....|
gi 575523317  1116 EPEESFRDFLLGEVRYASLHKTTPHLADALFSRTEEDARARFAQYRRLAG 1165
Cdd:TIGR02176 1116 EPDSSVAEFLNGEVRFASLKKSFPDDAERLFNKAAHEAKRRFKEYEHLAA 1165
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 799-1165 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: 667.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  799 PLLEFSGACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPSIPYTTNHRGHGPAWANSLFEDNAEFGLGMMLGG 878
Cdd:cd03377     1 PLFEFSGACAGCGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  879 QAVRQQIADDMTAALALPVSDELSDAMRQWLAKQDEGEGTRERADRLSERLAAEKegVPLLEQLWQNRDYFVRRSQWIFG 958
Cdd:cd03377    81 DQRRERARELVQKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEK--DELAKELLSLADYLVKKSVWIIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  959 GDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQVA 1038
Cdd:cd03377   159 GDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVAQIA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317 1039 MGADKDQTLRAIAEAEAWPGPSLVIAYAACINHGLKAGMRCSQREAKRAVEAGYWHLWRYHPQREAEGKTPFMLDSEEPE 1118
Cdd:cd03377   239 LGANDNQTLKAFREAEAYDGPSLIIAYSPCIAHGIKGGMTKSQEQQKLAVESGYWPLYRYNPRLVEEGKNPLQLDSKEPD 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 575523317 1119 ESFRDFLLGEVRYASLHKTTPHLADALFSRTEEDARARFAQYRRLAG 1165
Cdd:cd03377   319 GPVEEFLNNENRFAALKKANPERAEQLFEQLQADAKERYKRYKRLAA 365
PorA COG0674
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, alpha ...
 1-388 4.88e-119

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: 372.49  E-value: 4.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    1 MKTMDGNAAAAW-ISYAFTEVAAIYPITPSTPMAENVDEWAAqgKKNlfgqpVRLMEMQSEAGAAGAVHGALQAGALTTT 79
Cdd:COG0674     3 RVLMDGNEAVALgAIAAGCRVIAAYPITPSTEIAEYLAEWLA--ELG-----GVVVQAESEIAAIGAVIGASAAGARAMT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   80 YTASQGLLLMIPNMYKIAGELLPGVFHVSARALATNSLNIFGDHQDVMAV-----RQTGCAMLAENNVQQVMDLSAVAHL 154
Cdd:COG0674    76 ATSGPGLSLMQEGLGLAAGAELPLVIVVVQRAGPSTGLPIKGDQSDLMQAlygghGDTGWIVLAPSSVQEAFDLTIIAFN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  155 AAIKGRIPFVNFFDGFRTSHEIqKIEVLEYEQLATlLDRPalDSFRRNALHpDHPVIR-GTAQnPDIYF---QEREAGNR 230
Cdd:COG0674   156 LAEKYRVPVIVLFDGFLGSHEE-PVELPDDEEVKI-LPRP--EEYRPYALD-EDPRAIpGTAQ-PDVYFtglEHDETEDP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  231 fyQALPDIVESYMTQISALTgREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFF 310
Cdd:COG0674   230 --ENAEKMVEKRMRKFEKIR-DELPRVEYYGAEDAEVVIVAMGSTAGTAKEAVDRLREEGIKVGLLRVRLLRPFPAEALR 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575523317  311 AQLpKTVQRIAVLDRTKEpGaqaePLCLDVKNAFyhhdDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPLPmdGFTL 388
Cdd:COG0674   307 EAL-KGVKKVAVVERNKS-G----QLALDVRAAL----GADRVVGGIYGLGGRPFTPEEILAVIEELLKGAP--KFTL 372
POR_N pfam01855
Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg; This family includes the N ...
 19-243 1.21e-87

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: 282.61  E-value: 1.21e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    19 EVAAIYPITPSTPMAENVDEWAAQGKKNlfgqPVRLMEMQSEAGAAGAVHGALQAGALTTTYTASQGLLLMIPNMYKIAG 98
Cdd:pfam01855    8 DVIAAYPITPSSEIAEEAAEWAANGEKG----DVVVIQMESEIGAISAVIGAAAAGARAATATSGQGLLLMIENLGKAAG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    99 ELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGRIPFVNFFDGFRTSHEIQK 178
Cdd:pfam01855   84 ERLPVVIHVVARAGPSPGLSIFGDHSDVMAARDTGWIVLASENVQEAFDFALVAFNLAEKVRTPVIHLFDGFRTSHEREK 163

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317   179 IEVLEYEQLATLLDRPALDSFR-RNALHPDHPVIRGTAQNPDIYFQEREAGNRFYQALPDIVESYM 243
Cdd:pfam01855  164 VELPPDEDEKDLIDEFLPPYKRkRYGLDPEMPIARGTAQNPDTYFEHREYGNPAYDAAEVVIEEVM 229
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 800-1102 3.34e-75

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: 248.55  E-value: 3.34e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  800 LLEFSGACAGCGETPYARLITQLFG--DRMLIANATGCSSIWGASAPSIPYttnhrghGPAWANSLFEDNAEFGLGMmlg 877
Cdd:cd02018     1 LTEEHGACAGCGEVTAVRVVLAALPapEDTVIANSTGCSSVYASTAPFNSW-------AVPWVNSLFEDANAVASGL--- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  878 gqavrqqiaddmtaalalpvsdelsDAMRQWLAKQDEGEGTReradrlserlaaekegvplleqlwqnrdyfvrRSQWIF 957
Cdd:cd02018    71 -------------------------KRGLKARFPKDRELDKK--------------------------------KDVVVI 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  958 GGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQV 1037
Cdd:cd02018    94 GGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAATHGCVYVARL 173

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317 1038 AMgADKDQTLRAIAEAEAW-PGPSLVIAYAACINHGLKaGMRCSQREAKRAVEAGYWHLWRYHPQR 1102
Cdd:cd02018   174 SP-ALKKHFLKVVKEAISRtDGPTFIHAYTPCITEWGI-GSGKSLELARKAVKSRMFPLFEYDPRE 237
PorG COG1014
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, gamma ...
 411-845 3.04e-59

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: 210.32  E-value: 3.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  411 DGITACKFWGMGSDGTVGANKSAIKIIgDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPyLIHRADFISCSQQSY 490
Cdd:COG1014     2 AMDLEIRIAGVGGQGVVTAGKILAKAA-MREGYYVQGYPSYGSEQRGGPVVSHVRISDEPIRSP-LIDEADVLIALDPEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  491 VERYdlLDGLKPGGTFLLNCSWSDAELEqHLPvgfKRYLARENIHFYTLNAVDIARE-LGLGGRFNMLMQAAFFKLAAIi 569
Cdd:COG1014    80 LDRV--LDGLKPGGVLIVNSSLVPPEVW-RLP---QEALERKDIRVYVIDATKIAKElLGNARVANTVMLGALAALLGL- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  570 dpqtAADYLKQAVEKSYGSKGAAVIEMNQRAIELGMASLHQVTIPAhwatlDEPAAQASAMMPDFIRDILQPMNRQCGDQ 649
Cdd:COG1014   153 ----PLEALEEAIEETFGKKGEKVVELNLKAFEAGYEAAKEVFALA-----AAPAPLVLLAGNAAAALGAAAGGAAFAAA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  650 LPVSAFVGMEDgtFPSGTAAWEKRGIALEVPVWQPEGCTQCNQCAFICPHAAIRPA-----LLNGEEHDAAPVGLLSKPA 724
Cdd:COG1014   224 YPITPSTSLIE--AAAAAAAKVGGVVAEEEAAAAAAAAAAAAAAAGAAAAAAGGGGgaalaTEGLGLAGMTETPVVAVAA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  725 QGAKEYHYHLAISPLDCSGCGNCVDICPARGKALKMQSLDSQRQMAPVWDYALALTPKSNPFRKTTVKGSQFETPLLEFS 804
Cdd:COG1014   302 PRPGPGTGTPTEEEQGLLLLAAGGGGGEAPALALAPDTEEELLFAAAAAFALAEYAQALLLLLLLQLLVLLLTDLLLLLL 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 575523317  805 GACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPS 845
Cdd:COG1014   382 DLLRRRAGLGAEEAEARRKLLAAEGRAARAAGGGGGGGGGG 422
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 802-1131 3.87e-49

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: 175.33  E-value: 3.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  802 EFSGACAGCGETPYARLITQLF-----GDRMLIANATGCSSIWGAsapsiPYTTNhrghgpaWANSLFEDNAEFGLGMml 876
Cdd:COG1013    11 PGHRWCPGCGHGIILRLLLKALdelldGDKTVVVSGIGCSSVAPG-----YFNVP-------GFHTLHGRAAAVATGI-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  877 ggqavrqqiaddmtaalalpvsdelsdamrqwlakqdegegtrERAdrlserlaaekegvplleqlwqNRDYFVrrsqWI 956
Cdd:COG1013    77 -------------------------------------------KLA----------------------NPDLTV----IV 87

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  957 FGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQ 1036
Cdd:COG1013    88 FGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVAR 167

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317 1037 VAMGaDKDQTLRAIAEAEAWPGPSLVIAYAACINHGlkagmRCSQREAKRAVEAGYWHLWRYHPQREaegktpfMLDSEE 1116
Cdd:COG1013   168 ASVG-DPKDLKKKIKKAIEHKGFSFIEVLSPCPTGW-----GRDPSKTIEWAKEGMWPLYEYDPGEK-------LRLTYE 234

                         330
                  ....*....|....*..
gi 575523317 1117 PEESF--RDFLLGEVRY 1131
Cdd:COG1013   235 PKDKIpvGEFLKNQGRF 251
porA PRK09622
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
5-379 1.10e-45

2-oxoacid:ferredoxin oxidoreductase subunit alpha;


Pssm-ID: 181999 [Multi-domain]  Cd Length: 407  Bit Score: 170.33  E-value: 1.10e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    5 DGNAAAAW-ISYAFTEVAAIYPITPSTPMAENVDEWAAQGKKNlfGQPVRLmemQSEAGAAGAVHGALQAGALTTTYTAS 83
Cdd:PRK09622   14 DGNTAASNaLRQAQIDVVAAYPITPSTPIVQNYGSFKANGYVD--GEFVMV---ESEHAAMSACVGAAAAGGRVATATSS 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   84 QGLLLMIPNMYKIAGELLPGVFHVSARALATnSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAA--IKGRI 161
Cdd:PRK09622   89 QGLALMVEVLYQASGMRLPIVLNLVNRALAA-PLNVNGDHSDMYLSRDSGWISLCTCNPQEAYDFTLMAFKIAedQKVRL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  162 PFVNFFDGFRTSHEIQKIEVL----------EYEQLATLLDRpaldsfrrnalhpDHPVIRGTAQNPDIYFQEREagnRF 231
Cdd:PRK09622  168 PVIVNQDGFLCSHTAQNVRPLsdevayqfvgEYQTKNSMLDF-------------DKPVTYGAQTEEDWHFEHKA---QL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  232 YQALPD---IVESYMTQISALTGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAH 308
Cdd:PRK09622  232 HHALMSsssVIEEVFNDFAKLTGRKYNLVETYQLEDAEVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYER 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575523317  309 fFAQLPKTVQRIAVLDRTKePGAQAEPLCLDVKNAFYHHDDA--PLIVGGRYALGGKDVLPNDIAAVFDNLNK 379
Cdd:PRK09622  312 -LGQALKNLKALAILDRSS-PAGAMGALFNEVTSAVYQTQGTkhPVVSNYIYGLGGRDMTIAHLCEIFEELNE 382
TPP_PYR_PFOR_IOR-alpha_like cd07034
Pyrimidine (PYR) binding domain of pyruvate ferredoxin oxidoreductase (PFOR), indolepyruvate ...
 6-169 3.13e-40

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: 146.11  E-value: 3.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    6 GNAAAAWISYAFT-EVAAIYPITPSTPMAENVDEWAaqgkknLFGQPVRLMEMQSEAGAAGAVHGALQAGALTTTYTASQ 84
Cdd:cd07034     1 GNEAVARGALAAGvDVVAAYPITPSTEIAETLAKAV------LGELGGVVVQAESEHAAAEAAIGASAAGARAMTATSGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   85 GLLLMIPNMYKIAGELLPGVFHVSARALATnSLNIFGDHQDVMAVRQTG--CAMLAENNVQQVMDLSAVAHLAAIKGRIP 162
Cdd:cd07034    75 GLNLMAEALYLAAGAELPLVIVVAQRPGPS-TGLPKPDQSDLMAARYGGhpWPVLAPSSVQEAFDLALEAFELAEKYRLP 153


                  ....*..
gi 575523317  163 FVNFFDG 169
Cdd:cd07034   154 VIVLSDG 160
vorA PRK08366
2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed
 2-379 4.52e-40

2-ketoisovalerate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 169406 [Multi-domain]  Cd Length: 390  Bit Score: 153.23  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    2 KTMDGNAAAAWIS-YAFTEVAAIYPITPSTPMAENVDEWAAQGKKNLFGQPVrlmemQSEAGAAGAVHGALQAGALTTTY 80
Cdd:PRK08366    4 KVVSGNYAAAYAAlHARVQVVAAYPITPQTSIIEKIAEFIANGEADIQYVPV-----ESEHSAMAACIGASAAGARAFTA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   81 TASQGLLLMIPNMYKIAGELLPGVFHVSARALATnSLNIFGDHQDVMAVRQTG-CAMLAENNvQQVMDLSAVAHLAAIKG 159
Cdd:PRK08366   79 TSAQGLALMHEMLHWAAGARLPIVMVDVNRAMAP-PWSVWDDQTDSLAQRDTGwMQFYAENN-QEVYDGVLMAFKVAETV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  160 RIPFVNFFDGFRTSHEIQKIEVLEYEQLATLLD--RP--ALDSFrrnalhpDHPVIRGTAQNPDIYFQEREAGNRFYQAL 235
Cdd:PRK08366  157 NLPAMVVESAFILSHTYDVVEMIPQELVDEFLPprKPlySLADF-------DNPISVGALATPADYYEFRYKIAKAMEEA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  236 PDIVESYMTQISALTGREYHLFNYTG-AADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFaQLP 314
Cdd:PRK08366  230 KKVIKEVGKEFGERFGRDYSQMIETYyTDDADFVFMGMGSLMGTVKEAVDLLRKEGYKVGYAKVRWFRPFPKEELY-EIA 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575523317  315 KTVQRIAVLDRTKEPGaQAEPLCLDVKNAFYHHDDAPLIVGGRYALGGKDVLPNDIAAVFDNLNK 379
Cdd:PRK08366  309 ESVKGIAVLDRNFSFG-QEGILFTEAKGALYNTDARPIMKNYIVGLGGRDFTVNDVKAIAEDMKK 372
porA PRK08367
pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed
 2-381 6.63e-40

pyruvate ferredoxin oxidoreductase subunit alpha; Reviewed


Pssm-ID: 181403 [Multi-domain]  Cd Length: 394  Bit Score: 153.12  E-value: 6.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    2 KTMDGNAAAAWIS-YAFTEVAAIYPITPSTPMAENVDEWAAQGKKNlfgqpVRLMEMQSEAGAAGAVHGALQAGALTTTY 80
Cdd:PRK08367    5 TVMKANEAAAWAAkLAKPKVIAAFPITPSTLVPEKISEFVANGELD-----AEFIKVESEHSAISACVGASAAGVRTFTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   81 TASQGLLLMIPNMYKIAGELLPGVFHVSARALATnSLNIFGDHQDVMAVRQTG-CAMLAENNvQQVMDLSAVAHLAAIKG 159
Cdd:PRK08367   80 TASQGLALMHEVLFIAAGMRLPIVMAIGNRALSA-PINIWNDWQDTISQRDTGwMQFYAENN-QEALDLILIAFKVAEDE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  160 RI--PFVNFFDGFRTSHEIQKIEVLEYEQLATLLDR--PaldsfRRNALHPDHPVIRGTAQNPDIYFQER----EAGNRF 231
Cdd:PRK08367  158 RVllPAMVGFDAFILTHTVEPVEIPDQEVVDEFLGEyeP-----KHAYLDPARPITQGALAFPAHYMEARytvwEAMENA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  232 YQALPDIVESYMTQIsaltGREYHLFNYTGAADAERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFA 311
Cdd:PRK08367  233 KKVIDEAFAEFEKKF----GRKYQKIEEYRTEDAEIIFVTMGSLAGTLKEFVDKLREEGYKVGAAKLTVYRPFPVEEIRA 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  312 qLPKTVQRIAVLDRTKEPGAQAePLCLDVKNAFYHHDDAPLIVGGRYALGGKDVLPNDIAAVFDNLNKPL 381
Cdd:PRK08367  309 -LAKKAKVLAFLEKNISFGLGG-AVFADASAALVNESEKPKILDFIIGLGGRDVTFKQLDEALEIAEKAL 376
POR pfam01558
Pyruvate ferredoxin/flavodoxin oxidoreductase; This family includes a region of the large ...
 422-606 4.17e-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: 131.65  E-value: 4.17e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   422 GSDGTVGANKSAIKIIgDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYVERYdlLDGLK 501
Cdd:pfam01558    1 GGQGVVTAGKILAKAA-ARAGYYVQATPEYGSEIRGGPVVSHVRISDEPIVPAIPVGEADLLVALDPETLDRH--LDGLK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   502 PGGTFLLNCSWSDAEleqhlPVGFKRYLARENIHFYTLNAVDIARELGLGGRF-NMLMQAAFFKLAAIidpqtAADYLKQ 580
Cdd:pfam01558   78 PGGIIIYNSSEVPPE-----LLEKDLPAYPRLARVYGVPATEIAKEAGGNSRAaNTVMLGALAALLGL-----PLEALEE 147

                          170       180
                   ....*....|....*....|....*.
gi 575523317   581 AVEKSYGSKgAAVIEMNQRAIELGMA 606
Cdd:pfam01558  148 AIKKRFPGK-AKVIELNLKAFRAGYE 172
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 805-1098 1.23e-26

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: 109.64  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  805 GACAGCGETPYARLITQLFGDRMLIANATGCSSIWGASAPsipyTTNHRGhgpAWANSLFEDnaefglgmmlggqavrqq 884
Cdd:cd03376     6 RACAGCGAALALRHVLKALGPDTVVVNPTGCLEVITTPYP----YTAWRV---PWIHVAFEN------------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  885 iaddmTAALALPVsdelsdamrqwlakqdegegtrERAdrlserlaaekegvplLEQLWQNRDYFVrrsqWIFGGDGWAY 964
Cdd:cd03376    61 -----AAAVASGI----------------------EAA----------------LKALGRGKDITV----VAFAGDGGTA 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  965 DIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFA-----AQGKRTRKKDLGMMAMSYGNVYVAQVAM 1039
Cdd:cd03376    94 DIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTpvgkvSFGKKQPKKDLPLIMAAHNIPYVATASV 173

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 575523317 1040 GADKDqTLRAIAEAEAWPGPSLVIAYAACINhGLKAGMRCSQREAKRAVEAGYWHLWRY 1098
Cdd:cd03376   174 AYPED-LYKKVKKALSIEGPAYIHILSPCPT-GWRFDPSKTIEIARLAVETGFWPLYEY 230
EKR pfam10371
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
 621-676 1.32e-22

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: 91.76  E-value: 1.32e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317   621 DEPAAQASAMMPDFIRDILQPMNRQCGDQLPVSAFVgmEDGTFPSGTAAWEKRGIA 676
Cdd:pfam10371    1 EELPPPVPEDAPEFVKNVLAPMNAGEGDELPVSAFP--EDGTFPTGTSAYEKRGIA 54
NapF COG1145
Ferredoxin [Energy production and conversion];
504-766 3.15e-22

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 97.10  E-value: 3.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  504 GTFLLNCSWSDAELEQHLPVGFKRYLARENIHFYTLNAVDIARELGLGGRFNMLMQAAFFKLAAIIDPQTAADYLKQAVE 583
Cdd:COG1145     1 AALLLDLKEALSPKLKVLYAVVTGILGKIILNVIAGALLKAVALGGLLPIIGILAKEAFDALKDVLGILGAIVIGIGAGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  584 KSYGSKGAAVIEMNQRAIELGMASLHQVTIPAHWATLDEPAAQASAMMPDFIRDILQPMNRQCGDQLPVSAFVgmEDGTF 663
Cdd:COG1145    81 IVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPV--DALAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  664 PSGTAAWEKRGIALEVP--VWQPEGCTQCNQCAFICPHAAIRPallngeehdaapvgllskpaqgaKEYHYHLAISPLDC 741
Cdd:COG1145   159 SGGKKIEEELKIAIKKAkaVIDAEKCIGCGLCVKVCPTGAIRL-----------------------KDGKPQIVVDPDKC 215

                         250       260
                  ....*....|....*....|....*
gi 575523317  742 SGCGNCVDICPArgKALKMQSLDSQ 766
Cdd:COG1145   216 IGCGACVKVCPV--GAISLEPKEIE 238
EKR smart00890
Domain of unknown function; EKR is a short, 33 residue, domain found in bacterial and some ...
 618-677 1.02e-21

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: 89.21  E-value: 1.02e-21
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317    618 ATLDEPAAQASAMmPDFIRDILQPMNRQCGDQLPVSAFVgmEDGTFPSGTAAWEKRGIAL 677
Cdd:smart00890    1 SELDEPPPVPEEA-PEFVKNVVAPMNAGEGDDLPVSAFP--EDGTFPTGTAAYEKRGIAV 57
PRK11865 PRK11865
pyruvate synthase subunit beta;
806-1098 2.37e-21

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 95.94  E-value: 2.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  806 ACAGCGETPYARLITQLFGDRMLIANATGCSSIwgASAPSiPYTTnhrgHGPAWANSLFEDNAEFGLGMmlggqavrqqi 885
Cdd:PRK11865   20 ACAGCGAAIAMRLALKALGKNTVIVVATGCLEV--ITTPY-PETA----WNVPWIHVAFENAAAVASGI----------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  886 addmtaalalpvsdelsdamrqwlakqdegegtrERAdrlserLAAEKEGVPLLeqlwqnrdyfvrrsqwIFGGDGWAYD 965
Cdd:PRK11865   82 ----------------------------------ERA------VKALGKKVNVV----------------AIGGDGGTAD 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  966 IGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTR-----KKDLGMMAMSYGNVYVAQVAMG 1040
Cdd:PRK11865  106 IGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRgedrpKKNMPLIMAAHGIPYVATASIG 185

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317 1041 ADKD--QTLRAIAEAEawpGPSLVIAYAACInHGLKAGMRCSQREAKRAVEAGYWHLWRY 1098
Cdd:PRK11865  186 YPEDfmEKVKKAKEVE---GPAYIQVLQPCP-TGWGFPPEKTIEIGRLAVETGYWPLFEI 241
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 662-760 3.12e-21

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: 88.96  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  662 TFPSGTAAWEKRGIALEVPVWQPEGCTQCNQCAFICPHAAIRPallngeehdaapvgllskpaqgaKEYHYhLAISPLDC 741
Cdd:COG1144     7 TEPGGTAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIRV-----------------------DDGKY-YGIDYDYC 62

                          90
                  ....*....|....*....
gi 575523317  742 SGCGNCVDICPArgKALKM 760
Cdd:COG1144    63 KGCGICAEVCPV--KAIEM 79
PFOR_II pfam17147
Pyruvate:ferredoxin oxidoreductase core domain II; PFOR_II is a core domain of the anaerobic ...
 265-370 1.42e-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: 81.92  E-value: 1.42e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   265 AERVIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHfFAQLPKTVQRIAVLDRTKEPGAQAePLCLDVKNAF 344
Cdd:pfam17147    1 AEVVIVAMGSVAGTAKSAVDRLREEGIKVGLLRLRTFRPFPEEE-LKELLAGVKKVVVLDRNISFGSPG-QLGTEVKAAL 78

                           90       100
                   ....*....|....*....|....*.
gi 575523317   345 YHHDDAPLIVGGRyaLGGKDVLPNDI 370
Cdd:pfam17147   79 YDSDPPVVNFIAG--LGGRDITPEDI 102
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
957-1098 3.46e-16

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 80.52  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  957 FGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQ 1036
Cdd:PRK11864   98 WAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVAT 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317 1037 VAMGADKDqTLRAIAEAEAWPGPSLVIAYAACinhglKAGMRCSQRE----AKRAVEAGYWHLWRY 1098
Cdd:PRK11864  178 ASIAYPED-FIRKLKKAKEIRGFKFIHLLAPC-----PPGWRFDPDKtieiARLAVETGVWPLFEY 237
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
 19-169 1.40e-14

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: 72.38  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   19 EVAAIYPITPSTPMAENVDEwaaqgkknlfGQPVRLMEMQSEAGAAGAVHGALQAGALTTTY-TASQGLLLMIPNMYKIA 97
Cdd:cd06586    13 RHVFGYPGDEISSLLDALRE----------GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIvTSGTGLLNAINGLADAA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575523317   98 GELLPGVFHVSARALATNSLNIFGDHQDVMAVRQTGCAMLAENNVQQVMDLSAVAHLAAIKGRIPFVNFFDG 169
Cdd:cd06586    83 AEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYASQGPVVVRLPR 154
PorC_KorC TIGR02175
2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate family; A number ...
 417-604 8.22e-14

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: 70.84  E-value: 8.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   417 KFWGMGSDGTVGANK--SAIKIIGDKtplYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYVERY 494
Cdd:TIGR02175    5 RFHGRGGQGAVTASQllAEAAFLEGK---YAQAFPEFGAERRGAPVRAFLRISDRPIRVHSQIYEPDYVVVLDPTLLKTV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   495 DLLDGLKPGGTFLLNCSWSDAELeqhlpvgfkrylaRENIHFYTLNAVDIAreLGLGGR--FNMLMQAAFFKLAAIIDPQ 572
Cdd:TIGR02175   82 NVTAGLKEDGILIVNTKKDPEEL-------------RKELKVYTVDATKIA--LVVLGRpiVNTPMLGAFAKVTGLVSLE 146

                          170       180       190
                   ....*....|....*....|....*....|..
gi 575523317   573 TaadyLKQAVEKSYGSKGAaviEMNQRAIELG 604
Cdd:TIGR02175  147 S----LEKAIEESFPGKLA---EANAKAVERA 171
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 945-1069 2.61e-13

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: 69.86  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  945 NRDYFVrrsqWIFGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGM 1024
Cdd:cd03375    67 NPDLTV----IVVSGDGDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLA 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 575523317 1025 MAMSYGNVYVAQVAMGaDKDQTLRAIAEAEAWPGPSLVIAYAACI 1069
Cdd:cd03375   143 LALAAGATFVARGFSG-DIKQLKEIIKKAIQHKGFSFVEVLSPCP 186
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 684-760 1.61e-12

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: 63.61  E-value: 1.61e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523317  684 PEGCTQCNQCAFICPHAAIRpallngeehdaapvgllskpaQGAKEYHYHLAISPLDCSGCGNCVDICPArgKALKM 760
Cdd:COG1143     1 EDKCIGCGLCVRVCPVDAIT---------------------IEDGEPGKVYVIDPDKCIGCGLCVEVCPT--GAISM 54
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 675-760 1.06e-11

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 61.28  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  675 IALEVPVWQPEGCTQCNQCAFICPHAAIRPallngeEHDAAPVgllskpaqgakeyhyhlaISPLDCSGCGNCVDICPAr 754
Cdd:COG1149     1 VKRKIPVIDEEKCIGCGLCVEVCPEGAIKL------DDGGAPV------------------VDPDLCTGCGACVGVCPT- 55


                  ....*.
gi 575523317  755 gKALKM 760
Cdd:COG1149    56 -GAITL 60
PRK06853 PRK06853
indolepyruvate oxidoreductase subunit beta; Reviewed
 420-606 5.60e-10

indolepyruvate oxidoreductase subunit beta; Reviewed


Pssm-ID: 180732 [Multi-domain]  Cd Length: 197  Bit Score: 60.26  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  420 GMGSDGTVgankSAIKIIGdKTPLYAqayfSYDSKKS--------GGITVSHLRFGDrPINSPyLI--HRADFISCSQQS 489
Cdd:PRK06853   10 GVGGQGIL----LASKILG-EAALAA----GYDVKVSevhgmsqrGGSVVSHVRFGD-EVYSP-LIpeGKADLLLAFEPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  490 YVERYdlLDGLKPGGTFLLNcswsdAELEQHLPV--GFKRY---------LARENIHFYTLNAVDIARELGLGGRFNMLM 558
Cdd:PRK06853   79 EALRY--LPYLKKGGKVVVN-----TQPIVPVPVslGLAKYpedeeileeLKKLGIKVYVIDAEKIAKEAGNIKAANVVL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 575523317  559 QAAFFKLAAIidpqtAADYLKQAVEKSYGSKgaaVIEMNQRAIELGMA 606
Cdd:PRK06853  152 LGALAKFLPI-----DEETLEEAIKERVPPK---FVEVNLKAFEAGRE 191
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 955-1069 6.24e-10

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 61.78  E-value: 6.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  955 WIFGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYV 1034
Cdd:PRK11867   91 IVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALGAGATFV 170

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 575523317 1035 AQvAMGADKDQTLRAIAEAEAWPGPSLVIAYAACI 1069
Cdd:PRK11867  171 AR-GFDSDVKQLTELIKAAINHKGFSFVEILQPCP 204
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
687-753 3.99e-09

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 54.03  E-value: 3.99e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575523317   687 CTQCNQCAFICPHAAIRpallnGEEHDAAPVGLLSKPAQGAKEYHYHLAISPL--DCSGCGNCVDICPA 753
Cdd:pfam13484    1 CGSCGKCIDACPTGAIV-----GPEGVLDARRCISYLTIEKKGLIPDELRCLLgnRCYGCDICQDVCPW 64
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 687-752 2.78e-08

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: 50.99  E-value: 2.78e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317   687 CTQCNQCAFICPHAAIRPallngeehdaapvgllsKPAQGAKEYHyHLAISPLDCSGCGNCVDICP 752
Cdd:pfam12838    1 CIGCGACVAACPVGAITL-----------------DEVGEKKGTK-TVVIDPERCVGCGACVAVCP 48
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 680-761 3.56e-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: 53.17  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  680 PVWQPEGCTQCNQCAFICPHAAIRPallngeehdaAPVGLLSKPaqgakeyhyhLAISPLDCSGCGNCVDICParGKALK 759
Cdd:cd10549     1 LKYDPEKCIGCGICVKACPTDAIEL----------GPNGAIARG----------PEIDEDKCVFCGACVEVCP--TGAIE 58


                  ..
gi 575523317  760 MQ 761
Cdd:cd10549    59 LT 60
PRK08537 PRK08537
2-oxoacid:ferredoxin oxidoreductase subunit gamma;
436-605 7.21e-08

2-oxoacid:ferredoxin oxidoreductase subunit gamma;


Pssm-ID: 181462 [Multi-domain]  Cd Length: 177  Bit Score: 53.52  E-value: 7.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  436 IIGDKTPLYAQAYF----SYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYvERYdlLDGLKPGGTFLLncs 511
Cdd:PRK08537   21 ILGRAAALYDGKYAvqtqSYGPEARGGASKSEVVISDEEIDYPKVISPDILVAMSQEAY-DKY--LDDLKEGGTVIV--- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  512 wsDAELEQHLPVGFKrylarENIHFYTLNAVDIARE-LGLGGRFNMLMQAAFFKLAAIIDPQTAADYLKQAVEKsyGSKg 590
Cdd:PRK08537   95 --DPDLVPIREIEYE-----KKVKVYKVPFTEIAEEeIGLSIVANIVMLGALTKLTGIVSKEAIEKAILDSVPK--GTE- 164

                         170
                  ....*....|....*
gi 575523317  591 aaviEMNQRAIELGM 605
Cdd:PRK08537  165 ----EKNLMAFEKGY 175
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 684-752 2.53e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 48.94  E-value: 2.53e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575523317  684 PEGCTQCNQCAFICPHAAIRPAllngeehdaapvgllskpaqgaKEYHYHLAISPLDCSGCGNCVDICP 752
Cdd:COG1146     7 TDKCIGCGACVEVCPVDVLELD----------------------EEGKKALVINPEECIGCGACELVCP 53
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 957-1069 3.68e-07

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 53.34  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  957 FGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQ 1036
Cdd:PRK05778   94 VGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVAR 173

                          90       100       110
                  ....*....|....*....|....*....|...
gi 575523317 1037 vAMGADKDQTLRAIAEAEAWPGPSLVIAYAACI 1069
Cdd:PRK05778  174 -SFAGDVKQLVELIKKAISHKGFAFIDVLSPCV 205
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 680-759 4.14e-07

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 48.12  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  680 PVWQPEGCTQCNQCAFICPHAAIRpalLNGEehdaapvgllskpaqgakeyhyHLAISPLDCSGCGNCVDICPArgKALK 759
Cdd:COG2221    10 PKIDEEKCIGCGLCVAVCPTGAIS---LDDG----------------------KLVIDEEKCIGCGACIRVCPT--GAIK 62
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 659-760 5.05e-07

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 50.13  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  659 EDGTFPSGTAAWEkrgiaLEVPVWQPEGCTQCNQCAFICPHAAIrpallngeehdaapvglLSKPAQGAKEYHYHlaisp 738
Cdd:PRK09625   38 EQSSFTTSVAHWR-----VEKPVHNNEICINCFNCWVYCPDAAI-----------------LSRDKKLKGVDYSH----- 90

                          90       100
                  ....*....|....*....|..
gi 575523317  739 ldCSGCGNCVDICPARGKALKM 760
Cdd:PRK09625   91 --CKGCGVCVEVCPTNPKSLLM 110
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
680-770 5.66e-07

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 48.19  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  680 PVWQPEGCTQCNQCAFICPHAAIRpallngEEHDAApvgllskpaqgakeyhyhlAISPLDCSGCGNCVDICPArgKALK 759
Cdd:COG2768     6 PYVDEEKCIGCGACVKVCPVGAIS------IEDGKA-------------------VIDPEKCIGCGACIEVCPV--GAIK 58

                          90
                  ....*....|....
gi 575523317  760 MQSLDS---QRQMA 770
Cdd:COG2768    59 IEWEEDeefQEKMA 72
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 420-752 7.29e-07

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 52.31  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  420 GMGSDGTVgankSAIKIIGDKT---PLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYVERYDL 496
Cdd:PRK14028    9 GRGGQGIV----TATYIIANAAvidGFYAIANPEFGAERRGAPVKAFLTISKNPIEDQEPVKTPDVAVIFDDKLIDPMRF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  497 -LDGLKPGGTFLLNCSWSDAELeqhlpvgfKRYLARENIHFYTLNAVDIARE-LGL-------GGRFNMLMqaAFFKLAA 567
Cdd:PRK14028   85 aIDAVKPGGYVILNTGKQPEEA--------RKLVGRDDVYIVVLDAIGIARKhLKLdvpngplAGAFSKVM--GFPSLES 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  568 IidPQTAADYLKQAVEKSYgskgAAVIEMNQRAielgmaslhqVTIPAHWAtldEPAAQASAMMPDFIRDILQPMNRQCG 647
Cdd:PRK14028  155 I--RTAFETQLGKAVEENF----AATKEAYEVA----------VVIPPEKV---DASAKPKGIISTTSAFLTGPYELVGW 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  648 DQLPVSAFVGmEDGTFPSGTAAWEkrgiaLEVPVWQPEGCTQCNQCAFICPHAAIRPALLNGEehdaAPVGLLSKPAQGA 727
Cdd:PRK14028  216 QEVNKAGAVF-PGSSFPYLTGGWR-----IDKPVIDHSKCIMCRKCWLYCPDDAIIEAWREAE----GPRGRKFRMKMID 285

                         330       340
                  ....*....|....*....|....*
gi 575523317  728 KEYHYhlaispldCSGCGNCVDICP 752
Cdd:PRK14028  286 FDYQY--------CKGCGVCAEVCP 302
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 684-752 1.45e-06

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: 46.47  E-value: 1.45e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575523317   684 PEGCTQCNQCAFICPHAAIRPALLNGEEHDAAPVGLLSKpaqgakeyhyhlaispldCSGCGNCVDICP 752
Cdd:pfam13237    6 PDKCIGCGRCTAACPAGLTRVGAIVERLEGEAVRIGVWK------------------CIGCGACVEACP 56
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 687-753 5.24e-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: 44.99  E-value: 5.24e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575523317   687 CTQCNQCAFICPHAairpaLLNGEEHDAAPVGLLSKpAQGAKEYHYHLAISPLDCSGCGNCVDICPA 753
Cdd:pfam13183    2 CIRCGACLAACPVY-----LVTGGRFPGDPRGGAAA-LLGRLEALEGLAEGLWLCTLCGACTEVCPV 62
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
955-1064 6.32e-06

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 47.19  E-value: 6.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   955 WIFGGDGWAYDIGfGGLDHVLASGEDVNILVFDTEVYSNTGGQsskSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGnvyv 1034
Cdd:pfam02775   50 VAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYG---- 121

                           90       100       110
                   ....*....|....*....|....*....|
gi 575523317  1035 AQVAMGADKDQTLRAIAEAEAWPGPSLVIA 1064
Cdd:pfam02775  122 AKGARVESPEELEEALKEALEHDGPALIDV 151
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 687-760 7.93e-06

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: 47.25  E-value: 7.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  687 CTQCNQCAFICPHAAIRPALLngeehdAAPVGLLSKP----AQGAKEYHYHL--------AISPLD-------------- 740
Cdd:cd16373    16 CIRCGLCVEACPTGVIQPAGL------EDGLEGGRTPyldpREGPCDLCCDAcvevcptgALRPLDleeqkvkmgvavid 89

                          90       100
                  ....*....|....*....|....*....
gi 575523317  741 ---C------SGCGNCVDICPARGKALKM 760
Cdd:cd16373    90 kdrClawqggTDCGVCVEACPTEAIAIVL 118
Fer4_9 pfam13187
4Fe-4S dicluster domain;
687-752 6.50e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.39  E-value: 6.50e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317   687 CTQCNQCAFICPHAAIRPallngeehdaapvgllSKPAQGAKeyhyhLAISPLDCSGCGNCVDICP 752
Cdd:pfam13187    2 CTGCGACVAACPAGAIVP----------------DLVGQTIR-----GDIAGLACIGCGACVDACP 46
PRK08534 PRK08534
pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed
 417-602 7.00e-05

pyruvate ferredoxin oxidoreductase subunit gamma; Reviewed


Pssm-ID: 181460 [Multi-domain]  Cd Length: 181  Bit Score: 45.03  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  417 KFWGMGSDGTVGANKsAIKIIGDKTPLYAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYVERYDL 496
Cdd:PRK08534    5 RFHGRGGQGAVTAAE-ILAKAAFEDGKFSQAFPFFGVERRGAPVMAFTRIDDKPIRLRSQIYEPDYVIVQDPTLLDSVDV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  497 LDGLKPGGTFLLNCSWSDAELeqhlpvGFKRylareNIHFYTLNAVDIAreLGLGGR--FNMLMQAAFFKLAAIIDPqta 574
Cdd:PRK08534   84 TSGLKKDGIIIINTTKDPEDL------KYDT-----KAKVYTIDATKIA--LDVLGVpiVNTTMLGAFAGATGEVSL--- 147

                         170       180
                  ....*....|....*....|....*...
gi 575523317  575 aDYLKQAVEKSYGSKgaaVIEMNQRAIE 602
Cdd:PRK08534  148 -ESLKKAILERFPGK---LGEKNAEAVE 171
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 957-1069 1.40e-04

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 45.13  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  957 FGGDGWAYDIGFGGLDHVLASGEDVNILVFDTEVYSNTGGQSSKSTPVAAIAKFAAQGKRTRKKDLGMMAMSYGNVYVAQ 1036
Cdd:PRK11866   83 YGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVAR 162

                          90       100       110
                  ....*....|....*....|....*....|...
gi 575523317 1037 vAMGADKDQTLRAIAEAEAWPGPSLVIAYAACI 1069
Cdd:PRK11866  163 -GFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCV 194
ACS_1 cd01916
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ...
 687-838 2.26e-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: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  687 CTQCNQCAFICPHaairpALLNGEEHDAAPVGLLSKPAQGAKEyhyhlaispldCSGCGNCVDICPARGKALKMQSLDSQ 766
Cdd:cd01916   367 CTDCGWCTRACPN-----SLRIKEAMEAAKEGDFSGLADLFDQ-----------CVGCGRCEQECPKEIPIINMIEKAAR 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  767 RQMA-----------PVWDyalaltpksnpfrkttVKGSQFETPLL--EFSGACA--GCGETPY----ARLITQLFGDRM 827
Cdd:cd01916   431 ERIKeekgkmragrgPIKD----------------TEIRKVGAPIVlgDIPGVIAlvGCSNYPNgtkdVYKIAEEFLERN 494

                         170
                  ....*....|.
gi 575523317  828 LIANATGCSSI 838
Cdd:cd01916   495 YIVVTTGCMAM 505
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 684-752 2.63e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.41  E-value: 2.63e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575523317  684 PEGCTQCNQCAFICPHAAIRpallngEEHDAApvgllskpaqgakeyhyhlAISPLDCSGCGNCVDICP 752
Cdd:COG4231    21 EDKCTGCGACVKVCPADAIE------EGDGKA-------------------VIDPDLCIGCGSCVQVCP 64
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 673-760 2.82e-04

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 42.02  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   673 RG-IALEVPVWQPEGCTQCNQCAFICPHAAIRpalLNGEEHDAApvgllskpaqgaKEYHYHLAISPLDCSGCGNCVDIC 751
Cdd:TIGR01971   30 RGrIVLTRDPNGEEKCIGCTLCAAVCPADAIR---VVPAEGEDG------------KRRLKFYEINFGRCIFCGLCEEAC 94


                   ....*....
gi 575523317   752 PArgKALKM 760
Cdd:TIGR01971   95 PT--DAIVL 101
PRK14029 PRK14029
pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional
 417-595 7.74e-04

pyruvate/ketoisovalerate ferredoxin oxidoreductase subunit gamma; Provisional


Pssm-ID: 172523 [Multi-domain]  Cd Length: 185  Bit Score: 41.93  E-value: 7.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  417 KFWGMGSDGTVgankSAIKIIGDKTPL---YAQAYFSYDSKKSGGITVSHLRFGDRPINSPYLIHRADFISCSQQSYVER 493
Cdd:PRK14029    5 RFHGRGGQGAV----TAANILAEAAFLegkYVQAFPFFGVERRGAPVTAFTRIDEKPIRIKTQIYEPDVVVVLDPSLLDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  494 YDLLDGLKPGGTFLLNCSWSDAELEQHLpvgfKRYLARENIhfytLNAVDIARE-LGLGGRfNMLMQAAFFKLAAIIDPQ 572
Cdd:PRK14029   81 VDVTAGLKDGGIVIVNTEKSKEEVLEKL----KKKPKKLAL----VDATTIALEiLGLPIT-NTAILGAVAKATGLVKIE 151

                         170       180
                  ....*....|....*....|...
gi 575523317  573 TAADYLKQAVEKSYGSKGAAVIE 595
Cdd:PRK14029  152 SVEEAIKDTFSGELGEKNAKAAR 174
oorA PRK09627
2-oxoglutarate synthase subunit alpha;
264-306 1.26e-03

2-oxoglutarate synthase subunit alpha;


Pssm-ID: 182002 [Multi-domain]  Cd Length: 375  Bit Score: 42.39  E-value: 1.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 575523317  264 DAERVIIAMGSVCDTVQEVVDTLNAAGEKVGllsvhLFRPFSL 306
Cdd:PRK09627  274 DAEILIIAYGSVSLSAKEAIKRLREEGIKVG-----LFRPITL 311
PRK07119 PRK07119
2-ketoisovalerate ferredoxin reductase; Validated
 264-320 1.42e-03

2-ketoisovalerate ferredoxin reductase; Validated


Pssm-ID: 235942 [Multi-domain]  Cd Length: 352  Bit Score: 42.16  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575523317  264 DAERVIIAMGSVCDTVQEVVDTLNAAGEKVGllsvhLFRPFSLAHF----FAQLPKTVQRI 320
Cdd:PRK07119  246 DAELVLVAYGTSARIAKSAVDMAREEGIKVG-----LFRPITLWPFpekaLEELADKGKGF 301
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
684-752 2.51e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 41.20  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  684 PEGCTQCNQCAFICP-HAAIRpallNGEehdaapvgllskpaqgakeyhyhlaISPLDCSGCGNCVDICP 752
Cdd:COG0348   209 RGDCIDCGLCVKVCPmGIDIR----KGE-------------------------INQSECINCGRCIDACP 249
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 687-752 2.63e-03

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: 39.24  E-value: 2.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575523317  687 CTQCNQCAFICPHAAIrpallngeEHDAAPVGLLSKPaqgakeyhyhlaisplDCSGCGNCVDICP 752
Cdd:cd16372    49 CNQCGECIDVCPTGAI--------TRDANGVVMINKK----------------LCVGCLMCVGFCP 90
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 681-752 2.70e-03

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: 39.29  E-value: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523317  681 VWQPEGCTQCNQ--CAFICPHAAIrpallngeehdaapvgllSKPAQGAkeyhyhLAISPLDCSGCGNCVDICP 752
Cdd:cd04410    44 AFLPVSCMHCEDppCVKACPTGAI------------------YKDEDGI------VLIDEDKCIGCGSCVEACP 93
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 690-763 3.24e-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: 39.15  E-value: 3.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575523317  690 CNQCAFICPHAAIRPALLNGeeHDAAPVgllskpaqgakeyhyhlaISPLDCSGCGNCVDICPARgkALKMQSL 763
Cdd:cd10564    88 CRSCQDACPTQAIRFRPRLG--GIALPE------------------LDADACTGCGACVSVCPVG--AITLTPL 139
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
 268-356 5.21e-03

Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.


Pssm-ID: 460693 [Multi-domain]  Cd Length: 124  Bit Score: 38.35  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317   268 VIIAMGSVCDTVQEVVDTLNAAGEKVGLLSVHLFRPFSLAHFFAQLPKTVQRIAVLDRTKEPGAQAEPLCLDVKNAFYHH 347
Cdd:pfam02780   13 TIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEVAAALAEEAFDGL 92


                   ....*....
gi 575523317   348 DDAPLIVGG 356
Cdd:pfam02780   93 DAPVLRVGG 101
RnfC COG4656
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfC subunit [Energy production and ...
 678-754 5.83e-03

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


Pssm-ID: 443694 [Multi-domain]  Cd Length: 451  Bit Score: 40.51  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575523317  678 EVPVWQPEGCTQCNQCAFICPhAAIRPALLN----GEEHDAApvgllskpaqgaKEYHyhlaisPLDCSGCGNCVDICPA 753
Cdd:COG4656   357 EVPPPEEQPCIRCGRCVDACP-MGLLPQQLYwyarAGDFDKA------------EEYN------LMDCIECGCCSYVCPS 417


                  .
gi 575523317  754 R 754
Cdd:COG4656   418 K 418
 
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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