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Conserved domains on  [gi|167667617|gb|EDS11747|]
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glycine radical enzyme activase, YjjW family [Anaerotruncus colihominis DSM 17241]

Protein Classification

YjjW family glycine radical enzyme activase( domain architecture ID 11499336)

YjjW family glycine radical enzyme activase is a radical SAM protein that is paired with and appears to activate a glycyl radical enzyme of unknown function, designated YjjI

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 4-279 4.51e-175

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


:

Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 483.67  E-value: 4.51e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617    4 TAPVNRIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETQNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACII 83
Cdd:TIGR04041   1 KALVNKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   84 TCPHLASPRVKTMTPRQVMDEVCKNIPFIRGITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAYPALMEVC 163
Cdd:TIGR04041  81 VCPHQSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKAAGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  164 DGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRLKLITFRK 243
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEIDGLARFLGDLPSDTRIKLIAFRH 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167667617  244 NGVRGRLSETPSPSPETMQAHADYARAAGFNNIVLT 279
Cdd:TIGR04041 241 HGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
 
Name Accession Description Interval E-value
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 4-279 4.51e-175

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 483.67  E-value: 4.51e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617    4 TAPVNRIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETQNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACII 83
Cdd:TIGR04041   1 KALVNKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   84 TCPHLASPRVKTMTPRQVMDEVCKNIPFIRGITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAYPALMEVC 163
Cdd:TIGR04041  81 VCPHQSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKAAGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  164 DGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRLKLITFRK 243
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEIDGLARFLGDLPSDTRIKLIAFRH 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167667617  244 NGVRGRLSETPSPSPETMQAHADYARAAGFNNIVLT 279
Cdd:TIGR04041 241 HGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 1-278 9.44e-70

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 215.43  E-value: 9.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   1 MTLTAPVNRIIPFSTVDGPGS-RTSVFFQACNIACAYCHNPETQNMCRNcgacvpgcpegalsmADGRvvwdpdkcvecd 79
Cdd:COG1180    1 EEVRGRIYGISPFSTVDGPGSiRLSVFTQGCNLRCPYCHNPEISQGRPD---------------AAGR------------ 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  80 aciitcphlasprvkTMTPRQVMDEVCKNIPFIR---GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAY 156
Cdd:COG1180   54 ---------------ELSPEELVEEALKDRGFLDscgGVTFSGGEPTLQPEFLLDLAKLAKELGLHTALDTNGYIPEEAL 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617 157 PALMEVCDGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRL 236
Cdd:COG1180  119 EELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPV 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 167667617 237 KLITFRKngvRGRLSETPSPSPETMQAHADYARAAGFNNIVL 278
Cdd:COG1180  199 HLLPFHP---LYKLEDVPPPSPETLERAREIAREYGLKYVYI 237
pflA PRK11145
pyruvate formate lyase 1-activating protein;
1-262 1.09e-24

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 98.95  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   1 MTLTAPVNRIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETqnmcrncgacvpgcpegalsmadgrvvWDPDKCvecda 80
Cdd:PRK11145   1 MSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDT---------------------------WDTHGG----- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  81 ciitcphlasprvKTMTPRQVMDEVCKNIPFIR----GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNG------- 149
Cdd:PRK11145  49 -------------KEVTVEELMKEVVTYRHFMNasggGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGfvrrydp 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617 150 IVDlaaypALMEVCDGVMLDVKAWDSEMHRALTGADNanvKKNLGF---LSEHGKLEEIRIVCIDELVDTRAAIDGIART 226
Cdd:PRK11145 116 VID-----ELLDVTDLVMLDLKQMNDEIHQNLVGVSN---HRTLEFaryLAKRNQKTWIRYVVVPGWTDDDDSAHRLGEF 187

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 167667617 227 IGSRRTQTRLKLITFRKNGVRG--------RLSETPSPSPETMQ 262
Cdd:PRK11145 188 IKDMGNIEKIELLPYHELGKHKweamgeeyKLDGVKPPSKETME 231
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 16-44 2.26e-08

4Fe-4S single cluster 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: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 51.79  E-value: 2.26e-08
                          10        20
                  ....*....|....*....|....*....
gi 167667617   16 VDGPGSRTSVFFQACNIACAYCHNPETQN 44
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWD 29
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 28-87 5.40e-08

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 50.65  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCH----NPE---------------TQNMCRNCG--ACVPGCPEGALSM--ADGRVVWDPDKCVECDACIIT 84
Cdd:cd10550   12 RTCELACSLKHegvfNPSlsrirvvrfepegldVPVVCRQCEdaPCVEACPVGAISRdeETGAVVVDEDKCIGCGMCVEA 91


                 ...
gi 167667617  85 CPH 87
Cdd:cd10550   92 CPF 94
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 46-87 2.80e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.16  E-value: 2.80e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDpDKCVECDACIITCPH 87
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPVWG-HNCTHCLACIHRCPK 227
 
Name Accession Description Interval E-value
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 4-279 4.51e-175

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 483.67  E-value: 4.51e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617    4 TAPVNRIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETQNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACII 83
Cdd:TIGR04041   1 KALVNKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   84 TCPHLASPRVKTMTPRQVMDEVCKNIPFIRGITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAYPALMEVC 163
Cdd:TIGR04041  81 VCPHQSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKAAGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  164 DGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRLKLITFRK 243
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEIDGLARFLGDLPSDTRIKLIAFRH 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 167667617  244 NGVRGRLSETPSPSPETMQAHADYARAAGFNNIVLT 279
Cdd:TIGR04041 241 HGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 1-278 9.44e-70

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 215.43  E-value: 9.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   1 MTLTAPVNRIIPFSTVDGPGS-RTSVFFQACNIACAYCHNPETQNMCRNcgacvpgcpegalsmADGRvvwdpdkcvecd 79
Cdd:COG1180    1 EEVRGRIYGISPFSTVDGPGSiRLSVFTQGCNLRCPYCHNPEISQGRPD---------------AAGR------------ 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  80 aciitcphlasprvkTMTPRQVMDEVCKNIPFIR---GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAY 156
Cdd:COG1180   54 ---------------ELSPEELVEEALKDRGFLDscgGVTFSGGEPTLQPEFLLDLAKLAKELGLHTALDTNGYIPEEAL 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617 157 PALMEVCDGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRL 236
Cdd:COG1180  119 EELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPV 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 167667617 237 KLITFRKngvRGRLSETPSPSPETMQAHADYARAAGFNNIVL 278
Cdd:COG1180  199 HLLPFHP---LYKLEDVPPPSPETLERAREIAREYGLKYVYI 237
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
 13-272 9.86e-50

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 165.97  E-value: 9.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   13 FSTVDGPGSRTSVFFQACNIACAYCHNPETQ----------NMCRNCGACVPGCPEGA---LSMADGRVV--WDPDKCVE 77
Cdd:TIGR02494   7 YSVHDGPGIRTTVFLKGCPLRCKWCSNPESQrkspellfkeNRCLGCGKCVEVCPAGTarlSELADGRNRiiIRREKCTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   78 CDACIITCPHLASPRV-KTMTPRQVMDEVCKNIPFIR----GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVD 152
Cdd:TIGR02494  87 CGKCTEACPSGALSIVgEEMTVEEVMRVVLRDSIFYRnsggGVTLSGGEPLLQPEFALALLQACHERGIHTAVETSGFTP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  153 LAAYPALMEVCDGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRT 232
Cdd:TIGR02494 167 WETIEKVLPYVDLFLFDIKHLDDERHKEVTGVDNEPILENLEALAAAGKNVVIRIPVIPGFNDSEENIEAIAAFLRKLEP 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 167667617  233 -QTRLKLITFRKNGVR-----GR---LSETPSPSPETMQAHADYARAAG 272
Cdd:TIGR02494 247 gVDEIDLLPYHRLGENkyrqlGReypDSEIPDPAEEQLLELKEIFESKG 295
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
 13-262 2.11e-36

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 129.41  E-value: 2.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   13 FSTVDGPGSRTSVFFQACNIACAYCHNPETqnmcrncgacvpgcpegalsmadgrvvWDPDKCVEcdaciitcphlaspr 92
Cdd:TIGR02493   8 MGTVDGPGIRFVVFMQGCPLRCQYCHNPDT---------------------------WDLKGGTE--------------- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   93 vktMTPRQVMDEVCKNIPFIR----GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLA--AYPALMEVCDGV 166
Cdd:TIGR02493  46 ---VTPEELIKEVGSYKDFFKasggGVTFSGGEPLLQPEFLSELFKACKELGIHTCLDTSGFLGGCteAADELLEYTDLV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  167 MLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQTRLKLITFRKNGV 246
Cdd:TIGR02493 123 LLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRNKPIWIRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGV 202

                         250       260
                  ....*....|....*....|....
gi 167667617  247 --------RGRLSETPSPSPETMQ 262
Cdd:TIGR02493 203 ykwealgiEYPLEGVKPPNKEQLE 226
pflA PRK11145
pyruvate formate lyase 1-activating protein;
1-262 1.09e-24

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 98.95  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   1 MTLTAPVNRIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETqnmcrncgacvpgcpegalsmadgrvvWDPDKCvecda 80
Cdd:PRK11145   1 MSVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDT---------------------------WDTHGG----- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  81 ciitcphlasprvKTMTPRQVMDEVCKNIPFIR----GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNG------- 149
Cdd:PRK11145  49 -------------KEVTVEELMKEVVTYRHFMNasggGVTASGGEAILQAEFVRDWFRACKKEGIHTCLDTNGfvrrydp 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617 150 IVDlaaypALMEVCDGVMLDVKAWDSEMHRALTGADNanvKKNLGF---LSEHGKLEEIRIVCIDELVDTRAAIDGIART 226
Cdd:PRK11145 116 VID-----ELLDVTDLVMLDLKQMNDEIHQNLVGVSN---HRTLEFaryLAKRNQKTWIRYVVVPGWTDDDDSAHRLGEF 187

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 167667617 227 IGSRRTQTRLKLITFRKNGVRG--------RLSETPSPSPETMQ 262
Cdd:PRK11145 188 IKDMGNIEKIELLPYHELGKHKweamgeeyKLDGVKPPSKETME 231
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 43-89 5.04e-13

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 62.76  E-value: 5.04e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 167667617  43 QNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPHLA 89
Cdd:COG2221   14 EEKCIGCGLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGA 60
PRK10076 PRK10076
pyruvate formate lyase II activase; Provisional
 85-274 7.25e-13

pyruvate formate lyase II activase; Provisional


Pssm-ID: 182224 [Multi-domain]  Cd Length: 213  Bit Score: 65.94  E-value: 7.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  85 CPHLASPRV-KTMTPRQVMDEVCKNIPFIR----GITTSGGECSLRADFLTELFTMAQKEGLSCLMDSNGIVDLAAYPAL 159
Cdd:PRK10076   7 CPSGAFERIgRDITLDALEREVMKDDIFFRtsggGVTLSGGEVLMQAEFATRFLQRLRLWGVSCAIETAGDAPASKLLPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617 160 MEVCDGVMLDVKAWDSEMHRALTGADNANVKKNLGFLSEHGKLEEIRIVCIDELVDTRAAIDGIARTIGSRRTQtRLKLI 239
Cdd:PRK10076  87 AKLCDEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPGFTLSRENMQQALDVLIPLGIK-QIHLL 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 167667617 240 TF--------RKNGVRGRLSETPSPSPETMQAHADYARAAGFN 274
Cdd:PRK10076 166 PFhqygepkyRLLGKTWSMKEVPAPSSADVATMREMAERAGFQ 208
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
46-89 5.47e-12

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 60.13  E-value: 5.47e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPHLA 89
Cdd:COG2768   13 CIGCGACVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGA 56
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 46-89 3.15e-10

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 55.12  E-value: 3.15e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 167667617  46 CRNCGACVPGCPEGALSMADGR-VVWDPDKCVECDACIITCPHLA 89
Cdd:COG1149   13 CIGCGLCVEVCPEGAIKLDDGGaPVVDPDLCTGCGACVGVCPTGA 57
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 46-89 8.46e-10

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 54.28  E-value: 8.46e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPHLA 89
Cdd:COG4231   24 CTGCGACVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
22-87 4.53e-09

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 56.57  E-value: 4.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167667617  22 RTSVFFQACNIACAYCHNPET---QNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPH 87
Cdd:COG4624   66 VAISCIQVRGIIIIDKRGPSIirdKEKCKNCYPCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAVCPF 134
NapF COG1145
Ferredoxin [Energy production and conversion];
46-89 1.75e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 53.96  E-value: 1.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 167667617  46 CRNCGACVPGCPEGALSMADGR--VVWDPDKCVECDACIITCPHLA 89
Cdd:COG1145  184 CIGCGLCVKVCPTGAIRLKDGKpqIVVDPDKCIGCGACVKVCPVGA 229
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 16-44 2.26e-08

4Fe-4S single cluster 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: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 51.79  E-value: 2.26e-08
                          10        20
                  ....*....|....*....|....*....
gi 167667617   16 VDGPGSRTSVFFQACNIACAYCHNPETQN 44
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWD 29
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 28-86 5.03e-08

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 51.87  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCHN-PETQN----------------------MCRNCG--ACVPGCPEGALS-MADGRVVWDPDKCVECDAC 81
Cdd:COG0437   19 RACVVACKEENNlPVGVTwrrvrryeegefpnvewlfvpvLCNHCDdpPCVKVCPTGATYkREDGIVLVDYDKCIGCRYC 98


                 ....*
gi 167667617  82 IITCP 86
Cdd:COG0437   99 VAACP 103
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 28-87 5.40e-08

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 50.65  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCH----NPE---------------TQNMCRNCG--ACVPGCPEGALSM--ADGRVVWDPDKCVECDACIIT 84
Cdd:cd10550   12 RTCELACSLKHegvfNPSlsrirvvrfepegldVPVVCRQCEdaPCVEACPVGAISRdeETGAVVVDEDKCIGCGMCVEA 91


                 ...
gi 167667617  85 CPH 87
Cdd:cd10550   92 CPF 94
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 9-44 1.08e-07

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 50.43  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 167667617    9 RIIPFSTVDGPGSRTSVFFQACNIACAYCHNPETQN 44
Cdd:TIGR02491   4 NIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWN 39
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 43-86 1.39e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 49.32  E-value: 1.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 167667617  43 QNMCRNCGACVPGCPEGALSM-ADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10549   77 EEKCIGCGLCVKVCPVDAITLeDELEIVIDKEKCIGCGICAEVCP 121
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 45-87 1.45e-07

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: 49.31  E-value: 1.45e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 167667617  45 MCRNCG--ACVPGCPEGALSM-ADGRVVWDPDKCVECDACIITCPH 87
Cdd:cd04410   49 SCMHCEdpPCVKACPTGAIYKdEDGIVLIDEDKCIGCGSCVEACPY 94
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 45-86 1.75e-07

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 50.29  E-value: 1.75e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 167667617  45 MCRNC--GACVPGCPEGALS-MADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10561   68 QCMHCldPACVSACPVGALRkTPEGPVTYDEDKCIGCRYCMVACP 112
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 46-89 2.04e-07

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: 47.05  E-value: 2.04e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVW----DPDKCVECDACIITCPHLA 89
Cdd:COG1143    4 CIGCGLCVRVCPVDAITIEDGEPGKvyviDPDKCIGCGLCVEVCPTGA 51
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 46-87 2.78e-07

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: 46.37  E-value: 2.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 167667617   46 CRNCGACVPGCPEGALSM-----ADGRVVW--DPDKCVECDACIITCPH 87
Cdd:pfam12838   1 CIGCGACVAACPVGAITLdevgeKKGTKTVviDPERCVGCGACVAVCPT 49
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
46-87 2.95e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 50.70  E-value: 2.95e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPH 87
Cdd:PRK07118 215 CIGCGKCVKACPAGAITMENNLAVIDQEKCTSCGKCVEKCPT 256
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
28-89 3.33e-07

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 48.50  E-value: 3.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCHNPETQN------------------MCRNC--GACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPH 87
Cdd:COG1142   16 RTCEAACAVAHEGEEGEpflprirvvrkagvsapvQCRHCedAPCAEVCPVGAITRDDGAVVVDEEKCIGCGLCVLACPF 95


                 ..
gi 167667617  88 LA 89
Cdd:COG1142   96 GA 97
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 46-86 3.70e-07

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 48.84  E-value: 3.70e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNCG--ACVPGCPEGALSMAD-GRVVWDPDKCVECDACIITCP 86
Cdd:cd10562   70 CMHCTdaACVKVCPTGALYKTEnGAVVVDEDKCIGCGYCVAACP 113
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 20-86 4.21e-07

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


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 48.33  E-value: 4.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167667617  20 GSRTSVFFQACNIACAYCHNPetqnmcrncgACVPGCPEGALS-MADGRVVWDPDKCVECDACIITCP 86
Cdd:cd16371   40 GEFPEVFAYFLSMSCNHCENP----------ACVKVCPTGAITkREDGIVVVDQDKCIGCGYCVWACP 97
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
46-86 4.50e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 49.93  E-value: 4.50e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCP 86
Cdd:PRK07118 141 CLGLGSCVAACPFDAIHIENGLPVVDEDKCTGCGACVKACP 181
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 46-86 4.67e-07

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 47.78  E-value: 4.67e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 167667617  46 CRNCGACVPGCPEGALSMADG-----RVVWDPDKCVECDACIITCP 86
Cdd:cd10549    8 CIGCGICVKACPTDAIELGPNgaiarGPEIDEDKCVFCGACVEVCP 53
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 46-89 6.24e-07

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 45.86  E-value: 6.24e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 167667617  46 CRNCGACVPGCPEGALSMADGR---VVWDPDKCVECDACIITCPHLA 89
Cdd:COG1146   10 CIGCGACVEVCPVDVLELDEEGkkaLVINPEECIGCGACELVCPVGA 56
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 29-86 6.59e-07

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 47.65  E-value: 6.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167667617  29 ACNIACAYCHNPETQ-------------NMCRNCGA--CVPGCPEGALSM-ADGRVVWDPDKCVECDACIITCP 86
Cdd:cd16374   13 ACEIACAREHSGKPRisvevvedlasvpVRCRHCEDapCMEVCPTGAIYRdEDGAVLVDPDKCIGCGMCAMACP 86
PRK13795 PRK13795
hypothetical protein; Provisional
 46-86 1.04e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 49.61  E-value: 1.04e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 167667617  46 CRNCGACVPGCPEGALSMADG--RVVWDPDKCVECDACIITCP 86
Cdd:PRK13795 583 CVGCGVCVGACPTGAIRIEEGkrKISVDEEKCIHCGKCTEVCP 625
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 45-87 1.30e-06

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 46.87  E-value: 1.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 167667617  45 MCRNCG--ACVPGCPEGALSM--ADGRVVWDPDKCVECDACIITCPH 87
Cdd:cd10563   56 QCRHCDepPCVKACMSGAMHKdpETGIVIHDEEKCVGCWMCVMVCPY 102
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 46-89 1.68e-06

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: 45.04  E-value: 1.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVW-DPDKCVECDACIITCPHLA 89
Cdd:COG1144   32 CIGCGLCWIVCPDGAIRVDDGKYYGiDYDYCKGCGICAEVCPVKA 76
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 28-99 2.07e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 48.87  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCHNPETQNM----------------------CRNC--GACVPGCPEGALSMADGRVVWDPDKCVECDACII 83
Cdd:PRK12809  16 HACEIACAVAHNQENWPLshsdfrprihvvgkgqaanpvaCHHCnnAPCVTACPVNALTFQSDSVQLDEQKCIGCKRCAI 95

                         90
                 ....*....|....*.
gi 167667617  84 TCPHLASPRVKTMTPR 99
Cdd:PRK12809  96 ACPFGVVEMVDTIAQK 111
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 46-87 2.80e-06

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 47.16  E-value: 2.80e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 167667617  46 CRNCGACVPGCPEGALSMADGRVVWDpDKCVECDACIITCPH 87
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPVWG-HNCTHCLACIHRCPK 227
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 28-86 5.48e-06

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 47.43  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  28 QACNIACAYCHN----PETQN------------------MCRNC--GACVPGCPEGALSMADGRVVWDPDKCVECDACII 83
Cdd:PRK12769  16 HACEIACVMAHNdeqhVLSQHhfhpritvikhqqqrsavTCHHCedAPCARSCPNGAISHVDDSIQVNQQKCIGCKSCVV 95


                 ...
gi 167667617  84 TCP 86
Cdd:PRK12769  96 ACP 98
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-86 6.77e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 44.63  E-value: 6.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 167667617  44 NMCRNCGACVPGCPEGALSMADGRVVwdPDKCVECDACIITCP 86
Cdd:cd16372   77 KLCVGCLMCVGFCPEGAMFKHEDYPE--PFKCIACGICVKACP 117
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 8-86 7.84e-06

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 45.22  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617   8 NRIIPFSTVDGPGSRTSVFFQACNiacaYCHNPetqnmcrncgACVPGCPEGALS-MADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10551   31 NRVLEYEVGEYPNVKRTFLPVLCN----HCENP----------PCVKVCPTGATYkREDGIVLVDYDKCIGCRYCMAACP 96
Fer4_9 pfam13187
4Fe-4S dicluster domain;
45-87 1.14e-05

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 41.77  E-value: 1.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 167667617   45 MCRNCGACVPGCPEGALSMADG----RVVWDPDKCVECDACIITCPH 87
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVgqtiRGDIAGLACIGCGACVDACPR 47
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 34-86 1.48e-05

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of 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: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 43.89  E-value: 1.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167667617  34 CAYCHNPEtqnmcrncgaCVPGCPEGALSM--ADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10553   58 CFHCENPW----------CVKACPTGAMQKreKDGIVYVDQELCIGCKACIEACP 102
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
43-105 2.38e-05

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 45.24  E-value: 2.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167667617  43 QNMCRNCGACVPGCPEGALSMADGRVVW-DPDKCVECDACIITCPHLAsPRVKTMTPRQVMDEV 105
Cdd:COG1148  495 PEKCTGCGRCVEVCPYGAISIDEKGVAEvNPALCKGCGTCAAACPSGA-ISLKGFTDDQILAQI 557
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 45-86 2.51e-05

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 43.40  E-value: 2.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  45 MCRNC--GACVPGCPEGALSMADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10554   55 QCRQCedAPCANVCPVGAISQEDGVVQVDEERCIGCKLCVLACP 98
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 46-86 3.08e-05

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


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 43.16  E-value: 3.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNCG--ACVPGCPEGALSMAD-GRVVWDPDKCVECDACIITCP 86
Cdd:cd16366   70 CMHCTdaGCLAACPTGAIIRTEtGTVVVDPETCIGCGYCVNACP 113
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 27-86 4.76e-05

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 43.72  E-value: 4.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167667617  27 FQACnIACAYCHNP--ETQNMCRNCGACVPGCPEGALSMADGR-VVWDPDKCVECDACIITCP 86
Cdd:PRK00783 151 WQPG-SACGYKYYPriEVSEDCDECEKCVEACPRGVLELKEGKlVVTDLLNCSLCKLCERACP 212
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 49-86 4.85e-05

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


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 43.83  E-value: 4.85e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 167667617  49 CGACVPGCPEGALSMA-DGRVVWDPDKCVECDACIITCP 86
Cdd:COG2878  142 CGDCIKACPFDAIVGAaKGMHTVDEDKCTGCGLCVEACP 180
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
34-86 4.91e-05

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 43.89  E-value: 4.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167667617  34 CAYCHNPetqnmcrncgACVPGCPEGALSM--ADGRVVWDPDKCVECDACIITCP 86
Cdd:PRK10882 112 CMHCVDP----------NCVSVCPVSALTKdpKTGIVHYDKDVCTGCRYCMVACP 156
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 46-86 6.14e-05

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: 39.93  E-value: 6.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 167667617   46 CRNCGACVPGCPEGALS-------MADGRVVWDPDKCVECDACIITCP 86
Cdd:pfam13237   9 CIGCGRCTAACPAGLTRvgaiverLEGEAVRIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 46-86 1.34e-04

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 40.72  E-value: 1.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNC--GACVPGCPEGALSM-ADGRVVWDPDKCVECDACIITCP 86
Cdd:cd16370   53 CRACedPPCAEACPTGALEPrKGGGVVLDKEKCIGCGNCVKACI 96
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
46-89 1.78e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 41.97  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 167667617  46 CRNCGACVPGCPEGaLSMADGRVvwDPDKCVECDACIITCPHLA 89
Cdd:COG0348  212 CIDCGLCVKVCPMG-IDIRKGEI--NQSECINCGRCIDACPKDA 252
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 44-86 2.30e-04

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: 40.07  E-value: 2.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167667617  44 NMCRNCGACVPGCPEGALSM---------ADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10549   40 DKCVFCGACVEVCPTGAIELtpegkeyvpKEKEAEIDEEKCIGCGLCVKVCP 91
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-89 3.62e-04

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 39.63  E-value: 3.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 167667617  44 NMCRNCGACVPGCPEGALSMADGRVVW-DPDKCVECDACIITCPHLA 89
Cdd:cd16372   47 NVCNQCGECIDVCPTGAITRDANGVVMiNKKLCVGCLMCVGFCPEGA 93
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 67-89 4.78e-04

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: 38.11  E-value: 4.78e-04
                         10        20
                 ....*....|....*....|...
gi 167667617  67 RVVWDPDKCVECDACIITCPHLA 89
Cdd:COG1144   24 RPVVDEDKCIGCGLCWIVCPDGA 46
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 34-87 4.90e-04

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 41.19  E-value: 4.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167667617  34 CAYCHNPetqnmcrncgACVPGCPEGAL--SMADGRVVWDPDKCVECDACIITCPH 87
Cdd:cd10557  179 CNHCLNP----------ACVAACPSGAIykREEDGIVLIDQDRCRGWRMCVSACPY 224
PRK10330 PRK10330
electron transport protein HydN;
39-89 7.39e-04

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 39.49  E-value: 7.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167667617  39 NPETQNMCRNC--GACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPHLA 89
Cdd:PRK10330  51 NVSTATVCRQCedAPCANVCPNGAISRDKGFVHVMQERCIGCKTCVVACPYGA 103
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 38-86 7.52e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 39.63  E-value: 7.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167667617  38 HNPEtqnMCRNCGACVPGCPEGALSM----ADGRVVWDPD--KCVECDACIITCP 86
Cdd:PRK12387  35 YNPQ---QCIGCAACVNACPSNALTVetdlATGELAWEFNlgRCIFCGRCEEVCP 86
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 46-89 9.19e-04

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 37.78  E-value: 9.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167667617  46 CRNCGACVPGCPEGALSMAD------GRV--VWDPDKCVECDACIITCPHLA 89
Cdd:PRK09626  18 CKACDICVSVCPAGVLAMRIdphavlGKMikVVHPESCIGCRECELHCPDFA 69
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
46-87 1.04e-03

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 36.70  E-value: 1.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167667617   46 CRNCGACVPGCPEGALSMADGrvVWDPDKCVE------------------------CDACIITCPH 87
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEG--VLDARRCISyltiekkglipdelrcllgnrcygCDICQDVCPW 64
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
34-89 1.10e-03

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 39.47  E-value: 1.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 167667617  34 CAYCHNPetqnmcrncgACVPGCP-EGALSMADGRVVWDPDKCVECDACIITCPHLA 89
Cdd:PRK14993 100 CNHCDNP----------PCVPVCPvQATFQREDGIVVVDNKRCVGCAYCVQACPYDA 146
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 45-86 4.67e-03

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: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 35.69  E-value: 4.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 167667617   45 MCRNC--GACVPGCPEGALSM--ADGRVVWDPDKCVECDACIITCP 86
Cdd:pfam13247   9 QCRHClnPPCKASCPVGAIYKdeETGAVLLDEKTCRGWRECVSACP 54
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 43-141 6.24e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 37.36  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167667617  43 QNMCRNCGACVPGCPEGALSMADGRVVWDPDKCVECDACIITCPHLASPRVKTMTPRQVMDEvCKNIPFIRGITTSGGEC 122
Cdd:cd03110   63 QEKCIRCGNCERVCKFGAILEFFQKLIVDESLCEGCGACVIICPRGAIYLKDRDTGKIFISS-SDGGPLVHGRLNIGEEN 141

                         90
                 ....*....|....*....
gi 167667617 123 SlradflTELFTMAQKEGL 141
Cdd:cd03110  142 S------GKLVTELRKKAL 154
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 33-86 7.45e-03

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 36.98  E-value: 7.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167667617  33 ACAYCHNPetqnmcrncgACVPGCP-EGAL-SMADGRVVWDPDKCVECDACIITCP 86
Cdd:cd10558   69 GCMHCADP----------GCLKACPsPGAIvQYANGIVDFQSDKCIGCGYCIKGCP 114
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-86 7.55e-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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 36.13  E-value: 7.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167667617  33 ACAYCHNPEtqnmcrncgaCVPGCPEGALSMADGRVVWDPDKCVECDACIITCP 86
Cdd:cd16367   56 ACRHCVDPV----------CMIGCPTGAIHRDDGGEVVISDACCGCGNCASACP 99
 
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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