NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1592170950|ref|WP_132083330|]
View 

[FeFe] hydrogenase, group A [Anaerospora hongkongensis]

Protein Classification

Fe_hyd_lg_C and Fe_hyd_SSU domain-containing protein( domain architecture ID 13535246)

Fe_hyd_lg_C and Fe_hyd_SSU domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FeFe_hydrog_A6 super family cl48993
NADH-dependent [FeFe] hydrogenase, group A6;
11-457 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


The actual alignment was detected with superfamily member NF040763:

Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 627.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEIC----PVGAIEGE---------PGKAQTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlqerr 77
Cdd:NF040763  143 DPNKCILCRRCVTVCnevqGVGALGAVnrgfktvvgPAFGKPLADTACTNCGQCIAVC---------------------- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  78 mpanvrePLFAAYYVGDLPQVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYDTNFAAD 157
Cdd:NF040763  201 -------PTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAAD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 158 LTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAVYSVAIM 237
Cdd:NF040763  274 LTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKSPQQMFGAIAKTYYAEKMGIDPKDIVVVSIM 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 238 PCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRTAYE 317
Cdd:NF040763  354 PCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYE 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 318 ILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQPKll 397
Cdd:NF040763  434 VLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPI-- 511

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 398 lPEDQAAAYKLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:NF040763  512 -HTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEPLSHKAHELLHTHYTK 570
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
11-457 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 627.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEIC----PVGAIEGE---------PGKAQTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlqerr 77
Cdd:NF040763  143 DPNKCILCRRCVTVCnevqGVGALGAVnrgfktvvgPAFGKPLADTACTNCGQCIAVC---------------------- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  78 mpanvrePLFAAYYVGDLPQVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYDTNFAAD 157
Cdd:NF040763  201 -------PTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAAD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 158 LTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAVYSVAIM 237
Cdd:NF040763  274 LTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKSPQQMFGAIAKTYYAEKMGIDPKDIVVVSIM 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 238 PCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRTAYE 317
Cdd:NF040763  354 PCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYE 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 318 ILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQPKll 397
Cdd:NF040763  434 VLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPI-- 511

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 398 lPEDQAAAYKLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:NF040763  512 -HTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEPLSHKAHELLHTHYTK 570
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 8-395 1.65e-174

[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length.


Pssm-ID: 274171 [Multi-domain]  Cd Length: 374  Bit Score: 494.15  E-value: 1.65e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGK-------------AQTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlq 74
Cdd:TIGR02512   2 IVRDMSKCIGCGRCVRACTNVQIVGALGFlnrggktevapkfGRLLDESNCIGCGQCSLVC------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  75 errmpanvrePLFAAYYVGDLPQVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYDTNF 154
Cdd:TIGR02512  63 ----------PVGAITEKDHVDRVLKALADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 155 AADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAVYSV 234
Cdd:TIGR02512 133 AADLTIMEEGTELLERLKNGGKLPMFTSCCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYWAKKMGIDPEDVYVV 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 235 AIMPCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRT 314
Cdd:TIGR02512 213 SIMPCTAKKDEAQRPELKSDGYRDVDAVLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRT 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 315 AYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQP 394
Cdd:TIGR02512 293 AYEIVTGKELELIEFKAVRGLDGVKEATVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQP 372


                  .
gi 1592170950 395 K 395
Cdd:TIGR02512 373 K 373
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
10-455 2.15e-170

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 486.46  E-value: 2.15e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAqTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlqerrmpanvrePLFAA 89
Cdd:COG4624    88 RDKEKCKNCYPCVRACPVKAIKVDDGKA-EIDEEKCISCGQCVAVC-----------------------------PFGAI 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  90 YYVGDLPQVKEALADHSLfTMVQCAPAVRVAiaedFGmelGSLVPGKLAAALRRLGFKRIYDTNFAADLTIMEEGSELVK 169
Cdd:COG4624   138 TEKSDIEKVKKALKDPEK-VVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLE 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 170 RImENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAEldNIapaavYSVAIMPCTCKKSEALRP 249
Cdd:COG4624   210 RL-KKGKLPMITSCCPAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYYAP--DI-----KVVFIGPCIAKKFEAKRP 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 250 EMAdsgfRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPlgcYSGAGQIFGVTGGVMEAAIRTAYEILtqtplenvnv 329
Cdd:COG4624   282 EMK----GDVDYVLTFRELARMIKEAGIDLANLEEEEFDNE---SSGAGRIFGVTGGVMEAALRTAYELL---------- 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 330 ttvrggqgikrvtieAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQPKLLLPEDQAAAYklr 409
Cdd:COG4624   345 ---------------PDGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKR--- 406

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950 410 sASMYRhdEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHY 455
Cdd:COG4624   407 -VALYA--KEAPIRKSHENPEILDLYREFLGKPLSEKAHELLHTHY 449
Hydr_FeFe_Clost NF040762
ferredoxin hydrogenase, clostridial type; Members of this family of hydrogenases share ...
 10-455 6.22e-154

ferredoxin hydrogenase, clostridial type; Members of this family of hydrogenases share full-length homology with many other iron-only hydrogenases, but differ in transferrring electrons only to ferredoxins (EC 1.12.7.2) and not to NAD(P)+.


Pssm-ID: 468722 [Multi-domain]  Cd Length: 572  Bit Score: 449.16  E-value: 6.22e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICP------------------VGAIEGEpgkaqTIDAVKCVMCGQCVQVCSAYAscfeTYQYSHAQ 71
Cdd:NF040762  141 IDRSKCVLCGRCVAACKektgtesikfidkngeriVGTEDDK-----CFDDTNCLLCGQCVAACPVDA----LSEKSHID 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  72 RlqerrmpanvreplfaayyvgdlpqVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYD 151
Cdd:NF040762  212 R-------------------------VKEALEDPNKHVIVAMAPSVRTAMGELFKMGYGVDVTGKLYTALRMLGFDKIFD 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 152 TNFAADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAV 231
Cdd:NF040762  267 INFGADMTIMEEATELIERIKNNGPFPMFTSCCPGWVRQVENYFPELLDNLSSAKSPQQIFGAASKTYYPSISGIDPKDV 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 232 YSVAIMPCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAA 311
Cdd:NF040762  347 FTVTIMPCTAKKFEADRPEMENDGLRNIDAVLTTRELAKMIKDAKIDFANLEDSEADPAMGEYTGAGAIFGATGGVMEAA 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 312 IRTAYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGG 391
Cdd:NF040762  427 LRTAKDFLENKDLENIEYTQVRGLDGIKEATVEIGGKEYNIAVINGASNVFKFMKSGKMDEKQYHFIEVMACPGGCINGG 506

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950 392 GQPKLLLPEDQAAAY-KLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHY 455
Cdd:NF040762  507 GQPHVNSKDREKIDYrKLRASVLYNQDKNLPKRKSHENPALIKMYDNYMGKPGHGLAHELLHFKY 571
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
111-391 1.31e-151

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 432.04  E-value: 1.31e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 111 VQCAPAVRVAIAEDFGMELgSLVPGKLAAALRRLGFKRIYDTNFAADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKY 190
Cdd:pfam02906   5 AQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPGWVKY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 191 VEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIapaavYSVAIMPCTCKKSEALRPEMADSgfRDVDAVLTTRELAY 270
Cdd:pfam02906  84 VEKYYPELLPNLSTCKSPMQMFGALIKTYYAEDLKI-----YVVSIMPCTAKKFEAARPEMKGD--RDVDAVLTTRELAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 271 LIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRTAYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQL 350
Cdd:pfam02906 157 MIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEIGGTTV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1592170950 351 KTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGG 391
Cdd:pfam02906 237 KVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
 408-457 2.49e-21

Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold.


Pssm-ID: 214899 [Multi-domain]  Cd Length: 52  Bit Score: 86.92  E-value: 2.49e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  408 LRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:smart00902   1 QRAEALYNIDKSLPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHD 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 8-55 8.11e-12

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: 62.41  E-value: 8.11e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd10549    73 AEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVC 120
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 11-55 2.06e-07

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 49.45  E-value: 2.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  11 DAELCTGCQRCCEICPVGAIEGEPG-KAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK08348   40 DVDKCVGCRMCVTVCPAGVFVYLPEiRKVALWTGRCVFCGQCVDVC 85
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 13-59 3.66e-05

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: 45.24  E-value: 3.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  13 ELCTGCQRCCEICPVGAIEGEPGKaqtidAV---KCVMCGQCVQVCSAYA 59
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEMEDGK-----PVwghNCTHCLACIHRCPKEA 229
 
Name Accession Description Interval E-value
FeFe_hydrog_A6 NF040763
NADH-dependent [FeFe] hydrogenase, group A6;
11-457 0e+00

NADH-dependent [FeFe] hydrogenase, group A6;


Pssm-ID: 468723 [Multi-domain]  Cd Length: 571  Bit Score: 627.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEIC----PVGAIEGE---------PGKAQTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlqerr 77
Cdd:NF040763  143 DPNKCILCRRCVTVCnevqGVGALGAVnrgfktvvgPAFGKPLADTACTNCGQCIAVC---------------------- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  78 mpanvrePLFAAYYVGDLPQVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYDTNFAAD 157
Cdd:NF040763  201 -------PTGALTEKDNTDKVWDALADPDKHVVVQTAPAVRVALGEEFGLPPGTIVTGKMVAALRRLGFDKVFDTDFAAD 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 158 LTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAVYSVAIM 237
Cdd:NF040763  274 LTIMEEGTELLDRLKNGGVLPMITSCSPGWVKFCEHFYPDLLDNLSTCKSPQQMFGAIAKTYYAEKMGIDPKDIVVVSIM 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 238 PCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRTAYE 317
Cdd:NF040763  354 PCTAKKYEAARPEMSVDGYPDVDIVLTTRELARMIKEAGIDFANLPDEEFDNPLGESTGAGVIFGATGGVMEAALRTAYE 433

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 318 ILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQPKll 397
Cdd:NF040763  434 VLTGKELEKVDFTEVRGLEGIKEATVDINGTEVKVAVAHGLGNARKLLEKIKAGESDYHFIEIMACPGGCIGGGGQPI-- 511

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 398 lPEDQAAAYKLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:NF040763  512 -HTGNVDVRKKRAKALYEEDKNKPLRKSHENPAIKKLYEEFLGEPLSHKAHELLHTHYTK 570
FeFe_hydrog_A TIGR02512
[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and ...
 8-395 1.65e-174

[FeFe] hydrogenase, group A; This model describes iron-only hydrogenases of anaerobic and microaerophilic bacteria and protozoa. This model is narrower, and covers a longer stretch of sequence, than pfam02906. This family represents a division among families that belong to pfam02906, which also includes proteins such as nuclear prelamin A recognition factor in animals. Note that this family shows some heterogeneity in terms of periplasmic, cytosolic, or hydrogenosome location, NAD or NADP dependence, and overal protein protein length.


Pssm-ID: 274171 [Multi-domain]  Cd Length: 374  Bit Score: 494.15  E-value: 1.65e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGK-------------AQTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlq 74
Cdd:TIGR02512   2 IVRDMSKCIGCGRCVRACTNVQIVGALGFlnrggktevapkfGRLLDESNCIGCGQCSLVC------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  75 errmpanvrePLFAAYYVGDLPQVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYDTNF 154
Cdd:TIGR02512  63 ----------PVGAITEKDHVDRVLKALADPKKVVVVQIAPAVRVALGEEFGMPIGTDVTGKMVAALRKLGFDYVFDTNF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 155 AADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAVYSV 234
Cdd:TIGR02512 133 AADLTIMEEGTELLERLKNGGKLPMFTSCCPGWVNYAEKYYPELLPNLSSCKSPQQMLGAVIKTYWAKKMGIDPEDVYVV 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 235 AIMPCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRT 314
Cdd:TIGR02512 213 SIMPCTAKKDEAQRPELKSDGYRDVDAVLTTRELARMIKEAGIDFAKLPDSQFDSPFGEYSGAGAIFGATGGVMEAALRT 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 315 AYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQP 394
Cdd:TIGR02512 293 AYEIVTGKELELIEFKAVRGLDGVKEATVDIGGTKVKVAVAHGLGNARKLLDDVKAGEADYHFIEVMACPGGCVNGGGQP 372


                  .
gi 1592170950 395 K 395
Cdd:TIGR02512 373 K 373
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
10-455 2.15e-170

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 486.46  E-value: 2.15e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAqTIDAVKCVMCGQCVQVCsayascfetyqyshaqrlqerrmpanvrePLFAA 89
Cdd:COG4624    88 RDKEKCKNCYPCVRACPVKAIKVDDGKA-EIDEEKCISCGQCVAVC-----------------------------PFGAI 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  90 YYVGDLPQVKEALADHSLfTMVQCAPAVRVAiaedFGmelGSLVPGKLAAALRRLGFKRIYDTNFAADLTIMEEGSELVK 169
Cdd:COG4624   138 TEKSDIEKVKKALKDPEK-VVAQVAPAVRGQ----FG---GTVTPGKLVAALKKLGFDDVFETAFGADLTIMEEAKELLE 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 170 RImENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAEldNIapaavYSVAIMPCTCKKSEALRP 249
Cdd:COG4624   210 RL-KKGKLPMITSCCPAWVKLIEKYYPELLPNLSPCKSPMQAFGALIKTYYAP--DI-----KVVFIGPCIAKKFEAKRP 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 250 EMAdsgfRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPlgcYSGAGQIFGVTGGVMEAAIRTAYEILtqtplenvnv 329
Cdd:COG4624   282 EMK----GDVDYVLTFRELARMIKEAGIDLANLEEEEFDNE---SSGAGRIFGVTGGVMEAALRTAYELL---------- 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 330 ttvrggqgikrvtieAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGGGQPKLLLPEDQAAAYklr 409
Cdd:COG4624   345 ---------------PDGLELKVAVVSGLKNCRKLLEEIKAGKIDYHFIEVMACPGGCIGGPGQPIPPGSLEKRRKR--- 406

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950 410 sASMYRhdEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHY 455
Cdd:COG4624   407 -VALYA--KEAPIRKSHENPEILDLYREFLGKPLSEKAHELLHTHY 449
Hydr_FeFe_Clost NF040762
ferredoxin hydrogenase, clostridial type; Members of this family of hydrogenases share ...
 10-455 6.22e-154

ferredoxin hydrogenase, clostridial type; Members of this family of hydrogenases share full-length homology with many other iron-only hydrogenases, but differ in transferrring electrons only to ferredoxins (EC 1.12.7.2) and not to NAD(P)+.


Pssm-ID: 468722 [Multi-domain]  Cd Length: 572  Bit Score: 449.16  E-value: 6.22e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICP------------------VGAIEGEpgkaqTIDAVKCVMCGQCVQVCSAYAscfeTYQYSHAQ 71
Cdd:NF040762  141 IDRSKCVLCGRCVAACKektgtesikfidkngeriVGTEDDK-----CFDDTNCLLCGQCVAACPVDA----LSEKSHID 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  72 RlqerrmpanvreplfaayyvgdlpqVKEALADHSLFTMVQCAPAVRVAIAEDFGMELGSLVPGKLAAALRRLGFKRIYD 151
Cdd:NF040762  212 R-------------------------VKEALEDPNKHVIVAMAPSVRTAMGELFKMGYGVDVTGKLYTALRMLGFDKIFD 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 152 TNFAADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIAPAAV 231
Cdd:NF040762  267 INFGADMTIMEEATELIERIKNNGPFPMFTSCCPGWVRQVENYFPELLDNLSSAKSPQQIFGAASKTYYPSISGIDPKDV 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 232 YSVAIMPCTCKKSEALRPEMADSGFRDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAA 311
Cdd:NF040762  347 FTVTIMPCTAKKFEADRPEMENDGLRNIDAVLTTRELAKMIKDAKIDFANLEDSEADPAMGEYTGAGAIFGATGGVMEAA 426

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 312 IRTAYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGG 391
Cdd:NF040762  427 LRTAKDFLENKDLENIEYTQVRGLDGIKEATVEIGGKEYNIAVINGASNVFKFMKSGKMDEKQYHFIEVMACPGGCINGG 506

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950 392 GQPKLLLPEDQAAAY-KLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHY 455
Cdd:NF040762  507 GQPHVNSKDREKIDYrKLRASVLYNQDKNLPKRKSHENPALIKMYDNYMGKPGHGLAHELLHFKY 571
Fe_hyd_lg_C pfam02906
Iron only hydrogenase large subunit, C-terminal domain;
111-391 1.31e-151

Iron only hydrogenase large subunit, C-terminal domain;


Pssm-ID: 397172  Cd Length: 277  Bit Score: 432.04  E-value: 1.31e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 111 VQCAPAVRVAIAEDFGMELgSLVPGKLAAALRRLGFKRIYDTNFAADLTIMEEGSELVKRIMENKALPMFTSCCPAWVKY 190
Cdd:pfam02906   5 AQIAPAVRGAFGEEFGLPP-TVTTGKLVAALRKLGFDYVFDTAFGADLTIMEEATEFLERLEKGKKLPMFTSCCPGWVKY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 191 VEDEYPELIGHLSSCKSPQQMAGTMFKTYGAELDNIapaavYSVAIMPCTCKKSEALRPEMADSgfRDVDAVLTTRELAY 270
Cdd:pfam02906  84 VEKYYPELLPNLSTCKSPMQMFGALIKTYYAEDLKI-----YVVSIMPCTAKKFEAARPEMKGD--RDVDAVLTTRELAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 271 LIKEAGIDFNSLPEEGFDNPLGCYSGAGQIFGVTGGVMEAAIRTAYEILTQTPLENVNVTTVRGGQGIKRVTIEAGSVQL 350
Cdd:pfam02906 157 MIKEAGIDFAKLEDEEFDNPLGESSGAGRIFGVTGGVMEAALRTAYELLTGKELPAIEFKEVRGLEGIKEATVEIGGTTV 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1592170950 351 KTVVVAGLKNAAGLLEEIKLGKADFHFMEVMTCPAGCITGG 391
Cdd:pfam02906 237 KVAVVSGLKNARKLLEKIKAGELKYHFIEVMACPGGCIGGG 277
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 1-392 3.93e-57

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 195.50  E-value: 3.93e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   1 MMEGKQYvsIDAELCTGCQRC---------------CE-ICPVGAIE-GEPGKAqTIDAVKCVMCGQCVQVCsayascfe 63
Cdd:TIGR04105 132 MVNGRAY--IDQEKCIECGKCkkacpynaiveierpCEkACPVGAISsDEDGRA-VIDYDKCISCGACMVAC-------- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  64 tyqyshaqrlqerrmpanvrePLFAAYYVGDLPQVKEALADH-SLFTMVqcAPAvrvaIAEDFGMELGslvPGKLAAALR 142
Cdd:TIGR04105 201 ---------------------PFGAISDKSQIVQVIKALKSGkKVYAMV--APA----IVGQFGPKAT---PGQVKTALK 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 143 RLGFKRIYDTNFAADLTIMEEGSELVKRiMENKALPMFTSCCPAWVKYVEDEYPELIGHLSSCKSPQQMAGTMFKtygaE 222
Cdd:TIGR04105 251 KLGFADVVEVALGADMVAVHEAEEFAER-VEEGKKFMTTSCCPAFVNMIKKHFPELAENISTTVSPMVATARYIK----K 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 223 LDniaPAAVySVAIMPCTCKKSEALRPEMADsgfrDVDAVLTTRELAYLIKEAGIDFNSLPEEGFDNPlgcySGAGQIFG 302
Cdd:TIGR04105 326 KD---PDAK-VVFIGPCIAKKLEAQRDEVKG----DVDYVLTFEELAAMFDAKGIDLEECEEEDLDDA----SAFGRGFA 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950 303 VTGGVMEAairtayeiltqtplenvnvttvrggqgIKRVTIEAGS-VQLKTVVVAGLKNAAGLLEEIKLGKADFHFMEVM 381
Cdd:TIGR04105 394 VSGGVAAA---------------------------VKAAIKEKGPdVEVKPVKCNGLDECKKALTLAKAGKLPGNFIEGM 446

                         410
                  ....*....|.
gi 1592170950 382 TCPAGCITGGG 392
Cdd:TIGR04105 447 ACEGGCVGGPG 457
Fe_hyd_SSU pfam02256
Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only ...
 406-457 2.98e-25

Iron hydrogenase small subunit; This family represents the small subunit of the Fe-only hydrogenases EC:1.18.99.1. The subunit is comprised of alternating random coil and alpha helical structures that encompasses the large subunit in a novel protein fold.


Pssm-ID: 460511 [Multi-domain]  Cd Length: 56  Bit Score: 97.96  E-value: 2.98e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950 406 YKLRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:pfam02256   4 RKKRAEALYKIDKNKPLRKSHENPAVKKLYEEFLGEPLSHKAHELLHTHYTP 55
Fe_hyd_SSU smart00902
Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, ...
 408-457 2.49e-21

Iron hydrogenase small subunit; Many microorganisms, such as methanogenic, acetogenic, nitrogen-fixing, photosynthetic, or sulphate-reducing bacteria, metabolise hydrogen. Hydrogen activation is mediated by a family of enzymes, termed hydrogenases, which either provide these organisms with reducing power from hydrogen oxidation, or act as electron sinks. There are two hydrogenases families that differ functionally from each other: NiFe hydrogenases tend to be more involved in hydrogen oxidation, while Iron-only FeFe (Fe only) hydrogenases in hydrogen production. Fe only hydrogenases show a common core structure, which contains a moiety, deeply buried inside the protein, with an Fe-Fe dinuclear centre, nonproteic bridging, terminal CO and CN- ligands attached to each of the iron atoms, and a dithio moiety, which also bridges the two iron atoms and has been tentatively assigned as a di(thiomethyl)amine. This common core also harbours three [4Fe-4S] iron-sulphur clusters. In FeFe hydrogenases, as in NiFe hydrogenases, the set of iron-sulphur clusters is dispersed regularly between the dinuclear Fe-Fe centre and the molecular surface. These clusters are distant by about 1.2 nm from each other but the [4Fe-4S] cluster closest to the dinuclear centre is covalently bound to one of the iron atoms though a thiolate bridging ligand. The moiety including the dinuclear centre, the thiolate bridging ligand, and the proximal [4Fe-4S] cluster is known as the H-cluster. A channel, lined with hydrophobic amino acid side chains, nearly connects the dinuclear centre and the molecular surface. Furthermore hydrogen-bonded water molecule sites have been identified at the interior and at the surface of the protein. The small subunit is comprised of alternating random coil and alpha helical structures that encompass the large subunit in a novel protein fold.


Pssm-ID: 214899 [Multi-domain]  Cd Length: 52  Bit Score: 86.92  E-value: 2.49e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  408 LRSASMYRHDEEQQFRKSHENPAIQDVYEKFLGEPLGHKSHKLLHTHYVA 457
Cdd:smart00902   1 QRAEALYNIDKSLPLRKSHENPAVKKLYEEFLGGPLSHKAHELLHTHYHD 50
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 8-59 2.60e-13

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 65.06  E-value: 2.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtIDAVKCVMCGQCVQVCSAYA 59
Cdd:COG4231    17 YVIDEDKCTGCGACVKVCPADAIEEGDGKAV-IDPDLCIGCGSCVQVCPVDA 67
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 2-59 3.06e-13

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 64.69  E-value: 3.06e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1592170950   2 MEGKQYVSIDAELCTGCQRCCEICPVGAIEGEPGKAqTIDAVKCVMCGQCVQVCSAYA 59
Cdd:COG2221     4 IIGTWPPKIDEEKCIGCGLCVAVCPTGAISLDDGKL-VIDEEKCIGCGACIRVCPTGA 60
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
7-55 4.13e-13

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 64.37  E-value: 4.13e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1592170950   7 YVSIDAELCTGCQRCCEICPVGAIEGEPGKAqTIDAVKCVMCGQCVQVC 55
Cdd:COG2768     5 KPYVDEEKCIGCGACVKVCPVGAISIEDGKA-VIDPEKCIGCGACIEVC 52
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 4-55 7.58e-13

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 63.21  E-value: 7.58e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950   4 GKQYVSIDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:COG1149     2 KRKIPVIDEEKCIGCGLCVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVC 53
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 8-55 8.11e-12

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: 62.41  E-value: 8.11e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd10549    73 AEIDEEKCIGCGLCVKVCPVDAITLEDELEIVIDKEKCIGCGICAEVC 120
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 10-55 1.57e-11

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: 61.64  E-value: 1.57e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIE----GEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd10549     3 YDPEKCIGCGICVKACPTDAIElgpnGAIARGPEIDEDKCVFCGACVEVC 52
NapF COG1145
Ferredoxin [Energy production and conversion];
8-55 2.34e-11

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 63.59  E-value: 2.34e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQ-TIDAVKCVMCGQCVQVC 55
Cdd:COG1145   177 AVIDAEKCIGCGLCVKVCPTGAIRLKDGKPQiVVDPDKCIGCGACVKVC 225
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 7-59 5.51e-11

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 58.18  E-value: 5.51e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950   7 YVSIDAELCTGCQRCCEICPVGAIEGEP--GKAQTIDAVKCVMCGQCVQVCSAYA 59
Cdd:COG1146     2 MPVIDTDKCIGCGACVEVCPVDVLELDEegKKALVINPEECIGCGACELVCPVGA 56
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 13-55 1.38e-10

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: 57.06  E-value: 1.38e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  13 ELCTGCQRCCEICPVGAIEGEPGKAQ---TIDAVKCVMCGQCVQVC 55
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAITIEDGEPGkvyVIDPDKCIGCGLCVEVC 47
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 10-59 2.88e-10

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: 56.60  E-value: 2.88e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVCSAYA 59
Cdd:COG1144    27 VDEDKCIGCGLCWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
7-55 6.45e-09

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 54.28  E-value: 6.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950   7 YVSIDAELCTGCQRCCEICPVGAIEGEPGKAQTIdAVKCVMCG------QCVQVC 55
Cdd:COG1142    75 AVVVDEEKCIGCGLCVLACPFGAITMVGEKSRAV-AVKCDLCGgreggpACVEAC 128
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-55 1.24e-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: 53.35  E-value: 1.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtidAVKCVMCG---QCVQVC 55
Cdd:cd10550    75 VVVDEDKCIGCGMCVEACPFGAIRVDPETGK---AIKCDLCGgdpACVKVC 122
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
1-55 1.65e-08

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 56.79  E-value: 1.65e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1592170950   1 MMEGKQYVSIDAELCTGCQRCCEICPVGAIE-GEPGKAQtIDAVKCVMCGQCVQVC 55
Cdd:COG1148   484 LGVEPSVAEVDPEKCTGCGRCVEVCPYGAISiDEKGVAE-VNPALCKGCGTCAAAC 538
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 8-59 1.95e-08

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: 52.78  E-value: 1.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI--EGEPGKaqtidAVKCVMCGQ---------CVQVCSAYA 59
Cdd:cd04410    75 VLIDEDKCIGCGSCVEACPYGAIvfDPEPGK-----AVKCDLCGDrldeglepaCVKACPTGA 132
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 7-55 7.11e-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: 50.86  E-value: 7.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1592170950   7 YVSIDAELCTGCQRCCEICPVGAIE--------GEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd10549    34 GPEIDEDKCVFCGACVEVCPTGAIEltpegkeyVPKEKEAEIDEEKCIGCGLCVKVC 90
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 15-55 1.60e-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: 47.91  E-value: 1.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGKAQ------TIDAVKCVMCGQCVQVC 55
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKkgtktvVIDPERCVGCGACVAVC 47
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 11-55 2.06e-07

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 49.45  E-value: 2.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  11 DAELCTGCQRCCEICPVGAIEGEPG-KAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK08348   40 DVDKCVGCRMCVTVCPAGVFVYLPEiRKVALWTGRCVFCGQCVDVC 85
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 8-55 2.73e-07

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: 47.25  E-value: 2.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI------EGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:pfam13237   2 VVIDPDKCIGCGRCTAACPAGLTrvgaivERLEGEAVRIGVWKCIGCGACVEAC 55
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 11-55 4.35e-07

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: 51.15  E-value: 4.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1592170950  11 DAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:COG2878   135 CEYGCIGCGDCIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEAC 179
Fer4_9 pfam13187
4Fe-4S dicluster domain;
15-55 5.58e-07

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 46.39  E-value: 5.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGK---AQTIDAVKCVMCGQCVQVC 55
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPDLVGqtiRGDIAGLACIGCGACVDAC 45
PRK13795 PRK13795
hypothetical protein; Provisional
 12-55 6.91e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.53  E-value: 6.91e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1592170950  12 AELCTGCQRCCEICPVGAIEGEPGKAQ-TIDAVKCVMCGQCVQVC 55
Cdd:PRK13795  580 AAECVGCGVCVGACPTGAIRIEEGKRKiSVDEEKCIHCGKCTEVC 624
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 10-55 1.54e-06

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


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 48.26  E-value: 1.54e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPVDAIVGAAKAMHTVIADECTGCDLCVEPC 155
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
13-55 1.63e-06

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 47.95  E-value: 1.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950  13 ELCTGCQRCCEICPVGAI--EGEPGKAQT-------IDAVKCVMCGQCVQVC 55
Cdd:PRK05888   58 ERCIACKLCAAICPADAItiEAAEREDGRrrttrydINFGRCIFCGFCEEAC 109
PRK06273 PRK06273
ferredoxin; Provisional
 9-59 1.77e-06

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 47.78  E-value: 1.77e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1592170950   9 SIDAELCTGCQRCCEICPVGAIEGEP------------GKAQTIDAVKCVMCGQCVQVCSAYA 59
Cdd:PRK06273   45 KVFEELCIGCGGCANVCPTKAIEMIPvepvkitegyvkTKIPKIDYEKCVYCLYCHDFCPVFA 107
PRK13984 PRK13984
putative oxidoreductase; Provisional
 11-69 4.63e-06

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 48.99  E-value: 4.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEICPVGAI-----------EGEPGKAQTIDAVKCVMCGQCVQVCSAyASCFETYQYSH 69
Cdd:PRK13984   43 DWEKCIGCGTCSKICPTDAItmvevpdlpqeYGKKPQRPVIDYGRCSFCALCVDICTT-GSLKMTREYIH 111
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
15-55 6.47e-06

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.62  E-value: 6.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGKAQtIDAVKCVMCGQCVQVC 55
Cdd:PRK07118  215 CIGCGKCVKACPAGAITMENNLAV-IDQEKCTSCGKCVEKC 254
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 13-55 6.98e-06

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 45.51  E-value: 6.98e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1592170950  13 ELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK09625   59 EICINCFNCWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVC 101
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
8-55 7.61e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 47.36  E-value: 7.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI--EGEpgkaqtIDAVKCVMCGQCVQVC 55
Cdd:COG0348   205 VRYDRGDCIDCGLCVKVCPMGIDirKGE------INQSECINCGRCIDAC 248
PRK06991 PRK06991
electron transport complex subunit RsxB;
10-55 9.44e-06

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 47.10  E-value: 9.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK06991   82 IDEQLCIGCTLCMQACPVDAIVGAPKQMHTVLADLCTGCDLCVPPC 127
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 3-55 1.24e-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: 44.94  E-value: 1.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGAIE----GEPGKAQTID----AVKCVMCGQ------CVQVC 55
Cdd:cd10554    75 QEDGVVQVDEERCIGCKLCVLACPFGAIEmaptTVPGVDWERGpravAVKCDLCAGreggpaCVEAC 141
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-55 1.32e-05

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


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 44.63  E-value: 1.32e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKaqtIDAVKCVMCGQCVQVC 55
Cdd:cd16372    72 VMINKKLCVGCLMCVGFCPEGAMFKHEDY---PEPFKCIACGICVKAC 116
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
15-55 1.49e-05

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 42.48  E-value: 1.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPG---------------KAQTIDAVKCVM------CGQCVQVC 55
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGvldarrcisyltiekKGLIPDELRCLLgnrcygCDICQDVC 62
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-55 1.58e-05

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


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 44.49  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRC-------------------------------------CE------ICPVGAIE-GEPGKAQTIDAV 43
Cdd:cd10550     1 LVVDPEKCTGCRTCelacslkhegvfnpslsrirvvrfepegldvpvvcrqCEdapcveACPVGAISrDEETGAVVVDED 80

                          90
                  ....*....|..
gi 1592170950  44 KCVMCGQCVQVC 55
Cdd:cd10550    81 KCIGCGMCVEAC 92
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 1-40 2.58e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.02  E-value: 2.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1592170950   1 MMEGKQYVsIDAELCTGCQRCCEICPVGAIEGEPGKAQTI 40
Cdd:COG1149    30 LDDGGAPV-VDPDLCTGCGACVGVCPTGAITLEEREAGKI 68
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 13-59 3.66e-05

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: 45.24  E-value: 3.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  13 ELCTGCQRCCEICPVGAIEGEPGKaqtidAV---KCVMCGQCVQVCSAYA 59
Cdd:NF038196  185 DKCIGCGICAKVCPVNNIEMEDGK-----PVwghNCTHCLACIHRCPKEA 229
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
3-37 6.67e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.87  E-value: 6.67e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGAIEGEPGKA 37
Cdd:COG2768    30 IEDGKAVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-55 7.05e-05

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


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 42.64  E-value: 7.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI--EGEPGKaqtidAVKCVMCGQCVQVC 55
Cdd:cd16370    78 VVLDKEKCIGCGNCVKACIVGAIfwDEETNK-----PIICIHCGYCARYC 122
NapF COG1145
Ferredoxin [Energy production and conversion];
1-38 7.20e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 44.33  E-value: 7.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1592170950   1 MMEGKQYVSIDAELCTGCQRCCEICPVGAIEGEPGKAQ 38
Cdd:COG1145   201 LKDGKPQIVVDPDKCIGCGACVKVCPVGAISLEPKEIE 238
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 8-59 9.77e-05

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 45.02  E-value: 9.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtidavKCVMCGQ-------CVQVCSAYA 59
Cdd:PRK12809   80 VQLDEQKCIGCKRCAIACPFGVVEMVDTIAQ-----KCDLCNQrssgtqaCIEVCPTQA 133
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 3-55 1.19e-04

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: 41.99  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950   3 EGKQYVSIDAELCTGCQ--RCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd04410    38 GGGLERAFLPVSCMHCEdpPCVKACPTGAIYKDEDGIVLIDEDKCIGCGSCVEAC 92
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 8-55 1.27e-04

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 42.63  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtidAVKCVMCGQ---------CVQVC 55
Cdd:COG0437    85 VLVDYDKCIGCRYCVAACPYGAPRFNPETGV---VEKCTFCADrldegllpaCVEAC 138
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 3-31 1.98e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 39.64  E-value: 1.98e-04
                          10        20
                  ....*....|....*....|....*....
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGAIE 31
Cdd:COG4231    41 EGDGKAVIDPDLCIGCGSCVQVCPVDAIK 69
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 18-59 2.02e-04

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: 41.46  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  18 CQRCCEICPVGAIEGEP---GKAQ-TIDAVKCVMCGQCVQVCSAYA 59
Cdd:cd10564    88 CRSCQDACPTQAIRFRPrlgGIALpELDADACTGCGACVSVCPVGA 133
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 15-55 2.21e-04

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 40.31  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1592170950  15 CTGCQRCCEICPVGAIE-GEPGKAQT-IDAVKCVMCGQCVQVC 55
Cdd:TIGR00402  36 CTRCGECASACENNILQlGQQGQPTVeFDNAECDFCGKCAEAC 78
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 2-34 2.38e-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: 39.65  E-value: 2.38e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1592170950   2 MEGKQYVSIDAELCTGCQRCCEICPVGAIEGEP 34
Cdd:COG1144    49 VDDGKYYGIDYDYCKGCGICAEVCPVKAIEMVP 81
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 1-59 2.49e-04

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: 42.67  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1592170950   1 MMEGKQYVSIDAELCTGCQRCCEICPVGAIEGEPGKAQT--------IDAVKCVMC-GQCVQVCSAYA 59
Cdd:COG2878   155 VGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTVvvsswdkgKAVRKVVGCiGLCCKKCCPAA 222
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 9-63 3.08e-04

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: 42.37  E-value: 3.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950   9 SIDAELCTGCQRCCEICPVGAIeGEPGKAQTIDAVKCVMCGQCVQVCSAYASCFE 63
Cdd:cd03110    60 FIDQEKCIRCGNCERVCKFGAI-LEFFQKLIVDESLCEGCGACVIICPRGAIYLK 113
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
11-55 3.22e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.80  E-value: 3.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1592170950  11 DAELCTGCQR--CCEICPVGAIEGEPGKAQtIDAVKCVMCGQCVQVC 55
Cdd:COG1142    48 APVQCRHCEDapCAEVCPVGAITRDDGAVV-VDEEKCIGCGLCVLAC 93
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 13-55 3.76e-04

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: 40.69  E-value: 3.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  13 ELCTGCQRCCEICPVGAIE-GEPGKAQtIDAVK--CVMCGQCVQVC 55
Cdd:cd10564    13 DLCTRCGDCVEACPEGIIVrGDGGFPE-LDFSRgeCTFCGACAEAC 57
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 15-55 3.84e-04

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


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 40.85  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1592170950  15 CTGCQR--CCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd16366    70 CMHCTDagCLAACPTGAIIRTETGTVVVDPETCIGCGYCVNAC 112
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-55 3.84e-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: 40.40  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd16372    49 CNQCGECIDVCPTGAITRDANGVVMINKKLCVGCLMCVGFC 89
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 3-31 4.71e-04

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: 38.57  E-value: 4.71e-04
                          10        20
                  ....*....|....*....|....*....
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGAIE 31
Cdd:COG1143    25 EPGKVYVIDPDKCIGCGLCVEVCPTGAIS 53
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 11-55 6.07e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 40.79  E-value: 6.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEICPVGAIEGEPGKAQT-----IDAVKCVMCGQCVQVC 55
Cdd:PRK12387   36 NPQQCIGCAACVNACPSNALTVETDLATGelaweFNLGRCIFCGRCEEVC 85
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 8-64 6.73e-04

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 39.95  E-value: 6.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtidAVKCVMCGQ---------CVQVCSAYASCFET 64
Cdd:cd16374    68 VLVDPDKCIGCGMCAMACPFGVPRFDPSLKV---AVKCDLCIDrrregklpaCVEACPTGALKFGD 130
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 13-55 6.92e-04

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 41.41  E-value: 6.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1592170950  13 ELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK00783  169 EDCDECEKCVEACPRGVLELKEGKLVVTDLLNCSLCKLCERAC 211
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 21-55 7.26e-04

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


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 39.57  E-value: 7.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1592170950  21 CCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd16374    51 CMEVCPTGAIYRDEDGAVLVDPDKCIGCGMCAMAC 85
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 21-55 7.64e-04

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: 39.94  E-value: 7.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1592170950  21 CCEICPVGAIEGEPGKAQtIDAVKCVMCGQCVQVC 55
Cdd:cd10554    64 CANVCPVGAISQEDGVVQ-VDEERCIGCKLCVLAC 97
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 8-31 8.96e-04

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


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 36.46  E-value: 8.96e-04
                          10        20
                  ....*....|....*....|....
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIE 31
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 8-150 9.85e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 41.66  E-value: 9.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGA--IEGEPGKAQTIDAV--KCVMC-----GQ-CVQVCSAYASCFETYQY-SHAQRLQER 76
Cdd:PRK12769   80 IQVNQQKCIGCKSCVVACPFGTmqIVLTPVAAGKVKATahKCDLCagrenGPaCVENCPADALQLVTEQAlSGMAKSRRL 159

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1592170950  77 RMPANVREPLFAAyyvgdlpQVKEALADHSLFTMVQCAPAVRvaiaedfgmelgslVPGKLAAALRRLGFKRIY 150
Cdd:PRK12769  160 RTARQEHQPWHAS-------TAAQEMPAMSKVEQMQATPPRG--------------EPDKLAIEARKTGFDEIY 212
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 8-33 1.59e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 36.95  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....*.
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGE 33
Cdd:COG2221    39 LVIDEEKCIGCGACIRVCPTGAIKGE 64
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
15-55 1.60e-03

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 38.75  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK08764   87 CIGCTKCIQACPVDAIVGGAKHMHTVIAPLCTGCELCVPAC 127
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 3-36 1.71e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 1.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGAIEGEPGK 36
Cdd:COG1146    30 EGKKALVINPEECIGCGACELVCPVGAITVEDDE 63
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
15-55 1.89e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.92  E-value: 1.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1592170950  15 CTGCQRCCEICPVGAIEGEPGKAQtIDAVKCVMCGQCVQVC 55
Cdd:PRK07118  141 CLGLGSCVAACPFDAIHIENGLPV-VDEDKCTGCGACVKAC 180
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 10-55 1.93e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 38.78  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950  10 IDAELC------TGCQRCCEICPVGAI---EGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:cd16373    88 IDKDRClawqggTDCGVCVEACPTEAIaivLEDDVLRPVVDEDKCVGCGLCEYVC 142
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 15-59 2.11e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 38.41  E-value: 2.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1592170950  15 CTGCQR--CCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVCSAYA 59
Cdd:cd16370    53 CRACEDppCAEACPTGALEPRKGGGVVLDKEKCIGCGNCVKACIVGA 99
PRK09898 PRK09898
ferredoxin-like protein;
12-55 2.12e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 39.43  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1592170950  12 AELCTGCQ--RCCEICPVGAI--EGEPGkAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK09898  120 ADTCRQCKepQCMNVCPIGAItwQQKEG-CITVDHKRCIGCSACTTAC 166
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 7-55 2.24e-03

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: 38.39  E-value: 2.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1592170950   7 YVSIDAELCTGCQRCCEICPVGAIegEPGKAQTIdAVKCVMCG-----QCVQVC 55
Cdd:cd10563    82 IVIHDEEKCVGCWMCVMVCPYGAI--RPDKERKV-ALKCDLCPdretpACVEAC 132
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
10-59 2.26e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 39.92  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAQTI---------DAVK------CVMCGQCVQVCSAYA 59
Cdd:PRK07118  165 VDEDKCTGCGACVKACPRNVIELIPKSARVFvacnskdkgKAVKkvcevgCIGCGKCVKACPAGA 229
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 7-59 2.66e-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: 38.06  E-value: 2.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1592170950   7 YVSIDaELCTGCQRCCEICPVGAIegepgkaQTIDAVKCVMCGQ-----CVQVCSAYA 59
Cdd:cd16367    81 EVVIS-DACCGCGNCASACPYGAI-------QMVRAVKCDLCAGyagpaCVSACPTGA 130
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 10-55 2.91e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 38.77  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1592170950  10 IDAELCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVC 55
Cdd:PRK05113  111 IDEDNCIGCTKCIQACPVDAIVGATKAMHTVISDLCTGCDLCVAPC 156
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 8-99 2.92e-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: 38.91  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPGKAQtidAVKCVMC------GQ---CVQVCSAYASCFET------YQYSHAQR 72
Cdd:cd10558    96 VDFQSDKCIGCGYCIKGCPFDIPRISKDDNK---MYKCTLCsdrvsvGLepaCVKTCPTGALHFGTkedmlaLAEKRVAA 172

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1592170950  73 LQERRMP-ANVREP-----LFAAYYVGDLPQVK 99
Cdd:cd10558   173 LKERGYTnAGLYDPkgvggTHVMYVLHHADKPE 205
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 8-62 3.42e-03

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: 38.11  E-value: 3.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPgkaQTIDAVKCVMCGQ---------CVQVCSAYASCF 62
Cdd:cd10553    84 VYVDQELCIGCKACIEACPWGIPQWNP---ATGKVVKCDYCMDridqglkpaCVTGCTTHALSF 144
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 8-59 3.98e-03

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: 38.28  E-value: 3.98e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI---EGEPGKAQTID------AVKCVMCGQ---------CVQVCSAYA 59
Cdd:cd10551    78 VLVDYDKCIGCRYCMAACPYGARyfnPEEPHEFGEVPvrpkgvVEKCTFCYHrldegllpaCVEACPTGA 147
PRK09898 PRK09898
ferredoxin-like protein;
8-55 4.14e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 38.66  E-value: 4.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAIEGEPgkaQTIDAVKCVMCGQCVQVC 55
Cdd:PRK09898  149 ITVDHKRCIGCSACTTACPWMMATVNT---ESKKSSKCVLCGECANAC 193
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
24-55 4.20e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 38.89  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1592170950  24 ICPVGAIEGEPGKAQTI----DAVKCVMCGQCVQVC 55
Cdd:COG0348   187 LCPYGAFQGLLSDLSTLrvryDRGDCIDCGLCVKVC 222
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 9-31 4.77e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 37.22  E-value: 4.77e-03
                          10        20
                  ....*....|....*....|...
gi 1592170950   9 SIDAELCTGCQRCCEICPVGAIE 31
Cdd:cd10564   113 ELDADACTGCGACVSVCPVGAIT 135
RNAP_D cd07030
D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is ...
 8-59 6.18e-03

D subunit of Archaeal RNA polymerase; The D subunit of archaeal RNA polymerase (RNAP) is involved in the assembly of RNAP subunits. RNAP is a large multi-subunit complex responsible for the synthesis of RNA. It is the principal enzyme of the transcription process, and is a final target in many regulatory pathways that control gene expression in all living cells. A single distinct RNAP complex is found in archaea, which may be responsible for the synthesis of all RNAs. The archaeal RNAP harbors homologues of all eukaryotic RNAP II subunits with two exceptions (RPB8 and RPB9). The 12 archaeal subunits are designated by letters and can be divided into three functional groups that are engaged in: (I) catalysis (A'/A", B'/B" or B); (II) assembly (L, N, D and P); and (III) auxiliary functions (F, E, H and K). The D subunit is equivalent to the RPB3 subunit of eukaryotic RNAP II. It contains two subdomains: one subdomain is similar the eukaryotic Rpb11/AC19/archaeal L subunit which is involved in dimerization, and the other is an inserted beta sheet subdomain. The assembly of the two largest archaeal RNAP subunits that provide most of the enzyme's catalytic functions depends on the presence of the archaeal D/L heterodimer.


Pssm-ID: 132908 [Multi-domain]  Cd Length: 259  Bit Score: 38.40  E-value: 6.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950   8 VSIDAElCTGCQRCCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVCSAYA 59
Cdd:cd07030   165 IEIDED-CDGCGKCVEECPRGVLELEEGKVVVEDLEDCSLCKLCERACDAGA 215
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
14-95 7.04e-03

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 37.93  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592170950  14 LCTGCQR--CCEICPVGAIEGEPGKAQTIDAVKCVMCGQCVQVCsAYASCFETYQYSHA-------QRLQERRMPANVRE 84
Cdd:PRK14993   99 LCNHCDNppCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQAC-PYDARFINHETQTAdkctfcvHRLEAGLLPACVES 177

                          90
                  ....*....|.
gi 1592170950  85 PLFAAYYVGDL 95
Cdd:PRK14993  178 CVGGARIIGDI 188
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 2-31 7.26e-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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 34.95  E-value: 7.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1592170950   2 MEGKQYVSIDAELCTGCQRCCEICPV-GAIE 31
Cdd:pfam14697  28 GDGKRHHTVIEDECTGCNLCVSVCPVdDCIT 58
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 8-30 7.56e-03

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


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 33.74  E-value: 7.56e-03
                          10        20
                  ....*....|....*....|...
gi 1592170950   8 VSIDAELCTGCQRCCEICPVGAI 30
Cdd:pfam12837   2 VEVDPDKCIGCGRCVVVCPYGAI 24
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 11-56 7.99e-03

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 37.96  E-value: 7.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1592170950  11 DAELCTGCQRCCEICPVGAIEGEPGK-AQTIDAVK---CVMCGQCVQVCS 56
Cdd:PRK09477  206 DRQKCTRCMDCFHVCPEPQVLRPPLKgKQSPSQVTsgdCITCGRCIDVCS 255
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 14-55 8.12e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 36.85  E-value: 8.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1592170950  14 LCTGCQRCCEICPVGAI-----EGEPGKAQT--IDAVK--CVMCG-QCVQVC 55
Cdd:cd16373    15 LCIRCGLCVEACPTGVIqpaglEDGLEGGRTpyLDPREgpCDLCCdACVEVC 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 2-33 8.63e-03

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 36.61  E-value: 8.63e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1592170950   2 MEGKQYVSIDAELCTGCQRCCEICPVGAIEGE 33
Cdd:cd10549    97 LEDELEIVIDKEKCIGCGICAEVCPVNAIKLV 128
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 3-29 9.39e-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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 34.42  E-value: 9.39e-03
                          10        20
                  ....*....|....*....|....*..
gi 1592170950   3 EGKQYVSIDAELCTGCQRCCEICPVGA 29
Cdd:pfam12838  25 KGTKTVVIDPERCVGCGACVAVCPTGA 51
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH