ID R0BU82_9FIRM Unreviewed; 905 AA.
AC R0BU82;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:ENZ47797.1};
GN ORFNames=HMPREF1085_03968 {ECO:0000313|EMBL:ENZ47797.1};
OS Enterocloster bolteae 90A9.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=997894 {ECO:0000313|EMBL:ENZ47797.1, ECO:0000313|Proteomes:UP000013126};
RN [1] {ECO:0000313|EMBL:ENZ47797.1, ECO:0000313|Proteomes:UP000013126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90A9 {ECO:0000313|EMBL:ENZ47797.1,
RC ECO:0000313|Proteomes:UP000013126};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Courvalin P., Lambert T.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium bolteae 90A9.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENZ47797.1}.
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DR EMBL; AGYH01000013; ENZ47797.1; -; Genomic_DNA.
DR RefSeq; WP_002576877.1; NZ_KB851182.1.
DR AlphaFoldDB; R0BU82; -.
DR PATRIC; fig|997894.4.peg.4158; -.
DR HOGENOM; CLU_000422_4_0_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000013126; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 9..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 89..128
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 149..182
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 192..221
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 229..284
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 905 AA; 100006 MW; 3A03055C87346D4D CRC64;
MSHHIDPDTR IHIEIDHIPC EVAPETTILS AAAGLGIQIP TLCYMKELAP DGSCRMCVVE
VDGGRKKGLV TACSEHCTEG MVISTRSEKV MEARRFVLDL LMSNHREHCF SCPQNGSCKL
QDYCMEYGVE YTSYDSGKRV NAPKDTSSPF FEYNPELCIM CRRCVRICEE LQCRNVISLK
DRSFDTIITT AYGRPWSETT CESCGNCVSH CPTGALSAKD HKKYRSWEVR KVRTTCPHCA
TGCQMDLLVK DNRIVGAEPA DGPSNHNLLC VKGKFGSYKF VGSGDRLTHP LIRRNGQLEQ
ASWDEALDYM AEQFREIQKK YGNDAIAGFS CSRAPNEDNF VFQKMMRAAF RTNNVDNCAR
ICHSASVTGL AMTLGSGAMT NPIADITGDV DVILLVGSNP TEAHPVAGTQ IRRAVRRGTK
LIVVDPRKID LTNDAALHLQ IKPGTNVAFA NGMMHIILKE GLADMDFISS RTEGFEILEQ
ILEDYPPEKV AQICHIRQED LIQAARMYAG ARKAPIIYCL GVTEHSTGTE GVMSLSNLAM
MTGKLGRPGC GINPLRGQNN VQGACDMGCL PTDFPGYQKV ANPDVIHKFQ TAWSVELNTR
PGLTSTEVFP AAIKGSIKGL YIFGEDPIVT DPDTGHIEKA LKNLDFLVVQ ELFMTETAAY
ADVVLPGVSY AEKEGTFTNT ERRLQRVRKA VEPAGLARDD IQIFCDVMGR MGYPCHYDSA
AQVMDEIACV TPSYGGISHA RLDSGESLQW PCPSKDHPGT PILHAGRFSR GLGYFYPAVY
KESRELPDEE YPILLTTGRM LYHYNTRAMT KRTEGLNEIC SESYIEVNEE DAKALGISHG
DKVLVSSRRG RITSTARVGQ KVSPHEAFMT FHFADGNVNR ITNAALDDLA RIPEYKACAI
RIQKA
//