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Database: UniProt
Entry: R0BU82_9FIRM
LinkDB: R0BU82_9FIRM
Original site: R0BU82_9FIRM 
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
//
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