ID R8CJ46_BACCE Unreviewed; 980 AA.
AC R8CJ46;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EOO11545.1};
GN ORFNames=IGA_05407 {ECO:0000313|EMBL:EOO11545.1};
OS Bacillus cereus HuA3-9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053205 {ECO:0000313|EMBL:EOO11545.1, ECO:0000313|Proteomes:UP000014003};
RN [1] {ECO:0000313|EMBL:EOO11545.1, ECO:0000313|Proteomes:UP000014003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuA3-9 {ECO:0000313|EMBL:EOO11545.1,
RC ECO:0000313|Proteomes:UP000014003};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus HuA3-9.";
RL Submitted (DEC-2012) 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:EOO11545.1}.
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DR EMBL; AHDZ01000069; EOO11545.1; -; Genomic_DNA.
DR RefSeq; WP_016097198.1; NZ_KB976151.1.
DR AlphaFoldDB; R8CJ46; -.
DR PATRIC; fig|1053205.3.peg.5470; -.
DR HOGENOM; CLU_000422_4_0_9; -.
DR Proteomes; UP000014003; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 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; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..120
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 142..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 261..317
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 941..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 109415 MW; 1ECE888E3074B9B2 CRC64;
MTEQTVRVTV DGKEFFVSGE KTILQLFNES NLEHPQICHV PEVDPIQTCD TCIVEVNGSL
LRACSTKLED GMHIERQSER AKEAQTEAMD RILENHLLYC TVCDNNNGNC KVHNTVHMME
IEEQKYPYEP KVSACEVDTS HPFYRYDPNQ CIACGQCVEV CQNLQVNETL SIDWSLDRPR
VIWDNGVSIN ESSCVSCGQC VTVCPCNALM EKTMLGEAGF MTGLKPDVLN PMIDFVKDVE
PGYSSILAVS EVESAMRKTK INKTKTVCTF CGVGCSFEVW TKDRQILKVQ PVSDAPVNGI
STCVKGKFGW DFVNSEERIT KPLIRQGDMF VEASWEEALE VVASNMQHIK SEYGSDAFGF
ISSSKVTNEE NYLMQKLARQ IYGTNNVDNC SRYCQSPATD GLFKTVGMGG DAGTVKDIAE
AGLVIIVGAN PTEGHPVLAT RVKRAHKLHE QKLIVADLRK HEMAERADIF VHPSQGTDYV
WLAGITKYII DQEWHDKKFI AENVKNFDEY SKMLEKYTLD YTEKITGISK AQLKEMARMV
YEADGTCVLW GMGVTQNTGG STTSAAISNL LLVTGNYRRP GAGAYPLRGH NNVQGACDMA
TLPNWLPGYQ AVSDDVHRAK FEKAYGTTIP KEPGLNNIAM LLAAEEGKLR GMYVMGEEMA
LVDSNANHVQ HILANLDFLV VQDMFLSKTA RFADVILPAA PSLEKEGTFT NTERRIQRLY
EVLKPLGDSK PDWWILQKVA RALGGDWNYG SPSEIMDEIA SLAPLYSQAT YDRLEGWNSL
CWGSHDGSDT PLLYVDGFNF PDKLARLSLD EWVPPVVAPD EYDLLLNNGR MLEHFHEGNM
TNKSAGILSK VSEVFVEISP ELAKERNVKD GGLVELASPF GKIKVQALVT DRVTGNELYL
PMHATVNEEA INILTGTATD IYTCTPAYKQ TMVKLRVLRE KGNRPLPSSN PRDKKRHPQN
GVEIERKWQR KQYVSLVDQN
//
