ID C6Q013_9CLOT Unreviewed; 560 AA.
AC C6Q013;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EET85154.1};
GN ORFNames=CcarbDRAFT_4380 {ECO:0000313|EMBL:EET85154.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET85154.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET85154.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET85154.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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:EET85154.1}.
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DR EMBL; ACVI01000105; EET85154.1; -; Genomic_DNA.
DR AlphaFoldDB; C6Q013; -.
DR SMR; C6Q013; -.
DR STRING; 536227.Ccar_16080; -.
DR KEGG; cck:Ccar_16080; -.
DR PATRIC; fig|536227.13.peg.3370; -.
DR eggNOG; COG3383; Bacteria.
DR Proteomes; UP000004198; Unassembled WGS sequence.
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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198}.
FT DOMAIN 1..331
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 418..525
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 560 AA; 62934 MW; C14CE7E8210EB9A7 CRC64;
MSNGIHEIDD CDLVFIFGYN GADSHPIVAR RIVNAKRKGA KIVVTDPRIT ESARIADLWL
PIKNGTNMIL VNAFANVLIN EGLYNKQYVE EHTVGFEEYK ALVEKYTPEY AEKMTGVPAE
DIRKSMRMYS KAKNAMILYG MGVCQFGQAV DVVKGLASLA LLTGNFGRPN VGIGPVRGQN
NVQGACDMGA LPNVYPGYQS VTNDAIREKF ENAWGVKLPN KVGYHLTEVP HLVLKEDKIK
AYYIMGEDPV QSDPDAAEVR EALDKLELVI VQDIFMNKTA LHADVILPAT SWGEHEGVYS
SADRGFQRFR KAIEPTGDVK PDWQIISEIA KAMGYDMNYK NTKEIWDELR NLCPNFKGAS
YERLEELGGI QWPCPSEDHP GTSYLYKGNK FNTPSGKANL FAAEWRAPME STDKEYPLVL
STVREVGHYS VRTMTGNCRA LQQLADEPGY VQINPEDAKN LNILDQEFVR ISSRRGSVVA
KALVTDRVNK GAVYMTYQWW VGACNELTLN NLDPISKTPE YKYCAVKVEN IKDQKAAEQY
VQDEYTKIRK KMNINLECCK
//
