ID Q2RGF7_MOOTA Unreviewed; 746 AA.
AC Q2RGF7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 3.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Formate dehydrogenase, alpha subunit (F420) {ECO:0000313|EMBL:ABC20482.2};
DE EC=1.2.99.- {ECO:0000313|EMBL:ABC20482.2};
GN Name=fdhA {ECO:0000313|EMBL:ABC20482.2};
GN OrderedLocusNames=Moth_2193 {ECO:0000313|EMBL:ABC20482.2};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC20482.2};
RN [1] {ECO:0000313|EMBL:ABC20482.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC20482.2};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000232; ABC20482.2; -; Genomic_DNA.
DR STRING; 264732.Moth_2193; -.
DR KEGG; mta:Moth_2193; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_9; -.
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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 4: Predicted;
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 Oxidoreductase {ECO:0000313|EMBL:ABC20482.2};
KW Selenium {ECO:0000313|EMBL:ABC20482.2};
KW Selenocysteine {ECO:0000313|EMBL:ABC20482.2}.
FT DOMAIN 6..62
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT NON_STD 139
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:ABC20482.2"
SQ SEQUENCE 746 AA; 82693 MW; 01580D38FB86EF78 CRC64;
MKKVEPEQVL TVCPYCGTGC GLNLTVQDGK ITGVAPDRLH PVSEGELCVK GYYGYQYVQD
SRRLTAPLIK KDGGFVAVSW DEALEYVVSR LKKIKEESGP DAFALFTSAR ATNEDNYAAQ
KFTRAVMGTN NIDHCARLUH APTVAGLAMT LGSGAMTNSI AEISTYSDVI FIIGSNTAEC
HPLVARHVLK AKERGAKLIV ADPRLTEMAN KADIWLRVPV GYNIPLINGM LHLIIKEGLV
KKDFIQKHAE GLDELVRAVE QYTPAYVEEL TGIPQRDLIE AARLYGRAQA AMILYCMGVT
QFSHGTGNVV SLSNLAVVTG NLGRPGTGVC PLRGQNNVQG ACDMGGLPDV LPGYLNVTRE
EWRRRFEKEW KVKLPSKPGI RIPEVPEAIL EGKIRALYIF GENPIMSDPD SDHLRHALEH
LDLLVVQDIF LTETARLADV VLPAASWAEK DGTFTNTERR VQRVRKAVDL PGEARPDWQI
FGMLAQKMGY MGLNYSNSQE IWDEVRRLVP EKFGGISYAR LESVRGITWP CPQEEHPGTP
ILYEGGKFLT PSGKARLYPV IFYAKASNGA SKEKAKAGNQ VIVGTIAELP DEEYPFILTN
GRRVYHYHTG TMTRKSWLLD QIGPNELVEI NPQDARKMGI NDGDFVKVST RRGYVAVRAW
VTERVPEGTI FMTFHYWEAC CNELTNTAND AICSTPEFKL AAARMDKISP EEARAIYLEK
KAKYLVDLEK ANVPKTVIGE GGRVDA
//
