ID A0A0M8YHL4_9PSEU Unreviewed; 933 AA.
AC A0A0M8YHL4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=ADK67_15985 {ECO:0000313|EMBL:KOX26547.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX26547.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX26547.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX26547.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
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:KOX26547.1}.
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DR EMBL; LGED01000158; KOX26547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8YHL4; -.
DR STRING; 1415542.ADK67_15985; -.
DR PATRIC; fig|1415542.3.peg.3487; -.
DR Proteomes; UP000037722; 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:UniProtKB-EC.
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; cd00508; MopB_CT_Fdh-Nap-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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00932; MOLYBDOPTERIN_PROK_3; 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}.
FT DOMAIN 15..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 93..132
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 155..186
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 198..226
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 233..289
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 933 AA; 100165 MW; 040923DC8FCC8792 CRC64;
MKEPDFGTPA STSSTSVTVE VDGIPVTVPA GTSVMRAAAT SGIDIPKLCA TDSLEAFGSC
RLCLVEIDGR RGTPASCTTP VADGMRVRTQ TPKLEKLRQG VMELYISDHP LDCLTCSANG
DCELQDMSGA VGLRQVRYGY EGENHLSLEK DTSNPYFDFE PSKCISCSRC VRACGEVQGT
FALTIQGRGF ESQVSAAGVP LMESDCVSCG ACVQACPTAT LQEKSVVQLG MPSRTVLTTC
AYCGVGCSFK AELRGDELVR MVPYKDGGAN EGHSCVKGRF AFGYATHPDR VMSPMVREKI
TDPWREVSWE EAIGYTASRM REIQAAHGVG AIGGITSSRC TNEEVYVVQK LVRAAFGNNN
VDTCARVCHS PTGYGLKQTF GESAGTQDFR SVAAADVIVV IGANPTDGHP VFASRMKRRL
REGASLVVVD PRRIDLVRSP HVEATHHLQL QPGTNVAVVN AFAHVVVTEG LVDSDFVASR
CEGYEEWAEF IARPENSPEV VESITGVPAA EIRAAARLYA TGGNAAIYYG LGVTEHSQGS
TMVMGMANLA MATGNVGRDG VGVNPLRGQN NVQGSCDMGS FPHELPGYRH VSDDAVRTVF
EQVWGRSILP TPGLRIPNMF DSAIAGTFRG LFVQGEDIAQ SDPNLAHVTA ALTAMDLVVV
QDLFLNETSK FAHVFLPGTS FLEKDGTFTN AERRINRVRP VMAPKTGKHE WQIVCELAAA
LGYDMPYTHP REIMDEIAAL TPTFAGVSFA ALDRLGSIQW PCDEDAPAGT PTMHVDSFTR
GKGRFVPTSF VPTSERTTRK FPLILTTGRI LSQYNVGAQT RRTANIAWHP EDVLEIHPHD
AEVRGIGDGD SVTLASRVGA TSLHAVISDR MPVGVVYTTF HHPVTGANVV TTENSDWATN
CPEYKVTAVQ VALRADAAEA AAVPGTRERA VVD
//
