ID A0A1G6XD90_9BURK Unreviewed; 954 AA.
AC A0A1G6XD90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN05444679_113131 {ECO:0000313|EMBL:SDD76041.1};
OS Variovorax sp. CF079.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882774 {ECO:0000313|EMBL:SDD76041.1, ECO:0000313|Proteomes:UP000198763};
RN [1] {ECO:0000313|EMBL:SDD76041.1, ECO:0000313|Proteomes:UP000198763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF079 {ECO:0000313|EMBL:SDD76041.1,
RC ECO:0000313|Proteomes:UP000198763};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FMZU01000013; SDD76041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6XD90; -.
DR STRING; 1882774.SAMN05444679_113131; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000198763; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198763}.
FT DOMAIN 19..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 97..136
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 159..190
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 202..231
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 238..294
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 954 AA; 104216 MW; 37AA493EBEDECD23 CRC64;
MLDHLKETDY GTPRRESERE VTLEIDGYEV TVPAGTSLMR AAVDAGIQVP KLCATDSLEP
FGSCRLCLVE IDGRKGFPAS CTTPAEAGMK VRTQTPKLQE LRKGVMELYI SDHPLDCLTC
SANGNCELQD MAGVTGLRNV RYGFDGANHL KSAKDESNPY FTYDPSKCIV CNRCVRACEE
TQGTFALTIS GRGFESRVSP GQDQAFMESE CVSCGACVEA CPTATLQEKS VIWLGQAEHS
VITTCAYCGV GCAFKAEMKG SEVVRMVPWK DGKANEGHSC VKGRFAWGYA THQDRMLKPM
IRAKISDPWQ EVSWEVALNH AASEFKRLQA KYGKDSIGGI TSSRCTNEET YLVQKLVRAA
FGNNNVDTCA RVCHSPTGYG LKQTLGESAG TQTFKSVEKA DVVMVIGANP TDGHPVFASR
MKRRLREGAK LIVVDPRRID IVKSPHVKAA HHLQLKPGTN VAVVTALAHV IVTEGLAAED
FIAERCDTAS FNEWKAFVAR PEQSPEATEE ATGVPAAQLR AAARLFATAG NGAIYYGLGV
TEHSQGSTTV MGIANLAMVT GNVGREGVGV NPLRGQNNVQ GACDMGSFPH ELPGYRHVSD
STTRASFEAA WGVPINPEPG LRIPNMFDAA LGGAFKGLYC EGEDIVQSDP NTQHVAAAMM
AMECVVVQDM FLNETAKYAH VFLPGSSFLE KDGTFTNAER RISRVRKVMP PKAGYADWEI
TVKLAQALGY PMDYKSPEDV MAEIAALTPT FRGVSYKRLD ELGSIQWPCN DAAPEGTPTM
HIDSFVRGKG RFIVTQYVAT DEKVTRKFPL LLTTGRILSQ YNVGAQTRRT DNNQWHSEDR
LEIHPHDAEE RGIKDDDWVG IQSRAGETVL RATVSERMQP GVVYTTFHFP ESGANVITTD
NSDWATNCPE YKVTAVQVMP VMQPSAWQQE YSRFNEVQQG LLTAAQANET VPAK
//
