ID I1YI72_METFJ Unreviewed; 956 AA.
AC I1YI72;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=Q7C_1466 {ECO:0000313|EMBL:AFJ02615.1};
OS Methylophaga frappieri (strain ATCC BAA-2434 / DSM 25690 / JAM7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754477 {ECO:0000313|EMBL:AFJ02615.1, ECO:0000313|Proteomes:UP000009145};
RN [1] {ECO:0000313|EMBL:AFJ02615.1, ECO:0000313|Proteomes:UP000009145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM7 {ECO:0000313|EMBL:AFJ02615.1,
RC ECO:0000313|Proteomes:UP000009145};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003380; AFJ02615.1; -; Genomic_DNA.
DR RefSeq; WP_014704035.1; NC_017856.1.
DR AlphaFoldDB; I1YI72; -.
DR STRING; 754477.Q7C_1466; -.
DR KEGG; mec:Q7C_1466; -.
DR PATRIC; fig|754477.3.peg.1446; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000009145; Chromosome.
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:UP000009145}.
FT DOMAIN 21..99
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 161..192
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 205..233
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 240..296
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 956 AA; 104939 MW; 5946B79FFE4A9116 CRC64;
MRVETYNPNK DYGTPPSLSE ELITVEIDGV EITVPEGTSV MRAAALADIN IPKLCATDNL
ESFGSCRLCA VQIEGKRGYP ASCTTTVEAG MKVTTQNQKL GKLRRNIMEL YISDHPLDCL
TCPANGNCEL QDMAGAVGLR DVRYGYAGEN HLESAKDLSN PYFDFDPSKC IVCSRCVRAC
EEVQGTFALT IDGRGFASVV SPSQHEDFMD SECVSCGACV QACPTSTLME KSVVEMGQPE
HSVVTTCAYC GVGCSFKAEM KGNEVVRMVP YKGGDANHGH SCVKGRFAFG YATHQDRIKS
PMIRDAITDA WREVSWEDAI AFAADKLKQI QQKYGRNSIG GITSSRCTNE ETYLVQKLVR
AAFGNNNTDT CARVCHSPTG YGLKATMGES AGTQNFDSVM KADVVLVIGA NPTDAHPVFG
SMMRRRLREG AELIVADPRH IDLLDTPHLK SGQHLPLRPG TNVALVNALA HVVVTEGLED
MAFVEKRCDM ESYHSWRDFI QDPRHSPEAV EAITGVAAEK LRIAARTYAN APNAAIYYGL
GVTEHSQGST MVMGIANLAM ATGNIGREGV GVNPLRGQNN VQGSCDMGSF PHELPGYQHV
SNDESRQRFE SVWGVSIDNE PGLRIPNMFD AAISGEFKAL YVQGEDIAQS DPGTQHVESA
LKSLECLIVQ DLFLNETAKF AHVLLPGSSF LEKDGTFTNA ERRINRVRKV MPALAGKEDW
QVTMDLSNAL GYPMHYNHPS EIMDEIAALT PTFTGVNYKR LDELGSIQWP CNDDHPIGTP
TMHEVDFPIG KGQFSVTEYV ATDERTNSRF PLLLTTGRIL SQYNVGAQTR RTQNQMWHDE
DRLDLHPHDA EVRGIKENDW VGITSRAGQT VLRARISEDV LPGVVYTTFH HPGSGANVIT
TDNSDWATNC PEYKVTAVQV ERVSQPSEWQ RNFKAFESMQ LGLLEAAKED SVTGRN
//
