ID A3V0U8_9RHOB Unreviewed; 921 AA.
AC A3V0U8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SKA53_10449 {ECO:0000313|EMBL:EAQ08138.1};
OS Yoonia vestfoldensis SKA53.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ08138.1, ECO:0000313|Proteomes:UP000004507};
RN [1] {ECO:0000313|EMBL:EAQ08138.1, ECO:0000313|Proteomes:UP000004507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ08138.1,
RC ECO:0000313|Proteomes:UP000004507};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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=[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:EAQ08138.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMS01000001; EAQ08138.1; -; Genomic_DNA.
DR RefSeq; WP_007206039.1; NZ_CH672414.1.
DR AlphaFoldDB; A3V0U8; -.
DR STRING; 314232.SKA53_10449; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000004507; 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; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 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; 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; 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 PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000004507};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 141..171
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 180..213
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 226..281
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 921 AA; 99557 MW; FC331DEAD66D42FA CRC64;
MSDQITFTLD GVTVTAVPGQ TIWEVANGRG LVIPHLCHKP APGYRSDGNC RACMVAIEGE
RTLAASCIRE PRDGMVVTTD GPREVQARRM VMELLVADQP AQDVAHDRSS HLWDMAGAQG
VAVSRFPAKA EHIPLLDDSH VAMSVNLDAC IQCGLCVRAC REVQVNDVIG MAGRGGTAYP
VFDMDDPMGG SSCVACGECV QACPTGALLP ATVTDENQQG DTADYDREVA SVCPFCGVGC
QVSLKIKDNR VKFVEGINGP ANEGRLCVKG RFGFDYIHHP HRLTKPLIRR ADAPAKGLNV
DPGNWQKHFR EATWDEALDA AAGGLRAIGG TGVAGFGSAK CTNEEAYLFQ KLIRQGFGHN
NVDHCTRLCH ASSVAALMEN VGSGAVTATF NQIEHSDVAI VIGANPIENH PVAATYFKQF
AKRGGKLIVM DPRGQALKRH ASHMLQFRPG ADVSMLNAIM HVIVEEQLYD RQYIAAYTEN
WEAEKAHLAD FSPEKMAGIC GIDAETLRDV ARTFAGAKAA MIFWGMGVSQ HIHGTDNARC
LISLALMTGQ VGRPGAGLHP LRGQNNVQGA SDAGMIPMFL PDYQPVGDQG VRTAFQEVWQ
HGEIDATKGL TVTEILDAVH DGDIHGMYIL GENPAMSDPD VDHARAALAK LSHLVVQDIF
ITETANFADV ILPASAFAEK TGTVTNTNRQ VQMGRPAVPP PGDAREDWWI TVELAKRLGL
PWTYAHPSEV FGEMTQVMAS LNNITWDRLE AQSAVTYPSL TPDDPGQPIV FADGFPRENG
RAKFTPASVI APDETPDADY PMIMTTGRQL EHWHTGSMTR RSRVLDAVEP EANCSLHPST
LRRLGVEPGG MVRLTTRRGS IDIMARSDRA VAPDMVFVPF AYVEAAANIL TNPAIDPYGK
IPEFKFAAVR VEKAQSEVAA E
//
