ID A0A254QSZ5_9RHOB Unreviewed; 920 AA.
AC A0A254QSZ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=ATO1_06855 {ECO:0000313|EMBL:OWU80848.1};
OS Phaeobacter sp. 22II1-1F12B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU80848.1, ECO:0000313|Proteomes:UP000197279};
RN [1] {ECO:0000313|EMBL:OWU80848.1, ECO:0000313|Proteomes:UP000197279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU80848.1,
RC ECO:0000313|Proteomes:UP000197279};
RA Lai Q., Li G., Shao Z.;
RT "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL Submitted (APR-2013) 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:OWU80848.1}.
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DR EMBL; AQQP01000004; OWU80848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QSZ5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000197279; 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; SSF50692; ADC-like; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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:UP000197279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 3..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 142..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 227..282
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 920 AA; 100355 MW; 8416E7FD5287E4D0 CRC64;
MSDKVRFTLD GQEIEAEQGL TIWEIANGRG LVIPHLCHKP APGYRPDGNC RACMVEIEGE
RTLAASCIRE PSEGMVVTTD SARAASARKM VVEMLVADQP KREVAHDRSA HLWDMAEANG
VSESRFPKLE KERIPLLDDS HVAMRVNLDA CIQCGLCVRA CREVQVNDVI GMSGRGHDAF
PTFDMADPMG ASTCVACGEC VQACPTGALM EATVLDADQQ GDSADYDSEV ASVCPFCGVG
CQVSLKVKDG RVKYVDGIDG PANEGRLCVK GRFGFDYIHH DHRLTKPLIR REDAPAKGLN
VDPANWQTHF REASWDEALD VAANGLRGRG REVAGFGSAK CTNEEAYLFQ KIIRQGFGHN
NVDHCTRLCH ASSVAALMEN VGSGAVTATF NEIENADVAI VIGANPIENH PVAATYFKQF
TKRGGKLIVM DPRGQALKRF ASHMLQFRPG ADVSMLNAIM HVIVEEGLYD RQYIEAYTEN
WEAEKDHLSG FTPEKMSEIC GIEPEVLRDV ARTFAGARAG MIFWGMGVSQ HIHGTDNSRC
LISLALMTGQ VGRPGTGLHP LRGQNNVQGA SDAGMIPMFM PDYKDVTDDG VRSAFTEVWG
TGDFSNEKGL TVTEIMDAVH AGDINAMYIL GENPAMSDPD VDHARAALAK LDHLVVQDIF
ITETANYADV ILPASAFAEK TGTVTNTNRQ VQMGRAAVSP PGEAREDWWI EVELAKRLGL
GWTYTSPAEV FAEMKLNMES LDNITWERLE RENAVTYPSL SPEDPGQAIV FGDGFPRAGR
RAKFTPANVI APDEAPDAEY PMILTTGRQL EHWHTGSMTR RASVLDAVEP EANCSLHPKT
LRRLGVAPGG MLRLTTRRGS IEVMARADRA VSEDMVFLPF AYVEAAANIL TNPAIDPYGK
IPEFKFSAVK VEPAEAMAAE
//
