ID A0A1X4NHG2_9RHOB Unreviewed; 962 AA.
AC A0A1X4NHG2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:OSQ46807.1};
GN ORFNames=MGEO_17055 {ECO:0000313|EMBL:OSQ46807.1};
OS Marivita geojedonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Marivita.
OX NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ46807.1, ECO:0000313|Proteomes:UP000193926};
RN [1] {ECO:0000313|EMBL:OSQ46807.1, ECO:0000313|Proteomes:UP000193926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ46807.1,
RC ECO:0000313|Proteomes:UP000193926};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:OSQ46807.1}.
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DR EMBL; JFKC01000022; OSQ46807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NHG2; -.
DR STRING; 1123756.MGEO_17055; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000193926; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 3.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000193926};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 66..122
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 962 AA; 106685 MW; 5FB6868326CDF763 CRC64;
MLRKKTGGLT RRTARTGLIS EISNKSVDRR SFLRGSGLAI GGLAAISATG GAVTQASAQS
AVNGAVQTVK SVCTHCSVGC TVVAEVSNGV WIGQEPGWDS PFNLGAHCAK GAAVREHAHG
ERRLKYPMKK EGGEWKRISW EQAINEIGDK MLQVRDESGP DSVYWLGSAK HNNEQAYLLR
KFAAYWGTNN IDHQARICHS TTVAGVANTW GYGAMTNSYN DIHNSRAIFL IGGNPAEAHP
VSLLHILKAK EQNNAPVIVC DPRFTRTAAH ADEYVRFRPG TDVALVWGIL WHIFENGWED
KEFIRTRVWG MDQIKEEVAK WNPEEVERVT GTPGSQLERV ARTLANNRPG TVIWCMGGTQ
HTNGNNNTRA YCVLQLALGN MGTSGGGTNI FRGHDNVQGA TDLGVLADTL PGYYGLSAGS
WAHWARVWEE DLDWLKGQFS QEMVGETAMM NLTGIPVSRW IDGVLEDKEN LDQPDNTRVM
VLWGHAPNSQ TRLPEMKTAM EKLDTLVVID PFPTVSAVLH DRTDGVYLLP ATTQFETYGS
VTASNRSLQW REKVMEPLFE SKTDHEIMGL FAQKFGFHDR IFRNIKIEDD GVTPNIEDIT
REFNRGMWTI GYTGQSPERM RLHMENQHTF DRTTLRANGG PADGDFYGMP WPCWGTPEMK
HPGTANLYDM SLPVSKGGLT FRARFGVERD GDNLLAEGVA SANSEIQDGY PEFTMQMLMD
LGWDGDLTAE ERAAIDAVAG PNTNWKTDLS GGIQRVAIKH ECAPFGNAKA RAVVWTFPDP
VPLHREPLYT SRYDLVADYP TYEDKKFWRV PTMYKSIQST DFSSDYPIIL TSGRLVEYEG
GGDETRSNPW LAELQQDMFI EINPRDANDL GVRDGSQVWV EGPEGGKVKV MAMLTERVAP
GVAFMPFHFG GHFQGEDLRG KYPEGADPYV LGESTNTAQT YGYDSVTQMQ ETKATLCKIM
AA
//
