ID A0A0X3TWC0_9RHOB Unreviewed; 964 AA.
AC A0A0X3TWC0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KUJ79995.1};
GN ORFNames=AVO44_07440 {ECO:0000313|EMBL:KUJ79995.1};
OS Ruegeria profundi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ79995.1, ECO:0000313|Proteomes:UP000053690};
RN [1] {ECO:0000313|Proteomes:UP000053690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA Zhang G., Stingl U.;
RL Submitted (DEC-2015) 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:KUJ79995.1}.
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DR EMBL; LQBP01000003; KUJ79995.1; -; Genomic_DNA.
DR RefSeq; WP_068334768.1; NZ_LQBP01000003.1.
DR AlphaFoldDB; A0A0X3TWC0; -.
DR STRING; 1685378.AVO44_07440; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000053690; 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; 2.
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 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 964 AA; 106799 MW; 4611271587BBE4CE CRC64;
MLRKKTNGVA RRPQRTSILS QIGEKTVDRR AFLRGSGLTI GGLAAISATG GTVTQANAAA
TATGAVNLVK SVCTHCSVGC TVVAEVSNGV WIGQEPGWDS PFNLGAHCAK GASVREHAHG
ERRLKYPMKK EGGEWKRISW EEAINEIGDG MMNIRQESGP DSVYWLGSAK HNNEQAYLFR
KFAAYWGTNN VDHQARICHS TTVAGVANTW GYGAMTNSYN DIHNSKAIFI IGGNPAEAHP
VSLLHVLRAK EQNNAPLIVC DPRFTRTAAH ADEYVRFRPG TDVALIWGML WHIFDNGWED
KEFIRTRVWG MDQIREEVAN WTPEETERVT GVPGSQLKRV ARTLVNNRPG TVIWCMGGTQ
HTNGNNNTRA YCVLQLALGN MGTSGGGTNI FRGHDNVQGA TDLGVLSHTL PGYYGLSKGA
WAHWARVWGE DPEWLAGQFA SIKDKDGKDK PLQNERGIPV SRWIDGVLED PANMDQDNNV
RAMVLWGHAP NSQTRGPEMK TAMEKLDMLV VIDPYPTVSA VLHDRTDGVY LLPACTQFET
RGSVTASNRS LQWRDKVVDP LFESLPDEVI MAKFANKFGW ADRLFRNIEM EDPETPNVES
ITREFNRGLW TIGYTGQSPE RLKSHMANQH TFDRTTLQAV GGPNDGEYYG LPWPCWGTPE
MGHTGTPNLY DMSKPVAEGG LTFRARFGVE RDGDNLLAEG VYSVGSEIQD GYPEFTMQML
MDLGWDGDLT DEERAAIDAV AGPETNWKTD LSGGIQRVAI KHGCAPFGNA KARAVVWTFP
DPIPLHREPL YTNRRDLVED YPTYEDRQAY RLPTLYASIQ KNDFSKDYPI ILTSGRLVEY
EGGGDETRSN PWLAELQQDM FVEINPRDAN NLGIRDGSQV WVEGPEGGKV KVMAMLTNRV
GAGVAFMPFH FGGHFQGEDL RAKYPKGADP YVLGESTNTA QTYGYDSVTQ MQETKATLCK
IWAA
//
