ID A0A126V298_9RHOB Unreviewed; 1000 AA.
AC A0A126V298;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:AML52016.1};
GN ORFNames=RC74_12710 {ECO:0000313|EMBL:AML52016.1};
OS Falsihalocynthiibacter arcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsihalocynthiibacter.
OX NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML52016.1, ECO:0000313|Proteomes:UP000070371};
RN [1] {ECO:0000313|EMBL:AML52016.1, ECO:0000313|Proteomes:UP000070371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML52016.1};
RA Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT arctic marine sediment.";
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014327; AML52016.1; -; Genomic_DNA.
DR RefSeq; WP_039003915.1; NZ_CP014327.1.
DR AlphaFoldDB; A0A126V298; -.
DR STRING; 1579316.RC74_12710; -.
DR KEGG; hat:RC74_12710; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000070371; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000070371};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 65..121
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 736..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1000 AA; 110712 MW; 96AB1BA9900E648E CRC64;
MLRRKTNGIA RGSARPAVAQ AKSTSVDRRS FLRGSGLVIG GLAAVAATGG TVSKATAQTA
LDRTVEIKKS ICTHCSVGCT VIAEVDNGVW TGQEPGFDSP FNLGAHCAKG AAVREHAHGE
RRLKYPMKKE NGEWVKISWE TAINEIGDGM MKIREESGPD SVYWLGSAKH SNEQAYLFRK
FAAYWGTNNV DHQARICHST TVAGVANTWG YGAMTNSYND IHNSKAIFLI GANPAEAHPV
SLLHLLKAKE ENNAPLIVCD PRFTRTAAHA DEYVRFRPGS DVALVWGILW HIFENKWEDT
EFIRTRVWGM DQIRDEVKQW NPEEVERVTG APGEQLERVA RTLANNRPGT VIWCMGGTQH
SNGNNNTRAY CILQLALGNM GVAGGGTNIF RGHDNVQGAT DLGVLADTLP GYYGLSDGSW
AHWARVWDED LDWLKGQFSD ASFGDTKMMN LTGIPVSRWI DGVLEDKANL DQPDNTRAMV
LWGHAPNSQT RMKEMKTAME RLEMLVVIDP YPTVSAVMQD RTDGVYLLPA ATQFETRGSV
TASNRSLQWR EQVMDPLFES LPDHTILAKF AEKFGFHERM FRNIAIDEGG EPNVEDLTRE
FNRGMWTVGY TGQSPERLKM HMENQHTFDR TTLRAIGGPA DGDFYGLPWP CWGTPEMNHP
GTAILYDMSI PVAEGGLTFR ARFGVEREGD NLLAEGVYSK GSEIKDGYPE FTVQMLRDLG
WENDLTDVEK ASINGVAGYP EGAPLTAEPA DDGGSNNTEE VGETSQQGDI PSDFLAKTGG
VNWKTDLSGG IQRVAIAHGC APFGNAKARA VVWTFPDPVP LHREPLYTNR RDLVVDYPTY
EDKKFWRVPT MYRSIQENDF SQEYPIILTS GRLVEYEGGG DETRSNPWLA ELQQDMFVEI
NIRDANDLGV RDGAQVWVEG PEGGKVKVMA MVTERVGSGV AFMPFHFGGH FEGKDLRDKY
PEGADPYVLG ESTNTAQTYG YDSVTQMQET KATLCKIWSA
//
