ID A0A1W2ALM6_9RHOB Unreviewed; 1015 AA.
AC A0A1W2ALM6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:SMC61514.1};
GN ORFNames=SAMN06295998_103101 {ECO:0000313|EMBL:SMC61514.1};
OS Primorskyibacter flagellatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Primorskyibacter.
OX NCBI_TaxID=1387277 {ECO:0000313|EMBL:SMC61514.1, ECO:0000313|Proteomes:UP000192330};
RN [1] {ECO:0000313|EMBL:SMC61514.1, ECO:0000313|Proteomes:UP000192330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12644 {ECO:0000313|EMBL:SMC61514.1,
RC ECO:0000313|Proteomes:UP000192330};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 ---------------------------------------------------------------------------
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; FWYD01000003; SMC61514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2ALM6; -.
DR STRING; 1387277.SAMN06295998_103101; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000192330; 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 Reference proteome {ECO:0000313|Proteomes:UP000192330};
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"
FT REGION 746..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 111884 MW; EBE00BBB47E0873B CRC64;
MLRKKTNGVA RRPQRTSILS DVAQTSVDRR AFLRGSGLAI GGLAAIAATG GTVTQASAQS
AVSGAVELRK SVCTHCSVGC TVQAEVSNGV WIGQEPGWDS PFNLGAHCAK GASVREHAHG
ERRLKYPMKK EGGEWKRISW EQAINEIGDG MMQIREQSGP DSVYWLGSAK HSNEQAYLFR
KFASYWGTNN VDHQARICHS TTVAGVANTW GYGAMTNSYN DIHNSKAMFL IGSNPAEAHP
VSLLHLLKAK EENNAPLIVC DPRFTRTAAH ADEYVRFRPG TDVALIWGVL WHIFENGWED
KEFIRTRVWG MDQIREEVAK WNPDEVERVT GTPGSQLGRV ARTLANNRPG TLIWCMGGTQ
HSTGNNNTRA YCVLQLALGN IGTQGGGANI FRGHDNVQGA TDLGVLSHTL PGYYGLAKGA
WQHWARVWEE DFDWLNGQFQ TVKGADGKDK NLMYETGIPV SRWIDGVLED AENIDQPNNL
RAMVLWGHAP NSQTRMAEMK TAMEKLDMLV VVDPYPTVSA VLHDRADGVY LLPAATQFET
YGSVTASNRS LQWREKVFDP LFESKPDQEI IGLFAKKFGF HDRMFRNIAI EEDGVTPNVE
DTLRELNRGM WTVGYTGQSP ERLKLHMANQ HTFDRTTLQA IGGPADGDYY GLPWPCWGTP
EMNHPGTPNL YDMSKPVAEG GLCFRARFGV ERDGDNLLAE GVFNPGSEIQ DGYPEFTYQM
LVDLGWDGDL TDAEKRSIAG VAGVQIDGGV GESDDGDDGA TSGLTSADGT QGAAEEVGEQ
SMSPFPSDFN AKAKGVNWKT DLSGGIQRVA IKHGCAPFGN AKARTVVWTF PDPVPVHREP
LYSPRRDLVA DYPTYEDRKF YRLPTMYASI QKQDFSKDYP IILTSGRLVE YEGGGEETRS
NPWLAELQQD MFVEINPRDA NNLGVRDGAQ VWVEGAEGSK VKVMAMVTRR VGEGVAFMPF
HFGGHFQGED LRSKYPDGAD PYVLGESSNT AQTYGYDSVT QMQETKCTLC KIMPA
//
