ID A0A2T6BEW6_9RHOB Unreviewed; 964 AA.
AC A0A2T6BEW6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:PTX54605.1};
GN ORFNames=C8N43_3422 {ECO:0000313|EMBL:PTX54605.1};
OS Litoreibacter ponti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1510457 {ECO:0000313|EMBL:PTX54605.1, ECO:0000313|Proteomes:UP000243978};
RN [1] {ECO:0000313|EMBL:PTX54605.1, ECO:0000313|Proteomes:UP000243978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100977 {ECO:0000313|EMBL:PTX54605.1,
RC ECO:0000313|Proteomes:UP000243978};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX54605.1}.
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DR EMBL; QBKS01000002; PTX54605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6BEW6; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000243978; 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:UP000243978};
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; 106808 MW; 14F9450286F84FE2 CRC64;
MLRKKTNGVA RRPQRTSILS EAANAAVDRR AFLRGSGLAI GGLAAIAATG GSVTQATAQS
AAAGAVETVK SVCTHCSVGC TVIAEVQDGV WTGQEPGWDS PFNLGAHCAK GAAVREHAHG
ERRLKYPMKK EGGEWKRISW DQAINEIGDG MMKIRDESGP DSVYWLGSAK HNNEQAYLFR
KFAGYWGTNN VDHQARICHS TTVAGVANTW GYGAMTNSYN DIHNSKAIFI IGGNPAEAHP
VSLLHLLKAK EQQNAPVIVC DPRFTRTAAH ADEYVRFRPG SDVALVWGIL YHIFENGWED
KEFIRTRVWG MDQIKDEVAK WTPEEVERVT EVPGSQLKRV ARTLANNRPG TVIWCMGGTQ
HTNGNNNTRA YCILQLALGN MGTAGGGTNI FRGHDNVQGA TDLGVLSHTL PGYYGLTAGS
WAHWARVWGE DIDWLKGQFA VTKGADGKDK PLMNETGIPV SRWIDGVLED PENMDNPNKV
RAMVFWGHAP NSQTRMKEMK TAMEQLDMLV VVDPYPTVSA VMQDREDGVY LLPACTQFET
RGSVTASNRS IQWRDKVVEP LFESLPDEVI MAKFANKFGW ADRFFRNIEM EDAETPNVES
ITREFNSGMW TVGYTGQSPE RIKLHMANQH TFDRTTLQAV GGPADGDYYG MPWPCWGTPE
MKHPGTPNLY DMSKPVSEGG LTFRARFGVE RDGDNLLAEG VYSAGSEIQD GYPEFTMQML
MDLGWDGDLT DDERAAIDAV AGPKTNWKTD LSGGIQRVAI KHECAPFGNA KARAVVWTFP
DPVPVHREPL YTNRRDLVAD YPTYEDRKFY RLPTMYASIQ KNDFSKDYPM ILTSGRLVEY
EGGGDETRSN PWLAELQQDM FVEINPRDAN NLGVRDGAQV WVEGPEGGKV KVMAMVTNRV
GEGVAFMPFH FGGHFEGRDL RENYPDGADP YVLGESTNTA QTYGYDSVTQ MQETKATLCK
IWTA
//
