ID A3KAW8_9RHOB Unreviewed; 965 AA.
AC A3KAW8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Formate dehydrogenase, alpha subunit, putative {ECO:0000313|EMBL:EBA05696.1};
GN ORFNames=SSE37_03320 {ECO:0000313|EMBL:EBA05696.1};
OS Sagittula stellata E-37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sagittula.
OX NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA05696.1, ECO:0000313|Proteomes:UP000005713};
RN [1] {ECO:0000313|EMBL:EBA05696.1, ECO:0000313|Proteomes:UP000005713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E-37 {ECO:0000313|EMBL:EBA05696.1,
RC ECO:0000313|Proteomes:UP000005713};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2006) 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:EBA05696.1}.
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DR EMBL; AAYA01000026; EBA05696.1; -; Genomic_DNA.
DR RefSeq; WP_005864015.1; NZ_AAYA01000026.1.
DR AlphaFoldDB; A3KAW8; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000005713; 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:UP000005713};
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 965 AA; 107530 MW; A71D6A765D486207 CRC64;
MLRKKTNGVA RRPQRTSILS EVAKTSVDRR GFLRGSGLAI GGLAAIAATG GTVQQASAQT
AATGKVDLKK TVCTHCSVGC TVMAEVQDGV WTGQEPGWDS PFNLGSHCAK GASVREHTHG
ERRLKYPMKK VGGEWVRISW EDAINEIGDQ MMTIREESGP DSVYWLGSAK HNNEQAYLFQ
KFARYWGTNN VDHQARICHS TTVAGVANTW GYGAMTNSYN DIHNSKAIFI IGGNPAEAHP
VSLLHVLRAK EQNNAPLIVC DPRFTRTAAH ADEYVRFRPG TDVALVWGIL YHIFENGWED
REFIRTRVWG MDQIREEVAK WNPEEVERVT GVPGSQLERV ARTLANNRPG TVIWCMGGTQ
HTTGNNNTRA YCILQLALGN MGVSGGGTNI FRGHDNVQGA TDLGVLSHTL AGYYGLAKGS
WQHWTRVWGE DFDWLNGQFA KMPGADGKDK DLMYETGIPV SRWIDGVLED AENMDQPNKV
RGMVLWGHAP NSQTRMVEMK KAMELLDLLV VVDPYPTVSA VLHDRTDGVY LLPAATQFET
YGSVTASNRS IQWRQRVVKP IFESKPDHEI MGLFAKKFGY HDRLFRNIAI EEDGVTPNIE
DTLREINRGM WTVGYTGQSP ERLKLHMENQ HTFDRTTLRA VGGPADGDYY GLPWPCWGTA
EMNHPGSPNL YNIDLAVKDG GLPFRARYGV ERNGDNLLAE GVFNPGSEIQ DGYPEFTMQM
LMDLGWDADL TDEEKSTIEA IAGPKTNWKT DLSGGIQRVA IEHGCAPYGN AKARCVVWEF
PDPVPIHREA LYTNRRDLVA DYPTYDDRKF YRLPTMYASI QKQDFSKDYP MILTSGRLVE
YEGGGDETRS NPWLAELQQD MFVEINPRDA NNLGVRDAAM VWVEGPEGGK VKVKAMVTER
VGEGVAFMPF HFGGWYQGED LRSKYPEGAD PIVLGESTNT AQTYGYDSVT QMQETKATLC
KIMPA
//
