ID Q7MKS8_VIBVY Unreviewed; 951 AA.
AC Q7MKS8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=Putative formate dehydrogenase large subunit {ECO:0000313|EMBL:BAC94464.1};
GN OrderedLocusNames=VV1700 {ECO:0000313|EMBL:BAC94464.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC94464.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC94464.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC94464.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000037; BAC94464.1; -; Genomic_DNA.
DR RefSeq; WP_011150293.1; NC_005139.1.
DR AlphaFoldDB; Q7MKS8; -.
DR STRING; 672.VV93_v1c15920; -.
DR KEGG; vvy:VV1700; -.
DR PATRIC; fig|196600.6.peg.1675; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_6; -.
DR Proteomes; UP000002675; Chromosome I.
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; 4.
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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 61..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 951 AA; 106834 MW; 30EBC5E5D5F5C538 CRC64;
MKLIKRSDSV TKEQKQLGIS RRVFMRNSSL AAGGAIAGAS MFAPGMIRKA EAKSVDASAP
IEVKRTICSH CSVGCGIYAE VQNGVWTGQE PAFDHPFNAG GHCAKGAALR EHGHGERRLK
YPMKLENGKW KKLSWDQAIE EIGNKVLEIR EQSGPDSVYW LGSAKHNNEQ AYTFRKMASM
WGTNNVDHQA RICHSTTVAG VANTWGYGAM TNSFNDMHNC KSMLFIGSNP AEAHPVAMQH
ILIAKEKNSC KIVVADPRRT RTAAKADHYV SLRPGTDVAF IWGVLWHVFN NKWEDKEFIR
QRVFGMDEIR AEVAKWNPKE VERVTGVSEE DVYQTAKLLS DHRPGCIVWC MGGTQHTTGN
NNTRAYCVLE LALGNLGKSG GGANIFRGHD NVQGATDLGV LSHTLPGYYG LAEGSWKHWA
KVWGIDFDWL KNRFDQNKYN GKQPMFNMGI PVSRWIDGVL ENKDSIEQND NIRAMFYWGH
AVNSQTRGVE MKKAMEKLDM MVIVDPYPTV AAVMNDRTDG VYLLPATTQF ETHGSVTASN
RSIQWRDQVI EPLFESKPDH EIMYLLTKKL GFADQLFKNV RVVNNQPVIE DITREFNKGM
WTIGYTGQSP ERLKAHQQNW HTFHKTTLAA EGGPANGETY GLPWPCWGTP EMKHPGTHIL
YDTSKPVAQG GGTFRTRFGV EFEGKSLLAD GSYSKDSDIQ DGYPEFSDKL LKQLGWWDDL
TAEEKALAEG KNWKTDLSGG IQRVAIKHGC IPFGNGKART IVWEFPDRVP LHREPLYTPR
RDLIADYPTW DDAASIYRLP TLYKSIQDQD KSQEYPIILT SGRLVEYEGG GEETRSNPWL
AELQQEMFVE VNPKDANDLG FKDGDMVWVE GAEKGRIHVK AMVTRRVRPG MAFIPFHFGG
KFQGEDLRNK YPEGTDPYVI GESANIATTY GYDPVTQMQE TKVTLCNIRK A
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