ID D0IEV6_9VIBR Unreviewed; 951 AA.
AC D0IEV6;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Formate dehydrogenase-O major subunit {ECO:0000313|EMBL:EEZ00109.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:EEZ00109.1};
GN ORFNames=VOA_000157 {ECO:0000313|EMBL:EEZ00109.1};
OS Vibrio sp. RC586.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675815 {ECO:0000313|EMBL:EEZ00109.1, ECO:0000313|Proteomes:UP000006226};
RN [1] {ECO:0000313|EMBL:EEZ00109.1, ECO:0000313|Proteomes:UP000006226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC586 {ECO:0000313|EMBL:EEZ00109.1,
RC ECO:0000313|Proteomes:UP000006226};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Chertkov O., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (NOV-2009) 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; ADBD01000007; EEZ00109.1; -; Genomic_DNA.
DR RefSeq; WP_001236876.1; NZ_ADBD01000007.1.
DR AlphaFoldDB; D0IEV6; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000006226; 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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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 ECO:0000313|EMBL:EEZ00109.1}; 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; 106466 MW; 5991FF858C26D38E CRC64;
MRLIKRSDSV IKEQNQLGIS RRAFMKNTSL AAGGAAVGAS LFTPGMIRKA QASEVDRSAK
TEVKRTICSH CSVGCGIYAE VQNGVWTGQE PAFDHPFNAG GHCAKGAALR EHGHGERRLK
YPMKLEGGKW KKISWEQAIN EIGDKALKIR EESGPDSVYF LGSAKHSNEQ AYLFRKMASL
WGTNNVDHQA RICHSTTVAG VANTWGYGAM TNSFNDMHNC KSMLFIGSNP AEAHPVAMQH
ILIAKEKNSC KIVVADPRRT RTAAKADYFV SLRPGSDVAF IWGVLWHVFK NNWEDKEYIR
QRVFGMDEIR AEVAKWTPAE VERVTGVSEE EVYNTAKILA ENRPGCVVWC MGGTQHTTGN
NNTRAYCILE LALGNIGKSG GGANIFRGHD NVQGATDLGV LSDTLPGYYG LTEGSWKHWA
SVWGVDFEWI KNRFDQGTYN GALPMETPGI PVSRWIDGVL ENKDNLQQRE NIRAMFYWGH
AVNSQTRGVE MKKAMQKLDM MVIVDPYPTV AAVMNDRTDG VYLLPATTQF ETYGSVTASN
RSIQWRDQVI EPLFESKPDH EIMYLLSQKL GIVDQLCKNI RVENNQPLIE DITREFNRGM
WTIGYTGQSP ERLKTHQQNW HTFHKTTLAA EGGPANGDTY GMPWPCWGTP EMKHPGTHIL
YDTSKTVAEG GGNFRTRFGV EFEGKSLLAE DSYSKGCELQ DGYPEFSDKL LKQLGWWDDL
TAEEKAAAEG KNWKTDLSGG IQRVAIKHGC IPFGNAKARA IVWTFPDRVP LHREPLYTPR
RDLLADYPTW DDQAFIFRVP TLYKSIQAQD KSVEYPIILT SGRLVEYEGG GEETRSNPWL
AELQQEMFVE VNPKDANDLG FIDGDMVWVE GAEKGRIKVK AMVTRRVKPG MAFLPFHFGG
KFQGEDLRPK YPEGTQPYVV GEAANTATTY GYDPVTLMQE TKVTLCNIRK A
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