ID D2Y9M2_VIBMI Unreviewed; 774 AA.
AC D2Y9M2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Molybdopterin oxidoreductase, alpha subunit {ECO:0000313|EMBL:EEW08555.1};
GN ORFNames=VMB_02190 {ECO:0000313|EMBL:EEW08555.1};
OS Vibrio mimicus VM603.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=671074 {ECO:0000313|EMBL:EEW08555.1, ECO:0000313|Proteomes:UP000004827};
RN [1] {ECO:0000313|EMBL:EEW08555.1, ECO:0000313|Proteomes:UP000004827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM603 {ECO:0000313|EMBL:EEW08555.1,
RC ECO:0000313|Proteomes:UP000004827};
RX PubMed=19860885; DOI=10.1186/1471-2148-9-258;
RA Thompson C.C., Vicente A.C., Souza R.C., Vasconcelos A.T., Vesth T.,
RA Alves N.Jr., Ussery D.W., Iida T., Thompson F.L.;
RT "Genomic taxonomy of Vibrios.";
RL BMC Evol. Biol. 9:258-258(2009).
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 -!- 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:EEW08555.1}.
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DR EMBL; ACYU01000014; EEW08555.1; -; Genomic_DNA.
DR RefSeq; WP_001072106.1; NZ_ACYU01000014.1.
DR AlphaFoldDB; D2Y9M2; -.
DR Proteomes; UP000004827; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR PIRSF; PIRSF000144; CbbBc; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT DOMAIN 110..491
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
SQ SEQUENCE 774 AA; 86368 MW; A563F0230C3283EC CRC64;
MNQKEEIKEY PGPAAGWGAL KAVTKSWLGS ENGFRNLRAM LKTNQNGGFD CPGCAWGESP
ENGMVNFCEN GAKAVNWEAT SRLVDPEFFA QYSVSELSKQ TDYWLEYQGR LSHPMRYDAQ
TDHYVEISWE DVFALVGEHL NALQSPDEAE FYTSGRASNE AAFLYQLFVR AFGTNNFPDC
SNMCHEASAI GMFDSIGVGK GTVVFKDLEQ ADAIFVIGQN PGTNHPRMLE PLREAVKRGA
QVICLNPLKE RGLERFQNPQ HPIEMLSNGS EPTSSAYFRP ALGGDMAVFR GMAKFLLQWD
RQAQVQGDAP VLDHDFIREH TNGIEEYLSA VEQTSWEHIT QQSGLSLEEI EVLARMYRRA
ERVVMCWAMG LTQHRHSVYT IQEVVNLQLL RGNVGKPGAG LSPVRGHSNV QGDRTMGINE
KPPQFLLDAL EKRFQFKVPR THGHNAVLAI KAMEEKRAKV FVGLGGNFAQ ATPDTPRTHA
AMRNCELTVH IATKLNRSHL VTGHDALILP CLGRTEIDMQ ANGPQGVTVE DTFSMVHLSY
GQLKPRSPHL RSEAAILAGI AKATLGNFPI DWDWAIADYS HIRDLIADTI SGFQNFNQRV
QNPGGFYLGN SAARREWNTV SGKAQFSATT LPEQLVNDNV TQRGDKPDLI LQTLRSHDQY
NTTLYGLDDR YRGVFGRRDV VFANEEDIRR LGFKPGDRVD LVTLWDDGLE RRVNGFELVA
YDVPAGQAAA YYPETNPLVP LDSYGERTFT PTSKFVAIKL EKAKPTILIP ATVL
//