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Database: UniProt/TrEMBL
Entry: Q7MLI5_VIBVY
LinkDB: Q7MLI5_VIBVY
Original site: Q7MLI5_VIBVY 
ID   Q7MLI5_VIBVY            Unreviewed;       581 AA.
AC   Q7MLI5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   07-JUN-2017, entry version 88.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:BAC94206.1};
GN   OrderedLocusNames=VV1442 {ECO:0000313|EMBL:BAC94206.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC94206.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC94206.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC94206.1,
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.,
RA   Liu Y.M., Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T.,
RA   Hor L.I., Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine
RT   pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; BA000037; BAC94206.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q7MLI5; -.
DR   EnsemblBacteria; BAC94206; BAC94206; BAC94206.
DR   KEGG; vvy:VV1442; -.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; VVUL196600:GJ9W-1496-MONOMER; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002675};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002675}.
FT   COILED      476    510       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     366    366       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   581 AA;  64496 MW;  3DE7E16BB5841A01 CRC64;
     MLIKTGHCSR FGLDCLARTT SIIKSICYMA MEQKTADVSF DSLLKIFTIP EGPDSTLTQI
     EAKLSQNLNK FLGEHIVAEE KPLREIEKDF SSAQIPERPS FVSDHTEHLL NTLVSHSVHT
     SSPSFIGHMT SALPYFLMPL SKIMIALNQN LVKIETSKAF TPLERQVLGM LHRLIYSQDE
     AFYSHWMHSA EHSLGAFCSG GTIANITALW VARNNALRAQ GDFKGVEKEG LFRAMKHYGY
     EGLAVLVSER GHYSLKKAAD VLGIGQAGLV AIKTDENNRV CPDALEAKIK ELQAQNIKAF
     AVIGVAGTTE TGSVDPLAEM AKICQKYGCH FHVDAAWGGA TLMSNKYRSL LDGVELADSV
     TIDAHKQLYI PMGAGMVLFK DPNAMKSIEH HAQYILRKGS KDLGSHTLEG SRSGMAMLVY
     ASMHIISRPG YELLINQSIE KAKYFADLIK QQDDFELISE PELCLLTYRY IPARVKQALA
     AANAKQQLEL NELLNELTKF TQKRQRETGR SFVSRTRLNP AQWSRMNTIV FRVVLANPLT
     SFDILASVLE EQRNIIVHQA PNLLAKINKL ADGIITSTQS S
//
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