ID   Q7MLI5_VIBVY            Unreviewed;       581 AA.
AC   Q7MLI5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 117.
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; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   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., 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=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, 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   AlphaFoldDB; Q7MLI5; -.
DR   STRING; 672.VV93_v1c13540; -.
DR   KEGG; vvy:VV1442; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   COILED          476..510
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         366
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="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
//