ID   F2G682_ALTMD            Unreviewed;       544 AA.
AC   F2G682;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AEA99814.1};
GN   OrderedLocusNames=MADE_1018450 {ECO:0000313|EMBL:AEA99814.1};
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA99814.1, ECO:0000313|Proteomes:UP000001870};
RN   [1] {ECO:0000313|EMBL:AEA99814.1, ECO:0000313|Proteomes:UP000001870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC   {ECO:0000313|Proteomes:UP000001870};
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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; CP001103; AEA99814.1; -; Genomic_DNA.
DR   RefSeq; WP_012519843.1; NC_011138.3.
DR   AlphaFoldDB; F2G682; -.
DR   KEGG; amc:MADE_1018450; -.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000001870; Chromosome.
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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         333
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   544 AA;  60135 MW;  946C502265C4F213 CRC64;
     MGEAQVSLEH LFRVFTKPEH KDSKLAQIEQ HLSDNILDFL SQHVVTKKTS LEEIEKDFSD
     SKVPESPEFV STHAESLLDK LVAHSVNTYS PTFIGHMTSA LPYFHLPLSK LMVGLNQNLV
     KIETSKAFTP LERQVLGMMH NLVYDQPQRF YDNHLHSAAH SLGAFCSGGT IANITALWVA
     RNKLLGPQDG FCGVAKAGLA AAYRHLDINN LGVMCSKRGH YSLSKAVDVL GLGRDQLLTI
     PAPRQTLDPA KALRIGKRYQ EEGNKLLAIV GVGGTTETGH VDPLDELADV ANELGCWFHV
     DAAWGGATLF SSRYRDRLKG IERADSVTID AHKQMYVPMG AGMALFKDPQ NANAVRHHAQ
     YILRAGSKDL GATTLEGSRN GMAMMVYSAL HIFGRKGYEL LIDRSIDKAK DFSHMIDKAG
     DFELTTTPTL SLLTYRVCPE EVQEKLKHAD ANMRNAINEK VDALVVAVQK QQREAGKSFV
     SRTRLEAPDY PSQCITVFRV VLANPLTSHN DLAAILAEQH LIAKETQAWA ELMNFVRDSE
     KVAS
//