ID   A8QDP9_MALGO            Unreviewed;       552 AA.
AC   A8QDP9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=MGL_4226 {ECO:0000313|EMBL:EDP41413.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP41413.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP41413.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- FUNCTION: Glutamate decarboxylase (GAD) involved in the production of
CC       both gamma-aminobutyric acid (GABA) and its downstream catabolite
CC       succinate. Although GADs are ubiquitous enzymes in both fungi and
CC       plants, their exact physiological functions remain to be investigated
CC       in their native hosts. GABA was shown to serve as an alternative
CC       nitrogen source with potential roles in pathogenicity and development.
CC       {ECO:0000256|ARBA:ARBA00094355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + H(+) = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00047724};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786;
CC         Evidence={ECO:0000256|ARBA:ARBA00047724};
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:EDP41413.1}.
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DR   EMBL; AAYY01000023; EDP41413.1; -; Genomic_DNA.
DR   RefSeq; XP_001728627.1; XM_001728575.1.
DR   AlphaFoldDB; A8QDP9; -.
DR   STRING; 425265.A8QDP9; -.
DR   GeneID; 5852944; -.
DR   KEGG; mgl:MGL_4226; -.
DR   VEuPathDB; FungiDB:MGL_4226; -.
DR   InParanoid; A8QDP9; -.
DR   OMA; GHFENVQ; -.
DR   OrthoDB; 5152799at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:L-glutamate catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.40.640.10:FF:000017; Glutamate decarboxylase; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT   DOMAIN          75..404
FT                   /note="Pyridoxal phosphate-dependent decarboxylase major"
FT                   /evidence="ECO:0000259|Pfam:PF00282"
FT   REGION          526..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         310
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   552 AA;  62376 MW;  F881FE2E45042519 CRC64;
     MVLSLSVDPE EYVQRAHVKE SHEAVEKARS HRHRSVDIPH YTPTGRYGTK PVPKYHLPEK
     GLSERATYEL LSNELLLDGK PSLNLASFVH TWMPDEARRL MMDTIGVNLC DQDEYPATIA
     IHTRCISIIS NLWKAPKGHV KDGRRLAAMG TATTGSSEAL MLGLLSAKRR WQNKRKEQGK
     DIHHPGPNLV FGANVQVCVE KFARYWDVEE RPVPVDESTH YCLDPKRAMD YVDENTIAVV
     VILGSTYTGH YEPVEEMALE LDEYQKKTGH DVPIHVDGAS GAMVAPFATP DHKWSFDVPR
     VASINTSGHK FGMVYPGIGW IIFRSPEMVP SDLVFELHYL GSVEYSFGLN FSRPAAPMIG
     QMFNFISLGR EGFRSTMEAN LMNARLLSRA LEYSGLFVVL SDIHRPAEKK VPITTEASKY
     CPGLPVVSFR WTDEIKREYP HMEQSWVQTL LRAKGWIVPN YELPPNLSDV QILRVVVRDS
     LTESMVEVLV QDIINITRHL MEQQRVAREA SMDPVSTRGM TNMLLGHSYK KNNDHGRPYG
     QGQPPNGFKS QC
//