ID   A3LP27_PICST            Unreviewed;       507 AA.
AC   A3LP27;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=Glutamate decarboxylase 2 {ECO:0000313|EMBL:ABN64416.2};
DE            EC=4.1.1.15 {ECO:0000313|EMBL:ABN64416.2};
GN   Name=GAD2 {ECO:0000313|EMBL:ABN64416.2};
GN   ORFNames=PICST_55334 {ECO:0000313|EMBL:ABN64416.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64416.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN64416.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000496; ABN64416.2; -; Genomic_DNA.
DR   RefSeq; XP_001382445.2; XM_001382408.1.
DR   AlphaFoldDB; A3LP27; -.
DR   STRING; 322104.A3LP27; -.
DR   GeneID; 4836947; -.
DR   KEGG; pic:PICST_55334; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   InParanoid; A3LP27; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   MOD_RES         315
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   507 AA;  57285 MW;  ED33E523E03E0EA0 CRC64;
     MAITSDLETS RVEELDHLLT VLKPKLLSYI EKADRDSKNY EVNSLGHYYE PQFLKKQFFH
     PPQATSIVGN DPQDDDKLFE VIDKVLEYSV NTWNPGFLDK LYASNNPIGV VSDIILSMLN
     TNSHVYTVSP VLSIIENHIG RKYASLFFTN HRKTCGGLTF SGGSWSNITS LQMARSLRFP
     DTKENGNGSY KFAVYSSKHC HYSVEKAAIL LGLGSSNVFK VNILADGSMD ANDLEKKIDQ
     SIKDGYTPLY INATAGTTVF GSYDPFEKIA DIAQKYKIHF HVDGSWGGNV IFSATHKKKL
     AGVERADSIT VNPHKMLGVP NTCSFLLVPH VSHFQESMSL KAPYLFHGRE EEEDENYDLA
     DGTMGCGRRA DSFKFYMAWL YFGFEGFASR VDHAFAIARD FVEKISRDKR FELVIGDTEN
     LPQCLQVCFY YRPSSYTHED NTDITRYISR ELHKQGKYLV DFSPNPTSSD NKGEFFRVVF
     NSPILSDEVV DDLITSIVES GETYKHI
//