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Database: UniProt/TrEMBL
Entry: C4R641_KOMPG
LinkDB: C4R641_KOMPG
Original site: C4R641_KOMPG 
ID   C4R641_KOMPG            Unreviewed;       556 AA.
AC   C4R641;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   28-FEB-2018, entry version 55.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   OrderedLocusNames=PAS_chr3_0965 {ECO:0000313|EMBL:CAY71027.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia
OS   pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY71027.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY71027.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; FN392321; CAY71027.1; -; Genomic_DNA.
DR   RefSeq; XP_002493206.1; XM_002493161.1.
DR   STRING; 644223.XP_002493206.1; -.
DR   EnsemblFungi; CAY71027; CAY71027; PAS_chr3_0965.
DR   GeneID; 8199681; -.
DR   KEGG; ppa:PAS_chr3_0965; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; C4R641; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000000314; Chromosome 3.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 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   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000314};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000314}.
FT   MOD_RES     309    309       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   556 AA;  62772 MW;  30E32E981AE66A1D CRC64;
     MTLSNNTKRR ESSITPDQQK LIEKYLEKKN VHHQKKLQHV THTSTNVNLS SIKWKSLRLE
     DCGVSIPDSG LPAKIAYESI HDSLNLDGNP TLNLASFVNT GYINDYSEPL IHENLVKNLA
     DNDEYPVMLE LHERCLQMLT ELWNGDSKKS IGSATTGSSE AIMLGGLAMK KNWQTKRRAA
     GKSTEKPNII MASCCQVALE KFARYFEVDA RIISCDNNDY ILDYDLIYDA CDENTIGIFV
     ILGSTYTGAF EDVALVNKIL DRVEKEKGFD IPIHVDGASG AFVAPFIYPD LEWDFRVPRV
     KSINTSGHKF GLVTAGLGWI VFKDKEWLPK DLVFELRYLG GLEYSFTLNF SRPGHQVIHQ
     YFNFVALGKN GYSSIFDTCL TNARLLSSFL EETNYFKVVS NVHRPVEAGT TPHADDHLAF
     HPSLPVVSFQ FNEEFSKQYP EIPQSIISTL MRNKGWIIPN YPLPRTTKPV KDDEREILRV
     VVRYNLTLEL LQKLMSDIVS TLTVLTNSCK LIRESLNNDA LEDTDIIYDM LLSIALDGSE
     NLVKSSIKDH KHAGAC
//
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