ID   Q5K920_CRYNJ            Unreviewed;       557 AA.
AC   Q5K920; Q55LQ3;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 139.
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   OrderedLocusNames=CNH03700 {ECO:0000313|EMBL:AAW45225.1}, CNL03700
GN   {ECO:0000313|EMBL:AAW46416.1};
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW46416.1, ECO:0000313|Proteomes:UP000002149};
RN   [1] {ECO:0000313|EMBL:AAW46416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JEC21 {ECO:0000313|EMBL:AAW46416.1};
RA   Loftus B., Amedeo P., Roncaglia P., Vamathevan J., Utterback T.,
RA   Van Aken S., Fraser C.;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAW46416.1, ECO:0000313|Proteomes:UP000002149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 {ECO:0000313|EMBL:AAW46416.1}, and JEC21 / ATCC MYA-565
RC   {ECO:0000313|Proteomes:UP000002149};
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
RN   [3] {ECO:0000313|EMBL:AAW46416.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JEC21 {ECO:0000313|EMBL:AAW46416.1};
RA   Janbon G., Paulet D., Chon C.C., Mornico D.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 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|RuleBase:RU361171};
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; AE017348; AAW45225.1; -; Genomic_DNA.
DR   EMBL; AE017352; AAW46416.1; -; Genomic_DNA.
DR   RefSeq; XP_567933.1; XM_567933.1.
DR   RefSeq; XP_572532.1; XM_572532.1.
DR   AlphaFoldDB; Q5K920; -.
DR   STRING; 214684.Q5K920; -.
DR   PaxDb; 214684-Q5K920; -.
DR   EnsemblFungi; AAW45225; AAW45225; CNH03700.
DR   EnsemblFungi; AAW46416; AAW46416; CNL03700.
DR   GeneID; 3254998; -.
DR   GeneID; 3259079; -.
DR   KEGG; cne:CNH03700; -.
DR   KEGG; cne:CNL03700; -.
DR   VEuPathDB; FungiDB:CNH03700; -.
DR   VEuPathDB; FungiDB:CNL03700; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_019582_2_3_1; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; 2783360at2759; -.
DR   Proteomes; UP000002149; Chromosome 12.
DR   Proteomes; UP000002149; Chromosome 8.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
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|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002149}.
FT   MOD_RES         297
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   557 AA;  62717 MW;  A50822786EF33701 CRC64;
     MALSQHVDAD KLIEECKDHP IKRHLSHKAA LYDIPYTSRY EVEDEVPRYR LPSKGVNGRA
     TYQLLHDELM LDGNPNMNLA SFVHTWVPDE CNRLVQENIN KNLVDQDEYP AAQQIHERCI
     SMLSHLWHAP KEATAMGTAT TGSSEAIMLG GLALKRRWQE KMKAAGKDIH NPGPNIVMGA
     EAQVALEKFA RYFEVEARLV PIKPESSYVM DPKDVLKYVD ENTIGVFVIL GSTYTGAFES
     VKDVAQELDK YEAETGISVP IHVDAASGGF VAPFAYPHYQ WDFQIPRVHS INASGHKYGM
     STVGVGWIIW RSMEYLPKEL IFELHYLGAT DYSFNLNFSR PAHPILAQMF TFLNLGFEGY
     KRIMDKNLTV ARLISRALEH SGYFICLSKI HHPKALTESS SSAEQSNILP AVADAANTVL
     HGKKTTVDDA EYYCEGLPVV SFMFTDEIKK KYPGVKQAWI QMQLRSIGWI VPNYPLAPDC
     EKTEILRVVV RESLSGDLAR KLIHDILQVT EDLLNDAGPS YSMSTATRRH ENLDHGKLDN
     IDAVHIKQHT STYSKPC
//