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Database: UniProt/TrEMBL
Entry: A3GHR1_PICST
LinkDB: A3GHR1_PICST
Original site: A3GHR1_PICST 
ID   A3GHR1_PICST            Unreviewed;       569 AA.
AC   A3GHR1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 2.
DT   25-OCT-2017, entry version 67.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   Name=DCE1 {ECO:0000313|EMBL:EAZ63096.2};
GN   ORFNames=PICST_40180 {ECO:0000313|EMBL:EAZ63096.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 /
OS   NRRL Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:EAZ63096.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:EAZ63096.2, 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-
RT   fermenting yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAZ63096.2}.
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DR   EMBL; AAVQ01000002; EAZ63096.2; -; Genomic_DNA.
DR   RefSeq; XP_001387119.2; XM_001387082.1.
DR   ProteinModelPortal; A3GHR1; -.
DR   STRING; 322104.XP_001387119.2; -.
DR   EnsemblFungi; EAZ63096; EAZ63096; PICST_40180.
DR   GeneID; 4851810; -.
DR   KEGG; pic:PICST_40180; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000070228; -.
DR   InParanoid; A3GHR1; -.
DR   KO; K01580; -.
DR   OMA; RPNLVMG; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000002258; Chromosome 1.
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   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002258};
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:UP000002258}.
FT   MOD_RES     298    298       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   569 AA;  63950 MW;  866EBC8F0D1A0A32 CRC64;
     MTLSKHIDAE VLETALLKNA VKSKLTKREE YISQYDSEKL VPKYEIPSHS SSGELVYKYL
     SEELTLDGNP TLNLASFVNT SCDDTQLKLI TDNIVKNLAD NDEYPSLIDF QQRCISILSN
     LWHAPTKVDS TGKKVINSIG TATTGSSEAI MLAGLALKKR WQEKRKAAGK STENPNIIMA
     SVAQVALEKF ARYFDVEDRL IHVNEESGHL IDISKIKEAV DENTIGIFVI LGSTFTGAFE
     PVEQISHLLD EIEKEKGLDV RIHVDGASGG FVAPFVYPHL KWDFQIPRVD SINTSGHKFG
     LTTAGLGWVI WKDSELLPKS LKFSLDYLGG VEETFGLNFS RAGFPVVLQY YNFLTLGKEG
     YSKIFNSCIS NARLLSNILE KSEYFEVLSV IHKEVSDERA AQVYTKVHHV DSKHTKEAIH
     NEKFEPGLPV VAFRFSKELR ETYPEIPQGI FSTLLRNKGY IVPNYHLPPD EGEKEILRVV
     VRQSLSLNLL EKLVKDSIEA VELLIKSCKD VRDVIHAKHT TEEVDKGLVY SLLLSISSGG
     VEDKKEIQHE QLKQASVNPK HKRRYRATC
//
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