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Database: UniProt/TrEMBL
Entry: A8PCA2_COPC7
LinkDB: A8PCA2_COPC7
Original site: A8PCA2_COPC7 
ID   A8PCA2_COPC7            Unreviewed;       538 AA.
AC   A8PCA2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   05-JUL-2017, entry version 51.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CC1G_05236 {ECO:0000313|EMBL:EAU81406.1};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC
OS   9003) (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Psathyrellaceae;
OC   Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU81406.1, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU81406.1, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W.,
RA   Borodovsky M., Burns C., Canback B., Casselton L.A., Cheng C.K.,
RA   Deng J., Dietrich F.S., Fargo D.C., Farman M.L., Gathman A.C.,
RA   Goldberg J., Guigo R., Hoegger P.J., Hooker J.B., Huggins A.,
RA   James T.Y., Kamada T., Kilaru S., Kodira C., Kues U., Kupfer D.,
RA   Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J., Mackey A.J.,
RA   Manning G., Martin F., Muraguchi H., Natvig D.O., Palmerini H.,
RA   Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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:EAU81406.1}.
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DR   EMBL; AACS02000011; EAU81406.1; -; Genomic_DNA.
DR   RefSeq; XP_001840350.1; XM_001840298.2.
DR   ProteinModelPortal; A8PCA2; -.
DR   STRING; 240176.XP_001840350.1; -.
DR   EnsemblFungi; EAU81406; EAU81406; CC1G_05236.
DR   GeneID; 6016986; -.
DR   KEGG; cci:CC1G_05236; -.
DR   EuPathDB; FungiDB:CC1G_05236; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; A8PCA2; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
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; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001861};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT   MOD_RES     294    294       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   538 AA;  60919 MW;  D8731EE34F273B86 CRC64;
     MLSRHIDPEE IIQKCREHPH KKHGSEGGRR GYHQSWRRDE DASTIPKYVM PRVGIPAKSA
     YQVLHDETAL DGNPLLNLAS FVHTWMPEEA DKLIMENINK NIVDLDEYPA ASIIHNRCVS
     MLADLWKAPK EGKVIGTATA GSSEAIMLGG LAMKKRWQEA RKAEGKDYYH PNIVFGANAQ
     VALEKFARYF DVEARLVPVK EENGFIMDPH DALKYIDENT IGVIVILGST YTGHFENVEL
     MSKLLDDLQE RTGLDIPIHV DGASGAFIAP FAFPKLKWSF DVPRVVSINT SGHKFGLVYA
     GIGWVLWRDE KYLHKDLVFE LHYLGSTEYT FTLNFSKPAA PVIAQMFNFL NLGFEGYRKI
     AYKDLRNARM LSKALESTYF TVMSNIHRRI EADPHENRNN HEDSPEGYEP GLPVVAFRLS
     DEFKQEYPHV QQVWIQQLLR AKGWIVPNYN APKGAEEVEI LRVVVRETLS EDLIERLIID
     ILEVTESTMN SKESFIAVSA ASQVRAHPDH DQARPELENF ADGTTIGGPE QMGFSSQC
//
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