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Database: UniProt/TrEMBL
Entry: A8NGQ7_COPC7
LinkDB: A8NGQ7_COPC7
Original site: A8NGQ7_COPC7 
ID   A8NGQ7_COPC7            Unreviewed;       565 AA.
AC   A8NGQ7;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   25-OCT-2017, entry version 53.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CC1G_03790 {ECO:0000313|EMBL:EAU88118.1};
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:EAU88118.1, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU88118.1, 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: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:EAU88118.1}.
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DR   EMBL; AACS02000002; EAU88118.1; -; Genomic_DNA.
DR   RefSeq; XP_001833573.1; XM_001833521.1.
DR   ProteinModelPortal; A8NGQ7; -.
DR   STRING; 240176.XP_001833573.1; -.
DR   EnsemblFungi; EAU88118; EAU88118; CC1G_03790.
DR   GeneID; 6010070; -.
DR   KEGG; cci:CC1G_03790; -.
DR   EuPathDB; FungiDB:CC1G_03790; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   InParanoid; A8NGQ7; -.
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:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT   MOD_RES     318    318       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   565 AA;  63361 MW;  30A1621C921980D3 CRC64;
     MQYKPSDVDK IIREAHEKQR ETAKVSKGQS VKDREEGFIY AGRYGTNPAP QHHLSSKGIS
     ADDAYRLIHD ELALDGSTVL NFASFVHTWM PPQALKLVQE NISKNLIDAD EYPATQEIHK
     RCLSILADLW HAPSPKDAVG TATTGSSEAV EIGGLALKKR WQERMKKAGK NIHEPGPNIV
     MGANAQVALE KFARYFDVEC RLVPVSKESR YCLDTKAAMD YVDENTIGVF AILGSTYTGH
     YEDVKAMSDL LDEYEKKTGI YVPIHGKSLV RTTHPSAGTD LHIVDAASGG FIAPFISPDL
     PWDFRLPRVV SINASGHKFG LTYVGVGWVL FRSEEHLPKE LVFTLSYLGS TQYSFSLNFS
     RPAFPIIAQY FNLLHLGFEG YRAVMLDDLR NARTLSRALE RIGSGGGKDE QGWFEVISDV
     HRAKGVHSGK GIDDPDVEAY EPSLPVVAFK FTEKFKEEYP EIEQRWVHIM LRAKGWIIPN
     YALAPNLDNE EILRVVVREC VTEVLVDRLI KDIVEIMNQF MESKPHGDTL QMIDMAHNKG
     ARRGDDGPQK MKEEDHSSGT YNHPC
//
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