GenomeNet

Database: UniProt/TrEMBL
Entry: J0CYB0_AURST
LinkDB: J0CYB0_AURST
Original site: J0CYB0_AURST 
ID   J0CYB0_AURST            Unreviewed;       529 AA.
AC   J0CYB0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   25-OCT-2017, entry version 32.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=AURDEDRAFT_117124 {ECO:0000313|EMBL:EJD36278.1};
OS   Auricularia subglabra (strain TFB-10046 / SS5) (White-rot fungus)
OS   (Auricularia delicata (strain TFB10046)).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Auriculariaceae; Auricularia.
OX   NCBI_TaxID=717982 {ECO:0000313|EMBL:EJD36278.1, ECO:0000313|Proteomes:UP000006514};
RN   [1] {ECO:0000313|Proteomes:UP000006514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFB10046 {ECO:0000313|Proteomes:UP000006514};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kuees U.,
RA   Kumar T.K.A., Kuo A., LaButti K., Larrondo L.F., Lindquist E.,
RA   Ling A., Lombard V., Lucas S., Lundell T., Martin R., McLaughlin D.J.,
RA   Morgenstern I., Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A.,
RA   Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A.,
RA   Samejima M., Schmutz J., Slot J.C., St John F., Stenlid J., Sun H.,
RA   Sun S., Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A.,
RA   Eastwood D.C., Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; JH687866; EJD36278.1; -; Genomic_DNA.
DR   RefSeq; XP_007355632.1; XM_007355570.1.
DR   GeneID; 18850019; -.
DR   KEGG; adl:AURDEDRAFT_117124; -.
DR   InParanoid; J0CYB0; -.
DR   KO; K01580; -.
DR   OMA; KNIMQNC; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000006514; 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:UP000006514};
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:UP000006514}.
FT   MOD_RES     289    289       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   529 AA;  59256 MW;  ED383338FB0E2CE7 CRC64;
     MLSLHIDPEE VLQKAADNPV KKQDSRSAFH SYVRDGDIPI PKYTLPETGV NSKVAYQVIH
     DELTLDGNPT LNLASFVHTW MPPEAEKLIM ENISKNAVDQ DEYPATQVIH ARCISMLANL
     WKVPKGMKAI GTATAGSSEA IMLGGLALKK RWQEKRKAEG KDYFHPNIVF GANAQVALEK
     FARYFDVECR LVPVKEEHDF IMHPPDALQY IDENTIGVMV ILGSTYTGHF EDVALMSDLL
     DKLYEEKGLD IPIHVDGASG GFFAPFAYPE LKWSFDIPRV ASINTSGHKF GLVYAGLGWV
     LWKDESLLPK DLIFELHYLG SVEYSFTLNF SKPAAPIIAQ MFNFLNLGYQ GYRDVARKDL
     RNARLLSRAL ETTGYYKVLS NIHKESGNKN AGEHEPELYL PGLPVVAFRL SDEFKNDYPH
     VQQAWIQNLL RGKGWIVPNY GAPPAEDKQE ILRVVVRETM TADLVERLVT DLIAITESLM
     TTDSSGGTAQ MMAAIAGPHS KQGVHQPEAE HGRPQRPHPK RQNTYAKQC
//
DBGET integrated database retrieval system