ID   B9SR96_RICCO            Unreviewed;       498 AA.
AC   B9SR96;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   28-FEB-2018, entry version 47.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=RCOM_0112580 {ECO:0000313|EMBL:EEF33884.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae;
OC   Acalyphoideae; Acalypheae; Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B.,
RA   Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M.,
RA   Ravel J., Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; EQ974095; EEF33884.1; -; Genomic_DNA.
DR   RefSeq; XP_002528515.1; XM_002528469.2.
DR   ProteinModelPortal; B9SR96; -.
DR   GeneID; 8258742; -.
DR   KEGG; rcu:8258742; -.
DR   InParanoid; B9SR96; -.
DR   KO; K01580; -.
DR   Proteomes; UP000008311; 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   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   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:UP000008311};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:EEF33884.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   498 AA;  56536 MW;  145A0F913DD35C51 CRC64;
     MVLSKTASES DVSVHSTFAS RYVRASLPRF KMPESSIPKE AAYQIINDEL MLDGNPRLNL
     ASFVTTWMEP ECDKLIMASI NKNYVDMDEY PVTTELQNRC VNMIAHLFNA PLGDSETAVG
     VGTVGSSEAI MLAGLAFKRK WQNKRKAEGK PYDKPNIVTG ANVQVCWEKF ARYFEVELKE
     VKLRDGYYVM DPVKAVEMVD ENTICVAAIL GSTLNGEFED VKLLNDLLTE KNKQTGWDTP
     IHVDAASGGF IAPFLYPELE WDFRLPLVKS INVSGHKYGL VYAGIGWVIW RNKDDLPDEL
     IFHINYLGAD QPTFTLNFSK GSSQVIAQYY QLIRLGYEGY RNIMENCRDN MLVLKDGLEK
     TGRFTIVSKD NGVPLVAFSL KDNSSHNEFE ISELLRRFGW IVPAYTMPPD AQHVTVLRVV
     IREDFSRTFA ERLVLDIEKV LHELDTLPSR LREKIAIVEE KEKNGTKAAK KSVIETQREI
     TTIWKKFVLE KKKMNGVC
//