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Database: UniProt/TrEMBL
Entry: E9EPT7_METRA
LinkDB: E9EPT7_METRA
Original site: E9EPT7_METRA 
ID   E9EPT7_METRA            Unreviewed;       528 AA.
AC   E9EPT7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-APR-2018, entry version 38.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=MAA_01722 {ECO:0000313|EMBL:EFZ02140.1};
OS   Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS   anisopliae (strain ARSEF 23)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Metarhizium.
OX   NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ02140.1, ECO:0000313|Proteomes:UP000002498};
RN   [1] {ECO:0000313|EMBL:EFZ02140.1, ECO:0000313|Proteomes:UP000002498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z.,
RA   Hu X., Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W.,
RA   Wang S., Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y.,
RA   Feng M.G., Xia Y., Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
RN   [2] {ECO:0000313|EMBL:EFZ02140.1, ECO:0000313|Proteomes:UP000002498}
RP   GENOME REANNOTATION.
RC   STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and
RT   host adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:EFZ02140.1}.
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DR   EMBL; ADNJ02000001; EFZ02140.1; -; Genomic_DNA.
DR   RefSeq; XP_007817911.1; XM_007819720.1.
DR   EnsemblFungi; EFZ02140; EFZ02140; MAA_01722.
DR   GeneID; 19256008; -.
DR   KEGG; maj:MAA_01722; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000002498; 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:UP000002498};
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:UP000002498}.
FT   MOD_RES     300    300       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   528 AA;  59459 MW;  EEAC9DD6F8774143 CRC64;
     MVHLSAINKD DSGSAASIAN DAVAHLTQKA RSTLKLSSEE DSLTTSVYGS RFAEQELPRF
     TMPERAMPRE IAYRMIKDDL SLDNNPKLNL ASFVTTYMED EAEKLMAHSL SKNFIDYEEY
     PQSADIQSRC VNMIGDLFHA PSGNAIGTSS VGSSEAIMLA VLAMKRRWKI RRHAEGKSTE
     RPNLIMSSAV QVCWEKATRY FEIEEKFINC TPTRFVIDPE EMVAKCDENT IGCVLILGTT
     YTGDYEDVKA VNDLLIEKNI DVPIHVDAAS GGFVAPFVVP DLEWDFRCEK VVSINVSGHK
     YGLVYPGVGW AIWRAAEYLP QDLVFNIDYL GAQQSSFTLN FSKGASQVIG QYYQLIRLGK
     QGYRLIMSNL TRTADYLSDS LQKLGFIIMS KRAGEGLPLV AFRFPGPNEG GHQDRHYDEF
     TLARQLRSRG WVVPAYTMAP NTNKMKMLRV VVREDFSRSR CDVLIHDIKI CLGMLEEMDR
     ETVKRQEEYI KTHLTSSGRA QESIHKPQHF KDDDHSLQGK TGKTHAAC
//
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