ID E9EC41_METAQ Unreviewed; 501 AA.
AC E9EC41;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Glutamate decarboxylase, putative {ECO:0000313|EMBL:EFY86507.1};
GN ORFNames=MAC_07450 {ECO:0000313|EMBL:EFY86507.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY86507.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY86507.1,
RC ECO:0000313|Proteomes:UP000002499};
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., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA 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).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; GL698545; EFY86507.1; -; Genomic_DNA.
DR RefSeq; XP_007813790.1; XM_007815599.1.
DR AlphaFoldDB; E9EC41; -.
DR STRING; 655827.E9EC41; -.
DR GeneID; 19251761; -.
DR KEGG; maw:MAC_07450; -.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; E9EC41; -.
DR OMA; RHATYHA; -.
DR OrthoDB; 888358at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 501 AA; 54259 MW; 53A7EAE1E5098D4B CRC64;
MTVTATATNG HVRGNAANGS TTRLNRAEEL DDLLLAVRDL ILPFVKAADD AAAHRETGRL
PLDATGTPHN VLVDAVKPHI LAAHLKFILP EEGQGKEGLL EGIAKVLKYS VNTWDQGFLD
KLYASNNPLH VYQVSPALTI IEKTTGRALA NKFGFTGPRA GGVTCQGGSS SNLTSLVVAR
NTLYPDCKTK GNVKHDFVVF TSAHGHYSVE KSAMICGMGS SNVWKVPVDD GGRMNADALR
ELVVRAKEQG KTPLYVNTTA GSTVRGSYDP FEDISKICKE FGLWMHIDAS WGGPVVFSAR
QRWKVKGSHL ADSITINPHK MLNAPTTCSF LLGPDMSLFN KANTTDAGYL FHGSTEDDVW
DLADLTLQCG RRGDSLKVAL AWLYYGANGF EKQIDHAFDM ASYLWKLVQQ TGNFAMVSEN
PPPCLQVCFY YAPGGDLSSD AATNTNRTQA LVEKLIDRGF MVDYAPGDVG SFLRIVVNVQ
TLPSTVEGLT RALEEAGKEV A
//
