ID A0A0A2JYW0_PENEN Unreviewed; 785 AA.
AC A0A0A2JYW0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN ORFNames=PEX2_054110 {ECO:0000313|EMBL:KGO59833.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO59833.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO59833.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO59833.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000256|RuleBase:RU361171};
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: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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO59833.1}.
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DR EMBL; JQFZ01000089; KGO59833.1; -; Genomic_DNA.
DR RefSeq; XP_016600936.1; XM_016742685.1.
DR AlphaFoldDB; A0A0A2JYW0; -.
DR STRING; 27334.A0A0A2JYW0; -.
DR GeneID; 27678104; -.
DR HOGENOM; CLU_357190_0_0_1; -.
DR OrthoDB; 2783360at2759; -.
DR PhylomeDB; A0A0A2JYW0; -.
DR Proteomes; UP000030143; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010107; Glutamate_decarboxylase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF6; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361171};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU361171};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transferase {ECO:0000313|EMBL:KGO59833.1}.
FT DOMAIN 530..744
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|Pfam:PF12706"
FT REGION 480..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 785 AA; 89163 MW; 6AC193E9358C7354 CRC64;
MVHLAKVKKD NEVLPSVREI DSIPSLETND YDTNVYGSHF AADHMPQHEM PEGEMPRQVA
ARMIKDELSL DGNPKLNLAS FVTTYMEEEI EEIMTEAFSK NFIDYEEYPH SAEIQNRCVN
MIARLFNVPT DSDSENAMGT STIGSSEAIM LGTLAMKKRW QNKRKAEGKD YSRPNIVMNS
AVQVCWEKAA RYFDIEEKYV FCTDTRFVID PKEAVNLVDE NTIGICAILG TTYTGEYEDI
KAINDLLVER NIDCPIHVDA ASGGFVAPFI TPDLEWDFRL EKVVSINVSG HKYGLVYPGV
GWVIWRSPEF LPQELVFNIN YLGADQASFT LNFSKGASHV IGQYYQLIRL GKHGYRAIMT
NLTRISDYLS SEFAKMGMVI LSETHGRGLP LVAWRLPTNN GRVYDEFAVA HQLRERGWIV
PAYTMAPHSE KLQMMRIVIR EDFSMNRCDS LIQDFKLAIE TLDAMDKSMI AKYRTHMQNH
RNHPRHQSRA HPHYMGEKHS LQGKDGKTHG PNFLHAGDHV HLGPGMSSER LTDPAINLHD
LPQIDLVLLS HYHEDHFDKK VEASLRRDLP IITTPHAKKY LTSKKQDSFT SVSALDPFEQ
IEVSIEGTDG PGPPQLRVTG MPGKHVPPKR VVEKLNTLAN VFPPTNGWML ELGHASTNTT
DFYCGYRIYI SGDTLMFDEL REIPKRYAGQ QIDLMLAHLG GTTTPSPLVG RLMEPLAMTV
TMDAEKGLQL TQLIQPDVTI PTHYDDYDEF ASPLEDFRRT MEVAGLLDKV VFLNRRDQYC
FRVRR
//
