ID A0A0C9MWB6_9FUNG Unreviewed; 521 AA.
AC A0A0C9MWB6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=MAM1_0123d05931 {ECO:0000313|EMBL:GAN06448.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06448.1};
RN [1] {ECO:0000313|EMBL:GAN06448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06448.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; DF836412; GAN06448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MWB6; -.
DR STRING; 91626.A0A0C9MWB6; -.
DR OrthoDB; 2783360at2759; -.
DR Proteomes; UP000053815; 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; 3.90.1150.160; -; 1.
DR Gene3D; 4.10.280.50; -; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43321:SF6; GLUTAMATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 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:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT REGION 476..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 521 AA; 58614 MW; 1FE093B44AFBF5A7 CRC64;
MVFLSNAISN ARIEASNSQG ELHHESVGTT IYGTRWASQD IPRQRRYRFE MPQEEMPSNV
AYRLIKDDLA LDGNPALNLA TFVTTYMEEE AEKLMTENLS KNFIDYEEYP QSVELCNRCV
NMIARLYHAP MHSAEEEALG CSTVGSSEAI ILATLAMKRR WQNARKEKGL PYDNPNLVLG
ANCQVAWHKA IRYLEIEPRE VECTEELLYM DPHKAVELVD ENTIGVCAIL GSTYTGHYED
VKTLNTLLEA KNEQNGWDIG IHVDAASGGF VAPFVVPDLE WDFRLSRVVS INVSGHKYGL
TYAGIGWAVW RSAEYLPKSL IFNINYLGSD QASFTLNFSK GAAHVIAQYY VMIRLGQAGF
QKIMGNLTAT ADHLADKLKA TGRFTIMSES SGRGLPLVAF RLNKKHHYNE FDISAKLRER
GWIVPAYTMA PNVEHLKMLR VVVREDFSRS RCEILVKDIL AALHSLDEVD ELTIEKKREH
HSKHSHSSVY NSNPNKPASK ASKDAEANAE QDPKKPAQGI C
//
