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Database: UniProt
Entry: A0A0Y0NYD0_9MICO
LinkDB: A0A0Y0NYD0_9MICO
Original site: A0A0Y0NYD0_9MICO 
ID   A0A0Y0NYD0_9MICO        Unreviewed;       460 AA.
AC   A0A0Y0NYD0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=AWU67_14005 {ECO:0000313|EMBL:AMB59789.1};
OS   Microterricola viridarii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microterricola.
OX   NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB59789.1, ECO:0000313|Proteomes:UP000058305};
RN   [1] {ECO:0000313|EMBL:AMB59789.1, ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB59789.1,
RC   ECO:0000313|Proteomes:UP000058305};
RX   PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA   Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT   isolated from Sikkim Himalaya.";
RL   J. Biotechnol. 222:17-18(2016).
RN   [2] {ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA   Kumar R., Singh D., Swarnkar M.K.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT   Sikkim Himalaya.";
RL   Submitted (JAN-2016) 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|ARBA:ARBA00000018,
CC         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; CP014145; AMB59789.1; -; Genomic_DNA.
DR   RefSeq; WP_067230340.1; NZ_CP014145.1.
DR   AlphaFoldDB; A0A0Y0NYD0; -.
DR   KEGG; mvd:AWU67_14005; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000058305; Chromosome.
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:SF3; 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:UP000058305}.
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   460 AA;  50241 MW;  7EBE2C84F22E6780 CRC64;
     MSQNQPKPHD YAPAYTDGLS REKHPLLRLA EEPVDPGSAY RFIHDELLLD GSSRLNLATF
     VTTWMDPEAD KLMAESFDKN MIDKDEYPAT AAIEGRCVSI VADLFNAPGL DPDDPRSATG
     VSTIGSSEAV MLAGLAMKWR WRAARAATGA DQSRPKLIMG SNVQVVWEKF CRYFDVEPVY
     LPMEPGRYVI TPEQVVAAVD ENTIGVVAIL GTTFTGELEP VADIAAALDE LAGNGGPDVP
     IHVDGASGAF VVPFLDPDLK WDFRLPRVVS INASGHKYGL TYPGIGFVVW RSPEHLPDEL
     VFRVNYLGGD MPTFTLNFSR PGNQVIGQYY NFLRLGRGGY RAVMETLRDT AVEISGRLAE
     IPQLAVITDG SAIPVISFEV TPDAGFTVFE VSHELRAAGW QVPAYTMPAD AEDVAVLRIV
     VRDGFNTELG RMLTDAVVTA CRELTGREGG ARPQRSHFAH
//
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