ID A0A0M2LUI4_9MICO Unreviewed; 466 AA.
AC A0A0M2LUI4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:KKI21145.1};
GN ORFNames=XM48_06075 {ECO:0000313|EMBL:KKI21145.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI21145.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI21145.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI21145.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:KKI21145.1}.
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DR EMBL; LAYO01000086; KKI21145.1; -; Genomic_DNA.
DR RefSeq; WP_046454941.1; NZ_LAYO01000086.1.
DR AlphaFoldDB; A0A0M2LUI4; -.
DR STRING; 1642040.XM48_06075; -.
DR PATRIC; fig|1642040.3.peg.1390; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
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:UP000033836}.
FT MOD_RES 302
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 466 AA; 49917 MW; 0CBE1175BE4417E2 CRC64;
MTAEADPNAH TRMHSVSEET RSIVDLVLDY SRRRLLATDT PLDHASSPGE LTRLAGRTIS
EEGIGASRAL AAFEMVLAPA CITTDHPQYL SFIPSAPSKA AMAFDLVVSA SALYGGSWLE
GSGAVHAENE VLTWLAGEFG LPAGAGGVFV QGGTIGNLSA LVAARDTARR ARTAAGLPAR
PEGGWAVVCS AEAHSSVKSA AEIMDVDVIA VPGGDTGSLS AAAVREALES DGERVFAVVA
TGGSTNFGIV DDIAGVAALK DDFDFWLHVD GAYGLTAILS PLARHHFAGV ERADSVIVDP
HKWLFAPYDV CALIYRDPEN GRLAHTQHAE YLDVLTEQAA YDPSDYSIQL TRRPRGLPLW
FSLATYGAAT YRDAVTHSIA LARRIADEIE RRPGFSLVRD PQLSVVVFER DGWSKADYER
WSDQLLEDQQ AFVVPSSHAG RTNARFAIVN PLTTFEQLTA ILDSMK
//
