ID A0A1H3LQJ8_9PSEU Unreviewed; 459 AA.
AC A0A1H3LQJ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SDY66606.1};
GN ORFNames=SAMN05216215_10329 {ECO:0000313|EMBL:SDY66606.1};
OS Saccharopolyspora shandongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=418495 {ECO:0000313|EMBL:SDY66606.1, ECO:0000313|Proteomes:UP000199529};
RN [1] {ECO:0000313|EMBL:SDY66606.1, ECO:0000313|Proteomes:UP000199529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDY66606.1,
RC ECO:0000313|Proteomes:UP000199529};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; FNOK01000032; SDY66606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3LQJ8; -.
DR STRING; 418495.SAMN05216215_10329; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000199529; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; 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 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}.
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 459 AA; 48681 MW; 5CA4DF356B92B77A CRC64;
MHPKLSEDLA RLPELLDIAR RCAVEALSGI ADRPAAVPPA PPNPESLPDS GVGAEAALER
FQSRWAPGFS GSAGPRYLGF VTGGATPAAV AGDWLTSTFD QNAAAGGDSS ALDLEREATG
WLRELFGLGT AHEGAFVSGA TMSNFVGLAI GREWVGEQLG VSVAQDGVAA LGNVPVLSGS
PHSSVYKALS MLGLGRGCVR EVATLPEREA VDVDRLSAEL AALDGRPAIV VANAGTVNTV
DFDDLRAIAE LRRRFPFWLH VDAAFGGFAA LSPLHTELVA GIDEADSVCA DLHKWLNVPY
DSAIQFTRRR DLQVRVFQNA AAYLGRITED PDFVHLTPEN SRRLRALPAW FTLAAYGRQG
HREIVERDIA LARELGDRIA GMPHLRLLAP VRLNVVCFTL ADDPTAERIG ALARSVAGSG
EAFLTPTVYK GTPGLRAAFS NWRTTGADVG RIAAALRAG
//
