ID A0A136PUM4_9ACTN Unreviewed; 518 AA.
AC A0A136PUM4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KXK62085.1};
GN ORFNames=AWW66_10045 {ECO:0000313|EMBL:KXK62085.1};
OS Micromonospora rosaria.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK62085.1, ECO:0000313|Proteomes:UP000070620};
RN [1] {ECO:0000313|EMBL:KXK62085.1, ECO:0000313|Proteomes:UP000070620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 803 {ECO:0000313|EMBL:KXK62085.1,
RC ECO:0000313|Proteomes:UP000070620};
RA Yang H., He X., Zhu D.;
RT "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT which can produce antibacterial substance rosamicin.";
RL Submitted (JAN-2016) 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:KXK62085.1}.
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DR EMBL; LRQV01000026; KXK62085.1; -; Genomic_DNA.
DR RefSeq; WP_067363193.1; NZ_LRQV01000026.1.
DR AlphaFoldDB; A0A136PUM4; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000070620; 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 CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1650.10; PLP-dependent transferases; 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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000070620}.
FT MOD_RES 324
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 518 AA; 55482 MW; 65379E3B489A1212 CRC64;
MSLSGQPAEV APARPATGRG YLFSNGTVDD YRQVVAAGIE RVATRVAGTD RPFTGITPAE
LAPEVAAVDL DAPLAGTAAA LDELEDLYLR DAVWFHHPRY LAHLNCPVVI PALLGEAILT
AVNSSVDTWD QSAGATLIER RLVDWTAQRI GLGPAADGVF TSGGTQSNLQ ALLIAREEAC
ARAVVPGAGP TPTRAELLPR LRILASTAGH FSVQKSATLL GLAPEAVVTV ATDARRRMDP
AALAREIERC QRQGLVVMAV VATAGTTDFG SIDPLPAIAD ACAATGVRLH VDAAYGCGLL
VSRTRRNLLD GIERADSVTV DYHKSFFQPV SSSALLVRDR AVLRHCTYHA DYLNPARAVE
ERIPNQVDKS LQTTRRFDAL KLWLTLRIMG PDALGDLFDE VVDRAAEAWR MLDVDPRFEV
VTRSQLSTVV FRWLPGGECG PADGDLVDAA NRYAREALAA SGAGMVAATT VDGRQYLKFT
LLNPETTGAD VAYVLDLVAA HARRYVREHR PAALSCPV
//
