ID A0A2G1XND0_STRCJ Unreviewed; 333 AA.
AC A0A2G1XND0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BLA24_05675 {ECO:0000313|EMBL:PHQ52755.1}, CYQ11_02140
GN {ECO:0000313|EMBL:PPT11854.1};
OS Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces cinnamoneus group.
OX NCBI_TaxID=53446 {ECO:0000313|EMBL:PHQ52755.1, ECO:0000313|Proteomes:UP000222531};
RN [1] {ECO:0000313|EMBL:PHQ52755.1, ECO:0000313|Proteomes:UP000222531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21532 {ECO:0000313|EMBL:PHQ52755.1,
RC ECO:0000313|Proteomes:UP000222531};
RX PubMed=29053243;
RA Patteson J., Cai W., Johnson R.A., Santa Maria K., Li B.;
RT "Identification of the Biosynthetic Pathway for the Antibiotic
RT Bicyclomycin.";
RL Biochemistry 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:PPT11854.1, ECO:0000313|Proteomes:UP000239771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41675 {ECO:0000313|EMBL:PPT11854.1,
RC ECO:0000313|Proteomes:UP000239771};
RA Vior N.M., Lacret R., Chandra G., Dorai-Raj S., Trick M., Truman A.W.;
RT "Discovery and biosynthesis of the antibiotic bicyclomycin in distant
RT bacterial classes.";
RL Submitted (DEC-2017) 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}.
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:PHQ52755.1}.
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DR EMBL; NHZO01000072; PHQ52755.1; -; Genomic_DNA.
DR EMBL; PKFQ01000001; PPT11854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1XND0; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000222531; Unassembled WGS sequence.
DR Proteomes; UP000239771; 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:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000222531}.
FT REGION 245..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 333 AA; 35306 MW; 80C14AC166786EB0 CRC64;
MNERAMREAG RHAIDLVIDR MTTPGSRPPC HAPSPGALRS ALDEPLPFAV VATLGTTGTT
GTTGTTGTGT VDPLDHLADV CQEEGLWLHV DGAHGAAVAG TSRGHHLRNA LGRADSLTVD
PHKWLFQPYE IGCVLLRRPE LLPETFGVAR HALDQGYLRP AHPAAPAREE VNLSAYGPQQ
SRGLRALKLW LSLKTFGAGA FRRAVEQGAA LAEYAAGLVE THPELELVTP PSLAILTFRY
RLGTRPRHGT PTRRRHTSAE GCAPTAGPSS SPPRCEEPPC YACAPSTPPA PVPTSRTCWT
WSPVTAATPG ATSAAPDRPP RQTITSVDGP VIS
//
