ID A0A170X4N9_9ACTN Unreviewed; 464 AA.
AC A0A170X4N9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:GAT81514.1};
GN ORFNames=STXM2123_2215 {ECO:0000313|EMBL:GAT81514.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT81514.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT81514.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-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|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:GAT81514.1}.
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DR EMBL; BDDR01000011; GAT81514.1; -; Genomic_DNA.
DR RefSeq; WP_067393028.1; NZ_BDDR01000011.1.
DR AlphaFoldDB; A0A170X4N9; -.
DR STRING; 1840095.STXM2123_2215; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000078145; 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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000078145}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 464 AA; 48096 MW; 15FAE14021706B50 CRC64;
MSALPPGDPA RLASGPEGSR TLRPLVHTVL DALDSGRRAR GGPLPAGGPE AVAARVRDAV
GDVLPEHGDP DALRTLVHAL AEGAADPADP LCAAHLHCPP LAVATAADLA ASALNPSLDS
WDQAPAASEL EALVTRALAH EAGLADAVVT TGGTESNQLA LLLARENHGG AVRLVCGANA
HHSLPRAAWL LGLPEPVIVP APAGTVDLAA LHDALTELTG SRGSRGSLVV AATAGTTDAG
LIDPLPEIAG LCAAHGARLH IDAAHGGGLL FSERHRDKLT GLEAAHTVTL DLHKLGWQPV
AAGLLVVRRP RDLDVLHQRA DYLNAGDDTE AGLPDLLGRS LRTTRRPDIL KIAVTLKTLG
RSGLGALVDQ VCARAREFAD LVHDHPGFEL HGRPVISTVL FRPAGATDDA VAVIRRRLLT
EGRAVLGRAR LDGRLWLKAT LLNPETRSED LAALLKQVEG SIPG
//
