ID A0A1Q8CA86_9PSEU Unreviewed; 489 AA.
AC A0A1Q8CA86;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Amino acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BU204_30660 {ECO:0000313|EMBL:OLF11287.1};
OS Actinophytocola xanthii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF11287.1, ECO:0000313|Proteomes:UP000185596};
RN [1] {ECO:0000313|EMBL:OLF11287.1, ECO:0000313|Proteomes:UP000185596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-183 {ECO:0000313|EMBL:OLF11287.1,
RC ECO:0000313|Proteomes:UP000185596};
RA Wang W., Yuan L.;
RT "The draft genome sequence of Actinophytocola sp. 11-183.";
RL Submitted (DEC-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:OLF11287.1}.
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DR EMBL; MSIE01000069; OLF11287.1; -; Genomic_DNA.
DR RefSeq; WP_075129275.1; NZ_MSIE01000069.1.
DR AlphaFoldDB; A0A1Q8CA86; -.
DR STRING; 1912961.BU204_30660; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000185596; 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; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF70; MIP05841P; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000185596}.
FT MOD_RES 301
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 489 AA; 52909 MW; BC74A69592E620F2 CRC64;
MSERVGDWAP AEFERHGREL LAMVREHFES VREVPVTVPR TSAELMDALR APLPEAGEDF
ARVLADTRDR VLPHVVHWNH PSFHAYFANS ASFPGVLAET LTAAMNVNAM LWKSGPAASA
LERVVLDWVA ELVGYPAGAD SVLVNGASLA TLYALAAARD AALGDDVRVN GVPAGATLRV
YTSEQAHSSV DKAAITLGIG QANVVRLPVD EHYRLRPEVL EEAIRRDLAA GAVPVAVVAT
VGTTSVGAAD PVAPVAEVCA RHGVWLHVDA AFGGFWRLAP SLTDAVEDLS PADSLVVNPH
KCLYVPMEAT VLHCRRRGAL ARTFRLVPEY LTSHQDADTV DFMDLSPQLG RSFRALKLWW
VIRSFGRAGL ARRLENSVGQ ARWLRASVER HPDWHCPVTS LYPLVCLRFE PAALRGRRAE
VDALNAAVVE EVNASGSAFV SHAVVEEGYV IRVSIGNIHT THEDVERLWE LLTAVAARLS
PAPAASPAA
//