ID A0A0Q9TJ26_9ACTN Unreviewed; 475 AA.
AC A0A0Q9TJ26;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KRF34501.1};
GN ORFNames=ASG94_17055 {ECO:0000313|EMBL:KRF34501.1};
OS Nocardioides sp. Soil805.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736416 {ECO:0000313|EMBL:KRF34501.1, ECO:0000313|Proteomes:UP000051356};
RN [1] {ECO:0000313|EMBL:KRF34501.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34501.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF34501.1, ECO:0000313|Proteomes:UP000051356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil805 {ECO:0000313|EMBL:KRF34501.1,
RC ECO:0000313|Proteomes:UP000051356};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRF34501.1}.
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DR EMBL; LMSU01000003; KRF34501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9TJ26; -.
DR STRING; 1736416.ASG94_17055; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000051356; 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:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 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}.
FT MOD_RES 303
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 475 AA; 51346 MW; 5D0145A5E3080E21 CRC64;
MSPEEFRRQG HAAIDWIADY WASLDDLPVL ARVAPGDVRR ALPAAPPEQA EGFEALLADL
DEVVVPGLTH WQHPRYFAYF PANSSPAAIL GDLLSSGIGA QGMIWATSPA VTEVEQVVVD
WLAQALGLPE QFRHGAPGPG GGVIQDTAST ATFTALLAAL HAASGGRARD AGLGDTRWTL
YGSSQAHSSL VKAAMMAGLG SESVRMVDVD PATQAMDVRS LERMLAEDID DGCRPVFVQA
CVGTTSTGAV DDVQAIAEAL DGVGAWLHVD AAWAGVAAVC PEHRDTLTRG LHLAQSLVTN
PHKWLLTTFD CSVLWVPDRE SLTGALSLTP EYLRNAASES GEVVDYRDWH PQLGRRFRSL
KLWAVLRTYG LEGLRAHIRE GVELARRVEE HVLDDDRFEL VTPRSLSLVV FRALAGDEET
MAIMERVNAS GVAYLSHTRV EGRAAIRWAV GSWRTTAADI DRTWAALTEV AARPE
//
