ID A0A0Q7DQY9_9BURK Unreviewed; 495 AA.
AC A0A0Q7DQY9;
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:KQW75272.1};
GN ORFNames=ASC67_18180 {ECO:0000313|EMBL:KQW75272.1};
OS Methylibium sp. Root1272.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1736441 {ECO:0000313|EMBL:KQW75272.1, ECO:0000313|Proteomes:UP000053968};
RN [1] {ECO:0000313|EMBL:KQW75272.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW75272.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW75272.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW75272.1,
RC ECO:0000313|Proteomes:UP000053968};
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:KQW75272.1}.
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DR EMBL; LMDY01000002; KQW75272.1; -; Genomic_DNA.
DR RefSeq; WP_056315424.1; NZ_LMDY01000002.1.
DR AlphaFoldDB; A0A0Q7DQY9; -.
DR STRING; 1736441.ASC67_18180; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000053968; 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 InterPro; IPR021115; Pyridoxal-P_BS.
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.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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 313
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 495 AA; 52140 MW; D73D51F099DE5494 CRC64;
MPIEPPEPEP PAREAALAMA PAQFRALGHA LVDRIADMMA ALPQRPVSHG ETPAELRALV
GDGPLPTGGA DPAALLDGAA TLLFEHSLRS SHPRFHGYIA ASPAPIGVLA ELLAAALNAN
VALWHAAPVA SEIEAQTVRW LAELVGYPAG CGGLLTSGGN LANLVALLAA RRAARPAVRE
QGLCGAPPLA VYASTQTHAW LHKAVDIAGL GLQAVRWIPT DARQRLDVDA LGARIEADLA
AGVQPLMAVG TAGTVSTGAI DPLPAMAALC RRHGLWFHVD GAYGAPAACL GDAAPADLPG
LREADSVALD PHKWLYAPIE AGCVLVREPR HLLDAFSQRP SYYGAPRDDE GVNFHELGPQ
NTRGFRALKV WLALRMAGRD GYRRMIGDDI ALARRLHERV QATPRLEAGP GGLSIATLRY
RPEPRGAHDD AALDALNRRL LERLQQDGRA WLSPAVVDGR FWLRACIVNF GTGAAEVDAL
PALVLELGDA LGAGA
//
