ID A0A0Q7ABU7_9BURK Unreviewed; 493 AA.
AC A0A0Q7ABU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KQW37708.1};
GN ORFNames=ASC76_06280 {ECO:0000313|EMBL:KQW37708.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW37708.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW37708.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW37708.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW37708.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW37708.1,
RC ECO:0000313|Proteomes:UP000051611};
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|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:KQW37708.1}.
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DR EMBL; LMDS01000004; KQW37708.1; -; Genomic_DNA.
DR RefSeq; WP_056464062.1; NZ_LMDS01000004.1.
DR AlphaFoldDB; A0A0Q7ABU7; -.
DR STRING; 1736528.ASC76_06280; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000051611; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.170; -; 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 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:UP000051611}.
FT MOD_RES 293
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 493 AA; 53499 MW; E7C5C1843E7989A4 CRC64;
MSTGHAETGR LQDLLSRVGA GLDEFLRFEH PDALHPGRRW REHLEIALPR AGIGIDRVTE
ELVRHVIPNG SSIPRPGFSS FITTGAATAA TLASTAASIA SPQRYGHTAF NLLEELSLRW
LADMFGLNAM QGIYSSGGSV ANLLALGAAR QSTFERLGQD PAAEGVGRRV GVYASTETHH
TIQRSAGVLG LGRQAVRPID CDRDGRMRVD ALRQSIGDDL RAGIQPMAIV GNAGTTNRGA
IDPLSALGRV AREHGIWFHV DGAYGLPGVL DERVAPLYQG LELADSVIVD PHKWLGAAVG
IGATFVRDRE LLRRAFTQEP APYLEGSMAP GASDASAFQH SMDNFGLPYY DLGVELSAPC
RGVVVWALIR EIGVAGMRDR IRRHIDMAAH IAQLARTHPN LELMQEPTLS ICCFRYVAPG
VNDLDLLNQR LHRRLVHENR NMPSTTRLNG SLALRPCFVG ERSGMDHARA LVADVLRIGA
ELVTDTDICS PRR
//
