ID A0A0Q6WVW9_9BURK Unreviewed; 477 AA.
AC A0A0Q6WVW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASC87_28225 {ECO:0000313|EMBL:KQV90438.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV90438.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV90438.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV90438.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV90438.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV90438.1,
RC ECO:0000313|Proteomes:UP000051465};
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:KQV90438.1}.
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DR EMBL; LMDI01000036; KQV90438.1; -; Genomic_DNA.
DR RefSeq; WP_056667879.1; NZ_LMDI01000036.1.
DR AlphaFoldDB; A0A0Q6WVW9; -.
DR STRING; 1736433.ASC87_28225; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000051465; 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; 3.90.1150.170; -; 1.
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; 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:SF165; DECARBOXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04980)-RELATED; 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|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051465}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 477 AA; 51848 MW; 7782DC0BCA73E089 CRC64;
MEPTNHENKA LELGGAQLRE LIDRVAQRLE VFVDGIESSP ASREGGVSRL VDEPMPKVGA
PLDDVLDLLF SRVIPSGYNT TSPGFLGYFG GGGIPQAAVA DLIAGTVNRF VGRWAAAPEA
VQLESNVIRW FADMVGYPAT SRGVLTSGGS MSNLTALFTA RQRLLHGQDL RLARFYASDQ
SHFSLRKAAM VCGLPNEAFR EVPTGEDGRM DVDALDRLVR EDRAAGFLPF LVVATGGTFN
TGAVDDVAGI CALARRERLW CHLDAAYGGF FVLTGQGRAL LAGLDQCDSI TLDPHKSFFL
PYGTGALLVR DGRGLKQAHA VDADFYGPLQ DDPDCIDFCS HAMEQTRAWR GLRIWLPLKL
HGIAPFRANL EEKLALAAHA AEALQRIPGI ELVAKPALSV LAFRLVRPGC SPAELQRLNE
RLLAEINRRG HIFLMGSVVR KTYALRMCLL SFRTHIDRLE SGIADVHEAA RSLQPGA
//