ID A0A2G8E1R7_9GAMM Unreviewed; 519 AA.
AC A0A2G8E1R7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:PIJ68483.1};
GN ORFNames=BK416_16445 {ECO:0000313|EMBL:PIJ68483.1};
OS Erwinia sp. OLSSP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1912096 {ECO:0000313|EMBL:PIJ68483.1, ECO:0000313|Proteomes:UP000229786};
RN [1] {ECO:0000313|EMBL:PIJ68483.1, ECO:0000313|Proteomes:UP000229786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLSSP12 {ECO:0000313|EMBL:PIJ68483.1,
RC ECO:0000313|Proteomes:UP000229786};
RX PubMed=29067021; DOI=10.3389/fmicb.2017.01969;
RA Chen X., Hitchings M.D., Mendoza J.E., Balanza V., Facey P.D., Dyson P.J.,
RA Bielza P., Del Sol R.;
RT "Comparative Genomics of Facultative Bacterial Symbionts Isolated from
RT European Orius Species Reveals an Ancestral Symbiotic Association.";
RL Front. Microbiol. 8:1969-1969(2017).
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|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:PIJ68483.1}.
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DR EMBL; MNCH01000053; PIJ68483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8E1R7; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000229786; 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 CDD; cd06450; DOPA_deC_like; 1.
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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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:UP000229786}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 519 AA; 57197 MW; 45F4E2D42FAB65D5 CRC64;
MDLRSQNQPL HSLHTSSHPP TPYLQGTIFN DQQLSAWNKQ TQDVLALMTR TVKAVEKPFS
GIFPNELAQA FTGVDLEKPL GSNEAALAEL SELYLRDAVW FHHPKYMAHL NCPVVLPSLL
AEQVMAAVNS SVDTWDQSAG GTLIEQKVID WTLNRIGLPA DADGIFTSGG TQSNLMAMLL
ARDSWCALHH PGRLIKQKGL PPEAGRWRVF TSSLSHFSIQ KSMAILGLGY DAVISVDHDE
NYRMDTAHLE REIQRCHQEG LIPIAVVATS GTTDFGSIDP LGNISALCKQ YGLWMHVDAA
YGCGLLVSEK HAQLLAGIET ADSVTVDYHK SFFQTVSCGA FFVRNKQNLS HVTHHADYLN
PLSAQQEGTP NLVNKSIQTT RRFDALKMWL TLRIMGPDAL GKAFDTLIAL TQTAHARLSA
HPSIEVLHAP ELTTQVFRYL PRSSADDEQV DAINAAIRKA LFRSGNAVIA GTKVNGRQYL
KFTLLNPATT VEDIDDVIAL IVHYGREQLR DPALNVVNQ
//
