ID A0A014NSR1_9GAMM Unreviewed; 490 AA.
AC A0A014NSR1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:EXU76900.1};
GN ORFNames=BG55_02540 {ECO:0000313|EMBL:EXU76900.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU76900.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU76900.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU76900.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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|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:EXU76900.1}.
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DR EMBL; JFHN01000020; EXU76900.1; -; Genomic_DNA.
DR RefSeq; WP_034934015.1; NZ_JFHN01000020.1.
DR AlphaFoldDB; A0A014NSR1; -.
DR STRING; 69222.BG55_02540; -.
DR PATRIC; fig|69222.5.peg.535; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000019918; 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:UP000019918}.
FT MOD_RES 307
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 490 AA; 53400 MW; B883A70694990141 CRC64;
MSRSNPILAA SAQSTEAYQQ AIAQTSEAVV QWLQQPEMYQ GKSVAELRER IRLDFTPQGL
GNQAAIGRAV EYFLKDSLSV HHPQCVAHLH CPSLVISQAA EVLINATNQS MDSWDQSPSA
TIIEMKLIEW LRTQVGYQAG DAGVFTSGGT QSNLMGLMLA RDAFFARQGH SVQQDGLPGD
LKKIRVMCSE NAHFSVQKNM ALMGLGYQSV TLVKTDSCAR MDVNDLAEKV AQAQARGEQI
LAIVATAGTT DAGAIDPLRD IAALAAKHHI WLHVDAAWGG ALLLSEQYRH YLDGIELVDS
ITLDFHKQFF QTISCGAFLL KEARHYELMR YQAAYLNSEF DEAHGVPNLV SKSLQTTRRF
DALKLWMGLE ALGQKQYAEI IDHGVSLAQQ VAGYVSDHSA LQLVMQPQLA SVLFRYAPAQ
LTDSGEAAVA MLNQRIGDAL LDSGKANVGV TEHNGVTCLK LTLLNPTVTL DDIKVLLSLV
ESTAAQLPQA
//
