ID   A3P4N0_BURP0            Unreviewed;       433 AA.
AC   A3P4N0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Cys/Met metabolism PLP-dependent enzyme {ECO:0000313|EMBL:ABN92821.1};
GN   OrderedLocusNames=BURPS1106A_A1255 {ECO:0000313|EMBL:ABN92821.1};
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN92821.1, ECO:0000313|Proteomes:UP000006738};
RN   [1] {ECO:0000313|Proteomes:UP000006738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) 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|RuleBase:RU362118};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP000573; ABN92821.1; -; Genomic_DNA.
DR   RefSeq; WP_004537268.1; NC_009078.1.
DR   AlphaFoldDB; A3P4N0; -.
DR   GeneID; 56530632; -.
DR   KEGG; bpl:BURPS1106A_A1255; -.
DR   HOGENOM; CLU_018986_2_0_4; -.
DR   Proteomes; UP000006738; Chromosome II.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF86; METHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         241
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   433 AA;  46647 MW;  5CAAF943F84D9103 CRC64;
     MTYSSYHKKD IEGRPLHPET QMMSYGFDPF LSEGAVKPPV FLTSTFAFRS AEDGADFFDI
     VSGRKPLPQG EAAGLVYSRF NHPNLEIVED RLALLDGSEA AVVTSSGMSA ISAIFLAFLR
     PGDQLVQSVP LYGGTETLIA KYFREWGVGA HSIDNGLSPQ AIGAALEAAA QQGPVRLCYV
     ETPANPTNAL IDLDGMRREL DAFEARHGYR PISVCDNTLL GPIFQKPSEH GVDMSVYSLT
     KYVGGHSDLV GGGVTGRRDL VAKVRAVRSA FGSQLDPHSS WMLIRSMETV VLRVKQAART
     ASAVAKWLAT NPHQKVDVYH PELIVDDAYQ AVYKRQCTGA GSTFAFVLNG GRAEAFRFIN
     ALHLFKSAVS LGGTESLICH PASTTHSGVP EAARKAAGVS EGLIRVSIGL EHEEDLIADL
     DHAFRRSGLA TGV
//