ID   PPAT_STAAW              Reviewed;         395 AA.
AC   Q8NXY3;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase;
DE            EC=2.3.1.-;
GN   OrderedLocusNames=MW0505;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB94370.1; -; Genomic_DNA.
DR   RefSeq; WP_000250823.1; NC_003923.1.
DR   AlphaFoldDB; Q8NXY3; -.
DR   SMR; Q8NXY3; -.
DR   EnsemblBacteria; BAB94370; BAB94370; BAB94370.
DR   KEGG; sam:MW0505; -.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR010962; AONS_Archaea/Firmicutes.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01825; gly_Cac_T_rel; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..395
FT                   /note="Putative pyridoxal phosphate-dependent
FT                   acyltransferase"
FT                   /id="PRO_0000163842"
FT   BINDING         110..111
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..213
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         240..243
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  42892 MW;  6F894D2AA4C587FC CRC64;
     MVQSLHEFLE ENINYLKENG LYNEIDTIEG ANGPEIKING KSYINLSSNN YLGLATNEDL
     KSAAKAAIDT HGVGAGAVRT INGTLDLHDE LEETLAKFKG TEAAIAYQSG FNCNMAAISA
     VMNKNDAILS DELNHASIID GCRLSKAKII RVNHSDMDDL RAKAKEAVES GQYNKVMYIT
     DGVFSMDGDV AKLPEIVEIA EEFGLLTYVD DAHGSGVMGK GAGTVKHFGL QDKIDFQIGT
     LSKAIGVVGG YVAGTKELID WLKAQSRPFL FSTSLAPGDT KAITEAVKKL MDSTELHDKL
     WDNAQYLKNG LSKLGYDTGE SETPITPVII GDEKTTQEFS KRLKDEGVYV KSIVFPTVPR
     GTGRVRNMPT AAHTKDMLDE AIAAYEKVGK EMKLI