PPAT_STAAR
ID PPAT_STAAR Reviewed; 395 AA.
AC Q6GJB8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase;
DE EC=2.3.1.-;
GN OrderedLocusNames=SAR0555;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG39576.1; -; Genomic_DNA.
DR RefSeq; WP_000250820.1; NC_002952.2.
DR AlphaFoldDB; Q6GJB8; -.
DR SMR; Q6GJB8; -.
DR KEGG; sar:SAR0555; -.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR OrthoDB; 479874at2; -.
DR Proteomes; UP000000596; 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_0000163840"
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; 42848 MW; 6E7C5FBA51D5C6FA 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 MASTELHDKL
WDNAQYLKNG LSKLGYDTGE SETPITPVII GEEKTTQEFS KRLKDEGVYV KSIVFPTVPR
GTGRVRNMPT AAHTKDMLDE AIAAYEKVGK EMNLI