ID   Q2FUT9_STAA8            Unreviewed;       337 AA.
AC   Q2FUT9;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase {ECO:0000256|ARBA:ARBA00015148};
GN   OrderedLocusNames=SAOUHSC_03012 {ECO:0000313|EMBL:ABD31998.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD31998.1, ECO:0000313|Proteomes:UP000008816};
RN   [1] {ECO:0000313|Proteomes:UP000008816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL   (2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR   EMBL; CP000253; ABD31998.1; -; Genomic_DNA.
DR   RefSeq; WP_000639183.1; NC_007795.1.
DR   RefSeq; YP_501461.1; NC_007795.1.
DR   AlphaFoldDB; Q2FUT9; -.
DR   SMR; Q2FUT9; -.
DR   STRING; 93061.SAOUHSC_03012; -.
DR   PaxDb; 93061-SAOUHSC_03012; -.
DR   GeneID; 3921493; -.
DR   KEGG; sao:SAOUHSC_03012; -.
DR   PATRIC; fig|93061.5.peg.2720; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_9; -.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-ARBA.
DR   CDD; cd00609; AAT_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ABD31998.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD31998.1}.
FT   DOMAIN          22..309
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   337 AA;  38241 MW;  DB96854C55CFD799 CRC64;
     MIYIDKNESP VTPLDEKTMT SIISATPYNL YPDAAYEQFK EAYAKFYGLS PEQIIAGNGS
     DELIQKLMLI MPEGPALTLN PDFFMYQAYA AQVNREIAFV DAGSDLTFDL ETILTKIDEV
     QPSFFIMSNP HNPSGKQFDT AFLTAIADKM KALNGYFVID EAYLDYGTAY DVELAPHILR
     MRTLSKAFGI AGLRLGVLIS TAGTIKHIQK IEHPYPLNVF TLNIATYIFR HREETRQFLT
     MQRQLAEQLK QIFDTHVADK MSVFPSNANF VLTKGSAAQQ LGQYVYEQGF KPRFYDEPVM
     KGYVRYSIAT ASQLKQLEEI VKEWSAKYDL SKTTKHS
//