ID   Q2G1Y4_STAA8            Unreviewed;       445 AA.
AC   Q2G1Y4;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Aspartate aminotransferase family protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SAOUHSC_02924 {ECO:0000313|EMBL:ABD31919.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD31919.1, 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   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000253; ABD31919.1; -; Genomic_DNA.
DR   RefSeq; WP_000030057.1; NZ_LS483365.1.
DR   RefSeq; YP_501377.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1Y4; -.
DR   SMR; Q2G1Y4; -.
DR   STRING; 93061.SAOUHSC_02924; -.
DR   PaxDb; 1280-SAXN108_2873; -.
DR   GeneID; 3921375; -.
DR   KEGG; sao:SAOUHSC_02924; -.
DR   PATRIC; fig|93061.5.peg.2643; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008816}.
SQ   SEQUENCE   445 AA;  49082 MW;  CAC0847B5967969D CRC64;
     MSKAHQLIQE DEHYFAKSGR IKYYPLVIDH GYGATLVDIE GKTYIDLLSS ASSQNVGHAP
     REVTEAIKAQ VDKFIHYTPA YMYHEPLVRL AKKLCEIAPG DFEKRVTFGL TGSDANDGII
     KFARAYTGRP YIISFTNAYH GSTFGSLSMS AISLNMRKHY GPLLNGFYHI PFPDKYRGMY
     EQPQANSVEE YLAPLKEMFA KYVPADEVAC IVIETIQGDG GLLEPVPGYF EALEKICREH
     GILIAVDDIQ QGFGRTGTWS SVSHFNFTPD LITFGKSLAG GMPMSAIVGR KEIMNCLEAP
     AHLFTTGANP VSCEAALATI QMIEDQSLLQ ASAEKGEYVR KRMDQWVSKY NSVGDVRGKG
     LSIGIDIVSD KKLKTRDASA ALKICNYCFE HGVVIIAVAG NVLRFQPPLV ITYEQLDTAL
     NTIEDALTAL EAGNLDQYDI SGQGW
//