ID   SBNA_STAAM              Reviewed;         326 AA.
AC   Q932K9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=N-(2-amino-2-carboxyethyl)-L-glutamate synthase {ECO:0000305};
DE            Short=ACEGA synthase {ECO:0000305};
DE            EC=2.5.1.140 {ECO:0000250|UniProtKB:A6QDA0};
GN   Name=sbnA; OrderedLocusNames=SAV0116;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Catalyzes the synthesis of N-((2S)-2-amino-2-carboxyethyl)-L-
CC       glutamate (ACEGA) from O-phospho-L-serine and L-glutamate. Involved in
CC       the biosynthesis of L-2,3-diaminopropionic acid (L-Dap), a precursor of
CC       staphyloferrin B and antibiotics. {ECO:0000250|UniProtKB:A6QDA0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + O-phospho-L-serine = H(+) + N-[(2S)-2-amino-2-
CC         carboxyethyl]-L-glutamate + phosphate; Xref=Rhea:RHEA:52384,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57524, ChEBI:CHEBI:134610; EC=2.5.1.140;
CC         Evidence={ECO:0000250|UniProtKB:A6QDA0};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:A6QDA0};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:A6QDA0}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A6QDA0}.
CC   -!- INDUCTION: Up-regulated under iron-deficient growth conditions.
CC       Repressed by Fur under iron-rich growth conditions.
CC       {ECO:0000250|UniProtKB:Q2G1N3}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. SbnA subfamily. {ECO:0000305}.
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DR   EMBL; BA000017; BAB56278.1; -; Genomic_DNA.
DR   RefSeq; WP_000570808.1; NC_002758.2.
DR   AlphaFoldDB; Q932K9; -.
DR   SMR; Q932K9; -.
DR   PaxDb; Q932K9; -.
DR   EnsemblBacteria; BAB56278; BAB56278; SAV0116.
DR   KEGG; sav:SAV0116; -.
DR   HOGENOM; CLU_021018_1_0_9; -.
DR   OMA; GSWCPDQ; -.
DR   PhylomeDB; Q932K9; -.
DR   BioCyc; SAUR158878:SAV_RS00715-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR023927; SbnA.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR03945; PLP_SbnA_fam; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..326
FT                   /note="N-(2-amino-2-carboxyethyl)-L-glutamate synthase"
FT                   /id="PRO_0000395020"
FT   BINDING         77
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT   BINDING         185..189
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:A6QDA0"
SQ   SEQUENCE   326 AA;  35897 MW;  E682FB5D5E5F76AF CRC64;
     MIEKSQACHD SLLDSVGQTP MVQLHQLFPK HEVFAKLEYM NPGGSMKDRP AKYIIEHGIK
     HGLITENTHL IESTSGNLGI ALAMIAKIKG LKLTCVVDPK ISPTNLKIIK SYGANVEMVE
     EPDAHGGYLM TRIAKVQELL ATIDDAYWIN QYANELNWQS HYHGAGTEIV ETIKQPIDYF
     VAPVSTTGSI MGMSRKIKEV HPNAQIVAVD AKGSVIFGDK PINRELPGIG ASRVPEILNR
     SEINQVIHVD DYQSALGCRK LIDYEGIFAG GSTGSIIAAI EQLITSIEEG ATIVTILPDR
     GDRYLDLVYS DTWLEKMKSR QGVKSE