ID   SBNA_STAAB              Reviewed;         326 AA.
AC   Q2YUU0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=SAB0055;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI79743.1; -; Genomic_DNA.
DR   RefSeq; WP_000570810.1; NC_007622.1.
DR   AlphaFoldDB; Q2YUU0; -.
DR   SMR; Q2YUU0; -.
DR   KEGG; sab:SAB0055; -.
DR   HOGENOM; CLU_021018_1_0_9; -.
DR   OMA; GSWCPDQ; -.
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_0000395011"
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;  35995 MW;  21671D5F66E7F8E9 CRC64;
     MIEKSQACHD SLLDSVGQTP MVQLHQLFPK HEVFAKLEYM NPGGSMKDRP AKYIIEHGIK
     HGLITENTHL IESTSGNLGI ALAMIAKIKG LKLTCVVDPK ISPTNLKIIK SYGVNVEMVE
     EPDAHGGYLM TRIAKVQELL ATIEDAYWIN QYANELNWQS HYHGAGTEIV ETIKQPIDYF
     VAPVSTTGSI MGMSRKIKEV HPNVQIVAVD AKGSVIFGDK PINRELPGIG ASRVPEILNR
     SEINQVIHVD DYQSALGCRK LIDYEGIFAG GSTGSIIVAI EQLITSIEEG ATIVTILPDR
     GDRYLDLVYS DTWLEKMKSR QGVKSE