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 27-MAR-2024, entry version 94.
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; Bacillota; 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 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 CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR023927; SbnA.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR03945; PLP_SbnA_fam; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF254; N-(2-AMINO-2-CARBOXYETHYL)-L-GLUTAMATE SYNTHASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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
//
