SBNA_STAA2
ID SBNA_STAA2 Reviewed; 326 AA.
AC A6TXQ1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=SaurJH1_0107;
OS Staphylococcus aureus (strain JH1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=359787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JH1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT JH1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000736; ABR50969.1; -; Genomic_DNA.
DR RefSeq; WP_000570808.1; NC_009632.1.
DR AlphaFoldDB; A6TXQ1; -.
DR SMR; A6TXQ1; -.
DR KEGG; sah:SaurJH1_0107; -.
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_0000395014"
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