SBNA_STAA8
ID SBNA_STAA8 Reviewed; 326 AA.
AC Q2G1N3; Q6X7U7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
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:0000269|PubMed:24485762};
DE AltName: Full=Staphyloferrin B biosynthesis protein SbnA {ECO:0000305};
GN Name=sbnA {ECO:0000303|PubMed:14688077}; OrderedLocusNames=SAOUHSC_00075;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, NOMENCLATURE, AND INDUCTION.
RX PubMed=14688077; DOI=10.1128/iai.72.1.29-37.2004;
RA Dale S.E., Doherty-Kirby A., Lajoie G., Heinrichs D.E.;
RT "Role of siderophore biosynthesis in virulence of Staphylococcus aureus:
RT identification and characterization of genes involved in production of a
RT siderophore.";
RL Infect. Immun. 72:29-37(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
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
RL D.C. (2006).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=21906287; DOI=10.1186/1471-2180-11-199;
RA Beasley F.C., Cheung J., Heinrichs D.E.;
RT "Mutation of L-2,3-diaminopropionic acid synthase genes blocks
RT staphyloferrin B synthesis in Staphylococcus aureus.";
RL BMC Microbiol. 11:199-199(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=24485762; DOI=10.1016/j.chembiol.2013.12.011;
RA Kobylarz M.J., Grigg J.C., Takayama S.J., Rai D.K., Heinrichs D.E.,
RA Murphy M.E.;
RT "Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic
RT precursor.";
RL Chem. Biol. 21:379-388(2014).
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:0000269|PubMed:14688077,
CC ECO:0000269|PubMed:21906287, ECO:0000269|PubMed:24485762}.
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:0000269|PubMed:24485762};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52385;
CC Evidence={ECO:0000269|PubMed:24485762};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24485762};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:21906287}.
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:0000269|PubMed:14688077}.
CC -!- DISRUPTION PHENOTYPE: Mutation results in abrogation of synthesis of
CC staphyloferrin B. {ECO:0000269|PubMed:21906287}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. SbnA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD29258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY251022; AAP82063.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29258.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000570808.1; NZ_LS483365.1.
DR RefSeq; YP_498675.1; NC_007795.1.
DR AlphaFoldDB; Q2G1N3; -.
DR SMR; Q2G1N3; -.
DR STRING; 1280.SAXN108_0101; -.
DR EnsemblBacteria; ABD29258; ABD29258; SAOUHSC_00075.
DR GeneID; 3919453; -.
DR KEGG; sao:SAOUHSC_00075; -.
DR PATRIC; fig|93061.5.peg.64; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_9; -.
DR BioCyc; MetaCyc:G1I0R-69-MON; -.
DR BRENDA; 2.5.1.140; 3352.
DR PRO; PR:Q2G1N3; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..326
FT /note="N-(2-amino-2-carboxyethyl)-L-glutamate synthase"
FT /id="PRO_0000395023"
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
