SBNA_STAAE
ID SBNA_STAAE Reviewed; 326 AA.
AC A6QDA0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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, ECO:0000269|PubMed:26794841};
DE AltName: Full=Staphyloferrin B biosynthesis protein SbnA {ECO:0000305};
GN Name=sbnA {ECO:0000303|PubMed:21906287}; OrderedLocusNames=NWMN_0060;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
RN [2]
RP FUNCTION, AND PATHWAY.
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 [3]
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-152 AND
RP PHE-152/GLY-185 IN COMPLEXES WITH PYRIDOXAL 5'-PHOSPHATE AND
RP O-PHOSPHO-L-SERINE, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ARG-132;
RP TYR-152 AND SER-185, AND SUBUNIT.
RX PubMed=26794841; DOI=10.1021/acs.biochem.5b01045;
RA Kobylarz M.J., Grigg J.C., Liu Y., Lee M.S., Heinrichs D.E., Murphy M.E.;
RT "Deciphering the substrate specificity of SbnA, the enzyme catalyzing the
RT first step in staphyloferrin B biosynthesis.";
RL Biochemistry 55:927-939(2016).
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:21906287,
CC 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, ECO:0000269|PubMed:26794841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52385;
CC Evidence={ECO:0000269|PubMed:24485762, ECO:0000269|PubMed:26794841};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:24485762, ECO:0000269|PubMed:26794841};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:21906287}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26794841}.
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; AP009351; BAF66332.1; -; Genomic_DNA.
DR RefSeq; WP_000570808.1; NZ_CP023390.1.
DR PDB; 5D84; X-ray; 1.45 A; A=1-326.
DR PDB; 5D85; X-ray; 1.92 A; A=1-326.
DR PDB; 5D86; X-ray; 1.50 A; A=1-326.
DR PDB; 5D87; X-ray; 1.50 A; A=1-326.
DR PDBsum; 5D84; -.
DR PDBsum; 5D85; -.
DR PDBsum; 5D86; -.
DR PDBsum; 5D87; -.
DR AlphaFoldDB; A6QDA0; -.
DR SMR; A6QDA0; -.
DR EnsemblBacteria; BAF66332; BAF66332; NWMN_0060.
DR KEGG; sae:NWMN_0060; -.
DR HOGENOM; CLU_021018_1_0_9; -.
DR OMA; GSWCPDQ; -.
DR BRENDA; 2.5.1.140; 3352.
DR Proteomes; UP000006386; 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 1: Evidence at protein level;
KW 3D-structure; Pyridoxal phosphate; Transferase.
FT CHAIN 1..326
FT /note="N-(2-amino-2-carboxyethyl)-L-glutamate synthase"
FT /id="PRO_0000395024"
FT BINDING 77
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:26794841"
FT BINDING 185..189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:26794841"
FT BINDING 272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:26794841"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:26794841"
FT MUTAGEN 132
FT /note="R->A: No detectable enzyme activity. Does not form
FT pyridoxal 5'-phosphate-alpha-aminoacrylate reaction
FT intermediate."
FT /evidence="ECO:0000269|PubMed:26794841"
FT MUTAGEN 152
FT /note="Y->F: Very low enzyme activity. Does not form
FT pyridoxal 5'-phosphate-alpha-aminoacrylate reaction
FT intermediate; when associated with G-185."
FT /evidence="ECO:0000269|PubMed:26794841"
FT MUTAGEN 185
FT /note="S->G: 4-5 fold reduction in catalytic efficiency.
FT Does not form pyridoxal 5'-phosphate-alpha-aminoacrylate
FT reaction intermediate; when associated with F-152."
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5D84"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5D84"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5D84"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:5D84"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:5D84"
FT TURN 305..309
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:5D84"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5D86"
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
