SBNA_CUPMC
ID SBNA_CUPMC Reviewed; 341 AA.
AC Q44004; Q1LPC3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
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=Rmet_1117;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8808942; DOI=10.1128/jb.178.18.5499-5507.1996;
RA Gilis A., Khan M.A., Cornelis P., Meyer J.M., Mergeay M., van der Lelie D.;
RT "Siderophore-mediated iron uptake in Alcaligenes eutrophus CH34 and
RT identification of aleB encoding the ferric iron-alcaligin E receptor.";
RL J. Bacteriol. 178:5499-5507(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
CC -!- FUNCTION: Catalyzes the synthesis of N-((2S)-2-amino-2-carboxyethyl)-L-
CC glutamate (ACEGA) from O-phospho-L-serine and L-glutamate.
CC {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 -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. SbnA subfamily. {ECO:0000305}.
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DR EMBL; X97499; CAA66130.1; -; Genomic_DNA.
DR EMBL; CP000352; ABF08003.1; -; Genomic_DNA.
DR RefSeq; WP_011515904.1; NC_007973.1.
DR AlphaFoldDB; Q44004; -.
DR SMR; Q44004; -.
DR STRING; 266264.Rmet_1117; -.
DR EnsemblBacteria; ABF08003; ABF08003; Rmet_1117.
DR KEGG; rme:Rmet_1117; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_4; -.
DR OMA; GSWCPDQ; -.
DR OrthoDB; 1677960at2; -.
DR Proteomes; UP000002429; 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 3: Inferred from homology;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..341
FT /note="N-(2-amino-2-carboxyethyl)-L-glutamate synthase"
FT /id="PRO_0000167105"
FT BINDING 73
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT BINDING 181..185
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT BINDING 268
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:A6QDA0"
FT CONFLICT 17..18
FT /note="QL -> HV (in Ref. 1; CAA66130)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="QL -> HV (in Ref. 1; CAA66130)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> T (in Ref. 1; CAA66130)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..265
FT /note="GSVLFGQPSQARELPGIGASRVPELLCRDEIDEVIHIDDYTAATACRRLLAR
FT EGIFA -> FPCCSANRRKRASCRALAPRRAGIAVPGRDRRSDPYRRLHRRHGAGACWR
FT RRHLR (in Ref. 1; CAA66130)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="R -> T (in Ref. 1; CAA66130)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 36838 MW; 46EE65F2BBCD5F88 CRC64;
MVCNSIIESI GNTPLVQLRR LFGRADAEVF AKLELLNPAG SVKDRPARYI VEKGLTEGAI
GPHSHVIESS SGNLAIALAM ICGLKGLRFT AVVDPKISPT NLKILRCYGA GIEQVTAKDS
QGGYLETRIE RVRQMLREQR DAIWINQYAN PLNWESHYYG EAAEILAQLA QPADVLVLGV
STSGTVHGIA RRLRKAWPSM RVVGVDAVGS VLFGQPSQAR ELPGIGASRV PELLCRDEID
EVIHIDDYTA ATACRRLLAR EGIFAGGSSG AVVAAIEQVL HATPVSHRPL RILTLFPDRG
ERYLDTVYDD AWLARIAARR AVPNLAALPT VASLIPAGVS A
