YGEA_ECOLI
ID YGEA_ECOLI Reviewed; 230 AA.
AC P03813; Q2M9Z7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Broad specificity amino-acid racemase YgeA {ECO:0000305};
DE EC=5.1.1.10 {ECO:0000269|PubMed:28894939};
GN Name=ygeA; OrderedLocusNames=b2840, JW2808;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6350602; DOI=10.1016/s0022-2836(83)80022-9;
RA Stragier P., Patte J.-C.;
RT "Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli.
RT III. Nucleotide sequence and regulation of the lysR gene.";
RL J. Mol. Biol. 168:333-350(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / JM2433;
RX PubMed=2836407; DOI=10.1016/s0021-9258(18)68433-9;
RA Maiden M.C.J., Jones-Mortimer M.C., Henderson P.J.F.;
RT "The cloning, DNA sequence, and overexpression of the gene araE coding for
RT arabinose-proton symport in Escherichia coli K12.";
RL J. Biol. Chem. 263:8003-8010(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28894939; DOI=10.1007/s00726-017-2486-2;
RA Miyamoto T., Katane M., Saitoh Y., Sekine M., Homma H.;
RT "Identification and characterization of novel broad-spectrum amino acid
RT racemases from Escherichia coli and Bacillus subtilis.";
RL Amino Acids 49:1885-1894(2017).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates. Highest activity is observed with L-homoserine and D-
CC homoserine. Has tenfold lower activity against L-methionine, L-leucine,
CC L-valine and L-histidine. Has low activity with L-norvaline, L-
CC asparagine, D-methionine, L-aminobutyric acid, L-isoleucine, L-serine,
CC L-norleucine, L-alanine, L-glutamine, LL-diaminopimelic acid and L-
CC phenylalanine. Has no activity against ten L-amino acids (Thr, Glu,
CC Asp, Arg, Lys, Tyr, Trp, Orn, Cit and Aad) (PubMed:28894939). D-amino
CC acids might be used as components of peptidoglycan and/or be involved
CC in peptidoglycan metabolism and remodeling (PubMed:28894939).
CC {ECO:0000269|PubMed:28894939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC EC=5.1.1.10; Evidence={ECO:0000269|PubMed:28894939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine = D-homoserine; Xref=Rhea:RHEA:59404,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:143081;
CC Evidence={ECO:0000269|PubMed:28894939};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=171 mM for L-homoserine {ECO:0000269|PubMed:28894939};
CC KM=25.1 mM for D-homoserine {ECO:0000269|PubMed:28894939};
CC Vmax=295 nmol/min/mg enzyme with L-homoserine as substrate
CC {ECO:0000269|PubMed:28894939};
CC Vmax=43.2 nmol/min/mg enzyme with D-homoserine as substrate
CC {ECO:0000269|PubMed:28894939};
CC Note=kcat is 7.84 min(-1) with L-homoserine as substrate. kcat is
CC 1.15 min(-1) with D-homoserine as substrate.
CC {ECO:0000269|PubMed:28894939};
CC pH dependence:
CC Optimum pH is 8.5 with L-homoserine as substrate.
CC {ECO:0000269|PubMed:28894939};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:28894939};
CC -!- INTERACTION:
CC P03813; P77788: nudG; NbExp=2; IntAct=EBI-545190, EBI-545184;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000305}.
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DR EMBL; J03732; AAA23470.1; -; Genomic_DNA.
DR EMBL; J01614; AAA83863.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40487.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75879.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76909.1; -; Genomic_DNA.
DR PIR; A04438; QQECK.
DR RefSeq; NP_417317.1; NC_000913.3.
DR RefSeq; WP_000848659.1; NZ_LN832404.1.
DR AlphaFoldDB; P03813; -.
DR SMR; P03813; -.
DR BioGRID; 4262310; 16.
DR DIP; DIP-12147N; -.
DR IntAct; P03813; 2.
DR STRING; 511145.b2840; -.
DR jPOST; P03813; -.
DR PaxDb; P03813; -.
DR PRIDE; P03813; -.
DR EnsemblBacteria; AAC75879; AAC75879; b2840.
DR EnsemblBacteria; BAE76909; BAE76909; BAE76909.
DR GeneID; 947348; -.
DR KEGG; ecj:JW2808; -.
DR KEGG; eco:b2840; -.
DR PATRIC; fig|511145.12.peg.2938; -.
DR EchoBASE; EB1146; -.
DR eggNOG; COG1794; Bacteria.
DR HOGENOM; CLU_055360_1_0_6; -.
DR InParanoid; P03813; -.
DR OMA; TNTMHLI; -.
DR PhylomeDB; P03813; -.
DR BioCyc; EcoCyc:EG11157-MON; -.
DR BioCyc; MetaCyc:EG11157-MON; -.
DR BRENDA; 5.1.1.10; 2026.
DR PRO; PR:P03813; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0047661; F:amino-acid racemase activity; IDA:EcoCyc.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR InterPro; IPR015942; Asp/Glu/hydantoin_racemase.
DR InterPro; IPR001920; Asp/Glu_race.
DR InterPro; IPR018187; Asp/Glu_racemase_AS_1.
DR InterPro; IPR033134; Asp/Glu_racemase_AS_2.
DR InterPro; IPR004380; Asp_race.
DR PANTHER; PTHR21198:SF7; PTHR21198:SF7; 1.
DR Pfam; PF01177; Asp_Glu_race; 1.
DR SUPFAM; SSF53681; SSF53681; 2.
DR TIGRFAMs; TIGR00035; asp_race; 1.
DR PROSITE; PS00923; ASP_GLU_RACEMASE_1; 1.
DR PROSITE; PS00924; ASP_GLU_RACEMASE_2; 1.
PE 1: Evidence at protein level;
KW Isomerase; Reference proteome.
FT CHAIN 1..230
FT /note="Broad specificity amino-acid racemase YgeA"
FT /id="PRO_0000095537"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
FT BINDING 83..85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A140N890"
SQ SEQUENCE 230 AA; 25248 MW; 370E9549BD37FF61 CRC64;
MKTIGLLGGM SWESTIPYYR LINEGIKQRL GGLHSAQVLL HSVDFHEIEE CQRRGEWDKT
GDILAEAALG LQRAGAEGIV LCTNTMHKVA DAIESRCTLP FLHIADATGR AITGAGMTRV
ALLGTRYTME QDFYRGRLTE QFSINCLIPE ADERAKINQI IFEELCLGQF TEASRAYCAQ
VIARLAEQGA QGVIFGCTEI GLLVPEERSV LPVFDTAAIH AEDAVAFMLS
