YGEA_ECO57
ID YGEA_ECO57 Reviewed; 230 AA.
AC A0A0H3JGH6;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=L-aspartate/glutamate-specific racemase {ECO:0000250|UniProtKB:A0A140N890};
DE Short=L-Asp/Glu-specific racemase {ECO:0000250|UniProtKB:A0A140N890};
DE EC=5.1.1.13 {ECO:0000250|UniProtKB:A0A140N890};
DE EC=5.1.1.3 {ECO:0000250|UniProtKB:A0A140N890};
DE AltName: Full=EcL-DER {ECO:0000303|PubMed:27001440};
GN Name=ygeA {ECO:0000312|EMBL:BAB37120.1};
GN ORFNames=ECpv15279_3665 {ECO:0000312|EMBL:BBC51991.1},
GN ECs_3697 {ECO:0000312|EMBL:BAB37120.1},
GN EFE38_05130 {ECO:0000312|EMBL:RNG11621.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Pv15-279;
RA Ogura Y., Seto K., Morimoto Y., Nakamura K., Gotoh Y., Toyoda A., Itoh T.,
RA Ohnishi M., Hayashi T.;
RT "Genomic characterization of a non-sorbitol-fermenting and b-glucuronidase-
RT positive O157:H7 strain.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / C1-067;
RA Jia M., Yang H.;
RT "Draft genome sequence of Shiga toxin-producing Escherichia coli O157:H7
RT strain C1-067, isolated from feedlot cattle.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:5HQT, ECO:0007744|PDB:5HRA, ECO:0007744|PDB:5HRC}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP L-ASPARTATE AND D-ASPARTATE, AND ACTIVE SITE.
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=27001440; DOI=10.1002/1873-3468.12148;
RA Liu X., Gao F., Ma Y., Liu S., Cui Y., Yuan Z., Kang X.;
RT "Crystal structure and molecular mechanism of an aspartate/glutamate
RT racemase from Escherichiacoli O157.";
RL FEBS Lett. 590:1262-1269(2016).
CC -!- FUNCTION: Exhibits racemase activity for both L-glutamate and L-
CC aspartate. {ECO:0000250|UniProtKB:A0A140N890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate = D-glutamate; Xref=Rhea:RHEA:12813,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29986; EC=5.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:A0A140N890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12814;
CC Evidence={ECO:0000250|UniProtKB:A0A140N890};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate = D-aspartate; Xref=Rhea:RHEA:14973,
CC ChEBI:CHEBI:29990, ChEBI:CHEBI:29991; EC=5.1.1.13;
CC Evidence={ECO:0000250|UniProtKB:A0A140N890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14974;
CC Evidence={ECO:0000250|UniProtKB:A0A140N890};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A140N890}.
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000305}.
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DR EMBL; BA000007; BAB37120.1; -; Genomic_DNA.
DR EMBL; AP018488; BBC51991.1; -; Genomic_DNA.
DR EMBL; RICC01000001; RNG11621.1; -; Genomic_DNA.
DR RefSeq; NP_311724.1; NC_002695.1.
DR RefSeq; WP_000848664.1; NZ_SWKA01000005.1.
DR PDB; 5HQT; X-ray; 1.60 A; A=1-230.
DR PDB; 5HRA; X-ray; 1.60 A; A/B=1-230.
DR PDB; 5HRC; X-ray; 1.76 A; A/B=1-230.
DR PDBsum; 5HQT; -.
DR PDBsum; 5HRA; -.
DR PDBsum; 5HRC; -.
DR AlphaFoldDB; A0A0H3JGH6; -.
DR SMR; A0A0H3JGH6; -.
DR STRING; 155864.EDL933_4021; -.
DR EnsemblBacteria; BAB37120; BAB37120; ECs_3697.
DR GeneID; 66673293; -.
DR GeneID; 916475; -.
DR KEGG; ecs:ECs_3697; -.
DR PATRIC; fig|386585.9.peg.3864; -.
DR eggNOG; COG1794; Bacteria.
DR HOGENOM; CLU_055360_1_0_6; -.
DR OMA; TNTMHLI; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0047689; F:aspartate racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0008881; F:glutamate racemase activity; IEA:UniProtKB-EC.
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 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..230
FT /note="L-aspartate/glutamate-specific racemase"
FT /id="PRO_0000447008"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27001440"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27001440"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27001440"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27001440"
FT BINDING 83..85
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27001440"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27001440"
SQ SEQUENCE 230 AA; 25308 MW; 6D0E9549ACE1241D CRC64;
MKTIGLLGGM SWESTIPYYR LINEGIKQRL GGLHSAQVLL HSVDFHEIEE CQRRGEWDKT
GDILAEAALG LQRAGAEGIV LCTNTMHKVA DAIESRCTLP FLHIADATGR AITGAGMTRV
ALLGTRYTME QDFYRGRLTE QFSINCLIPE ADERAKINQI IFEELCLGQF TEASRAYYAQ
VIARLAEQGA QGVIFGCTEI GLLVPEERSV LPVFDTAAIH AEDAVAFMLS
