YGEA_ECOBD
ID YGEA_ECOBD Reviewed; 230 AA.
AC A0A140N890;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=L-aspartate/glutamate-specific racemase {ECO:0000303|PubMed:26555188};
DE Short=L-Asp/Glu-specific racemase {ECO:0000303|PubMed:26555188};
DE EC=5.1.1.13 {ECO:0000269|PubMed:26555188};
DE EC=5.1.1.3 {ECO:0000269|PubMed:26555188};
DE AltName: Full=EcL-DER {ECO:0000303|PubMed:26555188};
GN Name=ygeA {ECO:0000250|UniProtKB:A0A0H3JGH6};
GN OrderedLocusNames=ECBD_0884 {ECO:0000312|EMBL:ACT27951.1};
OS Escherichia coli (strain B / BL21-DE3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=469008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B / BL21-DE3;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT "Complete sequence of Escherichia coli BL21(DE3).";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5ELL, ECO:0007744|PDB:5ELM}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP L-GLUTAMIC ACID, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF
RP THR-83 AND CYS-197, AND ACTIVE SITE.
RC STRAIN=B / BL21-DE3;
RX PubMed=26555188; DOI=10.1016/j.febslet.2015.11.003;
RA Ahn J.W., Chang J.H., Kim K.J.;
RT "Structural basis for an atypical active site of an L-aspartate/glutamate-
RT specific racemase from Escherichia coli.";
RL FEBS Lett. 589:3842-3847(2015).
CC -!- FUNCTION: Exhibits racemase activity for both L-glutamate and L-
CC aspartate, but has threefold higher activity for L-glutamate than L-
CC aspartate. Cannot use D-glutamate or D-aspartate as substrate.
CC {ECO:0000269|PubMed:26555188}.
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:0000269|PubMed:26555188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12814;
CC Evidence={ECO:0000269|PubMed:26555188};
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:0000269|PubMed:26555188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14974;
CC Evidence={ECO:0000269|PubMed:26555188};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26555188}.
CC -!- INTERACTION:
CC A0A140N890; A0A140N890: ygeA; NbExp=2; IntAct=EBI-11476557, EBI-11476557;
CC -!- SIMILARITY: Belongs to the aspartate/glutamate racemases family.
CC {ECO:0000305}.
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DR EMBL; CP001665; ACT27951.1; -; Genomic_DNA.
DR RefSeq; WP_000848664.1; NZ_CP053602.1.
DR PDB; 5ELL; X-ray; 1.80 A; A/B=1-230.
DR PDB; 5ELM; X-ray; 2.00 A; A/B/C/D=1-230.
DR PDBsum; 5ELL; -.
DR PDBsum; 5ELM; -.
DR AlphaFoldDB; A0A140N890; -.
DR SMR; A0A140N890; -.
DR MINT; A0A140N890; -.
DR STRING; 469008.B21_02649; -.
DR GeneID; 66673293; -.
DR KEGG; ebd:ECBD_0884; -.
DR PATRIC; fig|469008.15.peg.2722; -.
DR eggNOG; COG1794; Bacteria.
DR HOGENOM; CLU_055360_1_0_6; -.
DR OMA; TNTMHLI; -.
DR Proteomes; UP000002032; 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:0042802; F:identical protein binding; IPI:IntAct.
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.
FT CHAIN 1..230
FT /note="L-aspartate/glutamate-specific racemase"
FT /id="PRO_0000447007"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:26555188"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:26555188"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26555188"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26555188"
FT BINDING 83..85
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26555188"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26555188"
FT MUTAGEN 83
FT /note="T->C: Shows bidirectional racemase activity."
FT /evidence="ECO:0000269|PubMed:26555188"
FT MUTAGEN 197
FT /note="C->S: Loss of racemase activity."
FT /evidence="ECO:0000269|PubMed:26555188"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5ELL"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5ELL"
FT HELIX 216..228
FT /evidence="ECO:0007829|PDB:5ELL"
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
