AEEP_CLOAB
ID AEEP_CLOAB Reviewed; 358 AA.
AC Q97MK4;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=L-Ala-D/L-Glu epimerase;
DE Short=AE epimerase;
DE Short=AEE;
DE EC=5.1.1.20 {ECO:0000269|PubMed:11747447};
GN OrderedLocusNames=CA_C0192;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11747447; DOI=10.1021/bi011640x;
RA Schmidt D.M.Z., Hubbard B.K., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily: functional
RT assignment of unknown proteins in Bacillus subtilis and Escherichia coli as
RT L-Ala-D/L-Glu epimerases.";
RL Biochemistry 40:15707-15715(2001).
CC -!- FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and
CC has probably a role in the metabolism of the murein peptide, of which
CC L-Ala-D-Glu is a component. Is also able to catalyze the epimerization
CC of L-Ala-D-Asp. {ECO:0000269|PubMed:11747447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanyl-L-glutamate = L-alanyl-D-glutamate;
CC Xref=Rhea:RHEA:28394, ChEBI:CHEBI:61395, ChEBI:CHEBI:61396;
CC EC=5.1.1.20; Evidence={ECO:0000269|PubMed:11747447};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cell wall degradation; peptidoglycan degradation.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001437; AAK78174.1; -; Genomic_DNA.
DR PIR; C96923; C96923.
DR RefSeq; NP_346834.1; NC_003030.1.
DR RefSeq; WP_010963516.1; NC_003030.1.
DR AlphaFoldDB; Q97MK4; -.
DR SMR; Q97MK4; -.
DR STRING; 272562.CA_C0192; -.
DR EnsemblBacteria; AAK78174; AAK78174; CA_C0192.
DR GeneID; 44996684; -.
DR KEGG; cac:CA_C0192; -.
DR PATRIC; fig|272562.8.peg.378; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_0_9; -.
DR OMA; MFGCYSD; -.
DR OrthoDB; 951991at2; -.
DR UniPathway; UPA00549; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0103031; F:L-Ala-D/L-Glu epimerase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034603; Dipeptide_epimerase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SFLD; SFLDF00010; dipeptide_epimerase; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR PROSITE; PS00908; MR_MLE_1; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..358
FT /note="L-Ala-D/L-Glu epimerase"
FT /id="PRO_0000388971"
FT ACT_SITE 162
FT /note="Proton acceptor; specific for (R)-substrate
FT epimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Proton acceptor; specific for (S)-substrate
FT epimerization"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 358 AA; 38905 MW; 6BE3980A1836DD23 CRC64;
MIIKDIVIGH LSVPLKKPFK TAVRSVNSVN DVVVKIITDT GNVGFGSAAS TGLVTGDITE
SIEGAINNYI KRSIVGMDIE DFEAILIKLD NCIVGNTSAK AAVDIALYDL YGQRYGAPLY
KLLGGFRNKL ETDITISVNS PEEMSRDSVD AVKLGYKTLK IKVGKNPKLD IKRMREIRKA
IGYEVNLRID ANQGWQPKEA IRALNEIENE GLKIELVEQP VKAWNLEGLK MVTDNVNIPV
MADESVFSPK DAARVMEMRA CDLINIKLMK TGGIHNALKI CALAEVYGME CMLGCMLEGK
VSVTAAVHLA AAKRIITKID LDGPVLCSRD DVVGGAMYDN SNIVLVDEPG LGIEGINN
