Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P51981 (AEEP_ECOLI)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

L-Ala-D/L-Glu epimerase

Gene

ycjG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala.2 Publications

Catalytic activityi

L-alanyl-D-glutamate = L-alanyl-L-glutamate.1 Publication

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Kineticsi

  1. KM=0.13 mM for L-Ala-D-Glu (at pH 8.5)1 Publication
  2. KM=0.19 mM for L-Ala-D-Asp (at pH 8.5)1 Publication
  3. KM=0.69 mM for L-Ala-D-Met (at pH 8.5)1 Publication
  4. KM=1.8 mM for L-Ala-D-Gln (at pH 8.5)1 Publication

    Pathwayi: peptidoglycan recycling

    This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.
    View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei124SubstrateBy similarity1
    Binding sitei149SubstrateBy similarity1
    Active sitei151Proton acceptor; specific for (R)-substrate epimerizationBy similarity1
    Metal bindingi176MagnesiumBy similarity1
    Metal bindingi202MagnesiumBy similarity1
    Metal bindingi225MagnesiumBy similarity1
    Active sitei247Proton acceptor; specific for (S)-substrate epimerizationBy similarity1
    Binding sitei275Substrate; via carbonyl oxygenBy similarity1
    Binding sitei297SubstrateBy similarity1
    Binding sitei299SubstrateBy similarity1

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    Keywordsi

    Molecular functionIsomerase
    Biological processCell wall biogenesis/degradation
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G6661-MONOMER.
    MetaCyc:G6661-MONOMER.
    SABIO-RKiP51981.
    UniPathwayiUPA00544.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-Ala-D/L-Glu epimerase (EC:5.1.1.201 Publication)
    Short name:
    AE epimerase
    Short name:
    AEE
    Gene namesi
    Name:ycjG
    Synonyms:ycjH
    Ordered Locus Names:b1325, JW1318
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13228. ycjG.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001712611 – 321L-Ala-D/L-Glu epimeraseAdd BLAST321

    Proteomic databases

    EPDiP51981.
    PaxDbiP51981.
    PRIDEiP51981.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4260152. 370 interactors.
    IntActiP51981. 1 interactor.
    STRINGi316385.ECDH10B_1444.

    Structurei

    Secondary structure

    1321
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 14Combined sources12
    Beta strandi25 – 36Combined sources12
    Beta strandi39 – 45Combined sources7
    Helixi49 – 51Combined sources3
    Helixi55 – 63Combined sources9
    Helixi66 – 70Combined sources5
    Helixi75 – 81Combined sources7
    Helixi86 – 101Combined sources16
    Turni102 – 104Combined sources3
    Helixi107 – 111Combined sources5
    Beta strandi117 – 121Combined sources5
    Beta strandi123 – 125Combined sources3
    Helixi130 – 142Combined sources13
    Beta strandi146 – 151Combined sources6
    Helixi157 – 167Combined sources11
    Beta strandi171 – 176Combined sources6
    Helixi186 – 195Combined sources10
    Beta strandi200 – 202Combined sources3
    Helixi211 – 214Combined sources4
    Beta strandi222 – 225Combined sources4
    Helixi231 – 233Combined sources3
    Helixi234 – 237Combined sources4
    Beta strandi241 – 246Combined sources6
    Helixi248 – 251Combined sources4
    Helixi254 – 266Combined sources13
    Beta strandi270 – 273Combined sources4
    Helixi280 – 286Combined sources7
    Helixi287 – 292Combined sources6
    Beta strandi294 – 296Combined sources3
    Helixi300 – 303Combined sources4
    Beta strandi304 – 306Combined sources3
    Beta strandi313 – 315Combined sources3
    Beta strandi318 – 320Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1JPDX-ray2.60X1-321[»]
    ProteinModelPortaliP51981.
    SMRiP51981.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51981.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the mandelate racemase/muconate lactonizing enzyme family.Curated

    Phylogenomic databases

    eggNOGiENOG4107S8C. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000185901.
    InParanoidiP51981.
    KOiK19802.
    OMAiSAFSSPW.
    PhylomeDBiP51981.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiView protein in InterPro
    IPR036849. Enolase-like_C_sf.
    IPR029017. Enolase-like_N.
    IPR034390. Enolase-like_superfamily.
    IPR029065. Enolase_C-like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    PfamiView protein in Pfam
    PF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    SFLDiSFLDS00001. Enolase. 1 hit.
    SMARTiView protein in SMART
    SM00922. MR_MLE. 1 hit.
    SUPFAMiSSF51604. SSF51604. 1 hit.
    PROSITEiView protein in PROSITE
    PS00908. MR_MLE_1. 1 hit.
    PS00909. MR_MLE_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P51981-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRTVKVFEEA WPLHTPFVIA RGSRSEARVV VVELEEEGIK GTGECTPYPR 
            60         70         80         90        100
    YGESDASVMA QIMSVVPQLE KGLTREELQK ILPAGAARNA LDCALWDLAA 
           110        120        130        140        150
    RRQQQSLADL IGITLPETVI TAQTVVIGTP DQMANSASTL WQAGAKLLKV 
           160        170        180        190        200
    KLDNHLISER MVAIRTAVPD ATLIVDANES WRAEGLAARC QLLADLGVAM 
           210        220        230        240        250
    LEQPLPAQDD AALENFIHPL PICADESCHT RSNLKALKGR YEMVNIKLDK 
           260        270        280        290        300
    TGGLTEALAL ATEARAQGFS LMLGCMLCTS RAISAALPLV PQVSFADLDG 
           310        320 
    PTWLAVDVEP ALQFTTGELH L
    Length:321
    Mass (Da):34,674
    Last modified:November 1, 1997 - v2
    Checksum:iB0AA31DD4EC2E2CB
    GO

    Sequence cautioni

    The sequence U33213 differs from that shown. Reason: Frameshift at position 285.Curated
    The sequence U33213 differs from that shown. Reason: Erroneous termination at position 275. Translated as Cys.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti236A → R in U33213 (PubMed:7499381).Curated1
    Sequence conflicti244V → I in U33213 (PubMed:7499381).Curated1
    Sequence conflicti257Missing in U33213 (PubMed:7499381).Curated1
    Sequence conflicti259A → G in U33213 (PubMed:7499381).Curated1
    Sequence conflicti301P → S in U33213 (PubMed:7499381).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U33213 Genomic DNA. No translation available.
    U00096 Genomic DNA. Translation: AAC74407.2.
    AP009048 Genomic DNA. Translation: BAA14907.1.
    PIRiH64881.
    RefSeqiNP_415841.4. NC_000913.3.
    WP_001261211.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74407; AAC74407; b1325.
    BAA14907; BAA14907; BAA14907.
    GeneIDi946013.
    KEGGiecj:JW1318.
    eco:b1325.
    PATRICifig|1411691.4.peg.953.

    Similar proteinsi

    Entry informationi

    Entry nameiAEEP_ECOLI
    AccessioniPrimary (citable) accession number: P51981
    Secondary accession number(s): P51982, P76048, P77345
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: March 28, 2018
    This is version 140 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome