UniProtKB - P51981 (AEEP_ECOLI)
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Protein
L-Ala-D/L-Glu epimerase
Gene
ycjG
Organism
Escherichia coli (strain K12)
Status
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
- KM=0.13 mM for L-Ala-D-Glu (at pH 8.5)1 Publication
- KM=0.19 mM for L-Ala-D-Asp (at pH 8.5)1 Publication
- KM=0.69 mM for L-Ala-D-Met (at pH 8.5)1 Publication
- KM=1.8 mM for L-Ala-D-Gln (at pH 8.5)1 Publication
: peptidoglycan recycling Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 124 | SubstrateBy similarity | 1 | |
Binding sitei | 149 | SubstrateBy similarity | 1 | |
Active sitei | 151 | Proton acceptor; specific for (R)-substrate epimerizationBy similarity | 1 | |
Metal bindingi | 176 | MagnesiumBy similarity | 1 | |
Metal bindingi | 202 | MagnesiumBy similarity | 1 | |
Metal bindingi | 225 | MagnesiumBy similarity | 1 | |
Active sitei | 247 | Proton acceptor; specific for (S)-substrate epimerizationBy similarity | 1 | |
Binding sitei | 275 | Substrate; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 297 | SubstrateBy similarity | 1 | |
Binding sitei | 299 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- racemase and epimerase activity, acting on amino acids and derivatives Source: EcoCyc
GO - Biological processi
- cellular amino acid catabolic process Source: InterPro
- cell wall organization Source: UniProtKB-KW
- peptidoglycan turnover Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Isomerase |
Biological process | Cell wall biogenesis/degradation |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:G6661-MONOMER. MetaCyc:G6661-MONOMER. |
SABIO-RKi | P51981. |
UniPathwayi | UPA00544. |
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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Organism-specific databases
EcoGenei | EG13228. ycjG. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000171261 | 1 – 321 | L-Ala-D/L-Glu epimeraseAdd BLAST | 321 |
Proteomic databases
EPDi | P51981. |
PaxDbi | P51981. |
PRIDEi | P51981. |
Interactioni
Subunit structurei
Monomer.1 Publication
Protein-protein interaction databases
BioGridi | 4260152. 370 interactors. |
IntActi | P51981. 1 interactor. |
STRINGi | 316385.ECDH10B_1444. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 3 – 14 | Combined sources | 12 | |
Beta strandi | 25 – 36 | Combined sources | 12 | |
Beta strandi | 39 – 45 | Combined sources | 7 | |
Helixi | 49 – 51 | Combined sources | 3 | |
Helixi | 55 – 63 | Combined sources | 9 | |
Helixi | 66 – 70 | Combined sources | 5 | |
Helixi | 75 – 81 | Combined sources | 7 | |
Helixi | 86 – 101 | Combined sources | 16 | |
Turni | 102 – 104 | Combined sources | 3 | |
Helixi | 107 – 111 | Combined sources | 5 | |
Beta strandi | 117 – 121 | Combined sources | 5 | |
Beta strandi | 123 – 125 | Combined sources | 3 | |
Helixi | 130 – 142 | Combined sources | 13 | |
Beta strandi | 146 – 151 | Combined sources | 6 | |
Helixi | 157 – 167 | Combined sources | 11 | |
Beta strandi | 171 – 176 | Combined sources | 6 | |
Helixi | 186 – 195 | Combined sources | 10 | |
Beta strandi | 200 – 202 | Combined sources | 3 | |
Helixi | 211 – 214 | Combined sources | 4 | |
Beta strandi | 222 – 225 | Combined sources | 4 | |
Helixi | 231 – 233 | Combined sources | 3 | |
Helixi | 234 – 237 | Combined sources | 4 | |
Beta strandi | 241 – 246 | Combined sources | 6 | |
Helixi | 248 – 251 | Combined sources | 4 | |
Helixi | 254 – 266 | Combined sources | 13 | |
Beta strandi | 270 – 273 | Combined sources | 4 | |
Helixi | 280 – 286 | Combined sources | 7 | |
Helixi | 287 – 292 | Combined sources | 6 | |
Beta strandi | 294 – 296 | Combined sources | 3 | |
Helixi | 300 – 303 | Combined sources | 4 | |
Beta strandi | 304 – 306 | Combined sources | 3 | |
Beta strandi | 313 – 315 | Combined sources | 3 | |
Beta strandi | 318 – 320 | Combined sources | 3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JPD | X-ray | 2.60 | X | 1-321 | [»] | |
ProteinModelPortali | P51981. | |||||
SMRi | P51981. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P51981. |
Family & Domainsi
Sequence similaritiesi
Belongs to the mandelate racemase/muconate lactonizing enzyme family.Curated
Phylogenomic databases
eggNOGi | ENOG4107S8C. Bacteria. COG4948. LUCA. |
HOGENOMi | HOG000185901. |
InParanoidi | P51981. |
KOi | K19802. |
OMAi | SAFSSPW. |
PhylomeDBi | P51981. |
Family and domain databases
Gene3Di | 3.20.20.120. 1 hit. 3.30.390.10. 1 hit. |
InterProi | View 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. |
Pfami | View protein in Pfam PF13378. MR_MLE_C. 1 hit. PF02746. MR_MLE_N. 1 hit. |
SFLDi | SFLDS00001. Enolase. 1 hit. |
SMARTi | View protein in SMART SM00922. MR_MLE. 1 hit. |
SUPFAMi | SSF51604. SSF51604. 1 hit. |
PROSITEi | View protein in PROSITE PS00908. MR_MLE_1. 1 hit. PS00909. MR_MLE_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
P51981-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence U33213 differs from that shown. Reason: Erroneous termination at position 275. Translated as Cys.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 236 | A → R in U33213 (PubMed:7499381).Curated | 1 | |
Sequence conflicti | 244 | V → I in U33213 (PubMed:7499381).Curated | 1 | |
Sequence conflicti | 257 | Missing in U33213 (PubMed:7499381).Curated | 1 | |
Sequence conflicti | 259 | A → G in U33213 (PubMed:7499381).Curated | 1 | |
Sequence conflicti | 301 | P → S in U33213 (PubMed:7499381).Curated | 1 |
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. |
PIRi | H64881. |
RefSeqi | NP_415841.4. NC_000913.3. WP_001261211.1. NZ_LN832404.1. |
Genome annotation databases
EnsemblBacteriai | AAC74407; AAC74407; b1325. BAA14907; BAA14907; BAA14907. |
GeneIDi | 946013. |
KEGGi | ecj:JW1318. eco:b1325. |
PATRICi | fig|1411691.4.peg.953. |
Similar proteinsi
Entry informationi
Entry namei | AEEP_ECOLI | |
Accessioni | P51981Primary (citable) accession number: P51981 Secondary accession number(s): P51982, P76048, P77345 | |
Entry historyi | Integrated 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |