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UniProtKB - P14900 (MURD_ECOLI)
Protein
UDP-N-acetylmuramoylalanine--D-glutamate ligase
Gene
murD
Organism
Escherichia coli (strain K12)
Status
Functioni
Cell wall formation (Probable). Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (PubMed:1765076).
Curated1 PublicationCatalytic activityi
- ATP + D-glutamate + UDP-N-acetyl-α-D-muramoyl-L-alanine = ADP + H+ + phosphate + UDP-N-acetyl-α-D-muramoyl-L-alanyl-D-glutamate1 PublicationEC:6.3.2.91 Publication
Cofactori
Mg2+1 Publication
Kineticsi
The optimum activity is at 11-16 mM for potassium phosphate and at 5 mM for Mg2+.1 Publication
- KM=7.5 µM for UDP-N-acetylmuramoyl-L-alanine1 Publication
- KM=55 µM for D-glutamate1 Publication
- KM=138 µM for ATP/ Mg2+1 Publication
pH dependencei
Optimum pH is 9.0.1 Publication
: peptidoglycan biosynthesis Pathwayi
This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 112 – 118 | ATPSequence analysis | 7 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- identical protein binding Source: IntAct
- UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Source: EcoCyc
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cell wall organization Source: UniProtKB-KW
- peptidoglycan biosynthetic process Source: EcoCyc
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Ligase |
Biological process | Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER |
BRENDAi | 6.3.2.9, 2026 |
SABIO-RKi | P14900 |
UniPathwayi | UPA00219 |
Names & Taxonomyi
Protein namesi | Recommended name: UDP-N-acetylmuramoylalanine--D-glutamate ligase1 Publication (EC:6.3.2.91 Publication)Alternative name(s): D-glutamic acid-adding enzyme UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase |
Gene namesi | Name:murD Ordered Locus Names:b0088, JW0086 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
Other locations
- cytoplasm Source: EcoliWiki
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL4732 |
DrugBanki | DB03801, Lysine Nz-Carboxylic Acid DB08112, N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08108, N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08106, N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid DB08105, N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid DB08107, N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID DB01673, Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine DB02314, Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000109013 | 2 – 438 | UDP-N-acetylmuramoylalanine--D-glutamate ligaseAdd BLAST | 437 |
Proteomic databases
jPOSTi | P14900 |
PaxDbi | P14900 |
PRIDEi | P14900 |
Interactioni
Binary interactionsi
P14900
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-554780,EBI-554780 |
trxC [P0AGG4] | 2 | EBI-554780,EBI-549392 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4261477, 566 interactors 849219, 5 interactors |
DIPi | DIP-10279N |
IntActi | P14900, 8 interactors |
STRINGi | 511145.b0088 |
Chemistry databases
BindingDBi | P14900 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P14900 |
SMRi | P14900 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P14900 |
Family & Domainsi
Sequence similaritiesi
Belongs to the MurCDEF family.Curated
Phylogenomic databases
eggNOGi | COG0771, Bacteria |
HOGENOMi | CLU_032540_1_0_6 |
InParanoidi | P14900 |
OMAi | CNFENYL |
PhylomeDBi | P14900 |
Family and domain databases
Gene3Di | 3.40.1190.10, 1 hit 3.90.190.20, 1 hit |
HAMAPi | MF_00639, MurD, 1 hit |
InterProi | View protein in InterPro IPR036565, Mur-like_cat_sf IPR004101, Mur_ligase_C IPR036615, Mur_ligase_C_dom_sf IPR013221, Mur_ligase_cen IPR005762, MurD |
Pfami | View protein in Pfam PF02875, Mur_ligase_C, 1 hit PF08245, Mur_ligase_M, 1 hit |
SUPFAMi | SSF53244, SSF53244, 1 hit SSF53623, SSF53623, 1 hit |
TIGRFAMsi | TIGR01087, murD, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P14900-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA
60 70 80 90 100
VERHTGSLND EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC
110 120 130 140 150
REAQAPIVAI TGSNGKSTVT TLVGEMAKAA GVNVGVGGNI GLPALMLLDD
160 170 180 190 200
ECELYVLELS SFQLETTSSL QAVAATILNV TEDHMDRYPF GLQQYRAAKL
210 220 230 240 250
RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL NHQQGETWLR
260 270 280 290 300
VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL
310 320 330 340 350
PHRFEVVLEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS
360 370 380 390 400
ADFSPLARYL NGDNVRLYCF GRDGAQLAAL RPEVAEQTET MEQAMRLLAP
410 420 430
RVQPGDMVLL SPACASLDQF KNFEQRGNEF ARLAKELG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 28 | R → A in CAA35611 (PubMed:2129548).Curated | 1 | |
Sequence conflicti | 174 | A → T in CAA35611 (PubMed:2129548).Curated | 1 | |
Sequence conflicti | 276 – 277 | AL → RV in CAA35611 (PubMed:2129548).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X51584 Genomic DNA Translation: CAA35933.1 X17609 Genomic DNA Translation: CAA35611.1 X55034 Genomic DNA Translation: CAA38865.1 M30807 Genomic DNA Translation: AAA83858.1 U00096 Genomic DNA Translation: AAC73199.1 AP009048 Genomic DNA Translation: BAB96656.1 |
PIRi | S08396, CEECME |
RefSeqi | NP_414630.1, NC_000913.3 WP_000796481.1, NZ_SSZK01000004.1 |
Genome annotation databases
EnsemblBacteriai | AAC73199; AAC73199; b0088 BAB96656; BAB96656; BAB96656 |
GeneIDi | 944818 |
KEGGi | ecj:JW0086 eco:b0088 |
PATRICi | fig|1411691.4.peg.2192 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X51584 Genomic DNA Translation: CAA35933.1 X17609 Genomic DNA Translation: CAA35611.1 X55034 Genomic DNA Translation: CAA38865.1 M30807 Genomic DNA Translation: AAA83858.1 U00096 Genomic DNA Translation: AAC73199.1 AP009048 Genomic DNA Translation: BAB96656.1 |
PIRi | S08396, CEECME |
RefSeqi | NP_414630.1, NC_000913.3 WP_000796481.1, NZ_SSZK01000004.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1E0D | X-ray | 2.40 | A | 2-438 | [»] | |
1EEH | X-ray | 1.90 | A | 2-438 | [»] | |
1UAG | X-ray | 1.95 | A | 2-438 | [»] | |
2JFF | X-ray | 1.89 | A | 2-438 | [»] | |
2JFG | X-ray | 1.52 | A | 2-438 | [»] | |
2JFH | X-ray | 1.97 | A | 2-438 | [»] | |
2UAG | X-ray | 1.70 | A | 2-438 | [»] | |
2UUO | X-ray | 2.50 | A | 2-438 | [»] | |
2UUP | X-ray | 1.88 | A | 2-438 | [»] | |
2VTD | X-ray | 1.94 | A | 1-438 | [»] | |
2VTE | X-ray | 2.20 | A | 1-438 | [»] | |
2WJP | X-ray | 1.60 | A | 2-438 | [»] | |
2X5O | X-ray | 1.46 | A | 2-438 | [»] | |
2XPC | X-ray | 1.49 | A | 2-438 | [»] | |
2Y1O | X-ray | 1.49 | A | 1-438 | [»] | |
2Y66 | X-ray | 1.49 | A | 1-438 | [»] | |
2Y67 | X-ray | 1.85 | A | 1-438 | [»] | |
2Y68 | X-ray | 1.49 | A | 1-438 | [»] | |
3UAG | X-ray | 1.77 | A | 2-438 | [»] | |
4UAG | X-ray | 1.66 | A | 2-438 | [»] | |
5A5E | X-ray | 1.84 | A | 2-438 | [»] | |
5A5F | X-ray | 1.90 | A | 2-438 | [»] | |
AlphaFoldDBi | P14900 | |||||
SMRi | P14900 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261477, 566 interactors 849219, 5 interactors |
DIPi | DIP-10279N |
IntActi | P14900, 8 interactors |
STRINGi | 511145.b0088 |
Chemistry databases
BindingDBi | P14900 |
ChEMBLi | CHEMBL4732 |
DrugBanki | DB03801, Lysine Nz-Carboxylic Acid DB08112, N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08108, N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08106, N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid DB08105, N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid DB08107, N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID DB01673, Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine DB02314, Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate |
Proteomic databases
jPOSTi | P14900 |
PaxDbi | P14900 |
PRIDEi | P14900 |
Genome annotation databases
EnsemblBacteriai | AAC73199; AAC73199; b0088 BAB96656; BAB96656; BAB96656 |
GeneIDi | 944818 |
KEGGi | ecj:JW0086 eco:b0088 |
PATRICi | fig|1411691.4.peg.2192 |
Organism-specific databases
EchoBASEi | EB0615 |
Phylogenomic databases
eggNOGi | COG0771, Bacteria |
HOGENOMi | CLU_032540_1_0_6 |
InParanoidi | P14900 |
OMAi | CNFENYL |
PhylomeDBi | P14900 |
Enzyme and pathway databases
UniPathwayi | UPA00219 |
BioCyci | EcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER |
BRENDAi | 6.3.2.9, 2026 |
SABIO-RKi | P14900 |
Miscellaneous databases
EvolutionaryTracei | P14900 |
PROi | PR:P14900 |
Family and domain databases
Gene3Di | 3.40.1190.10, 1 hit 3.90.190.20, 1 hit |
HAMAPi | MF_00639, MurD, 1 hit |
InterProi | View protein in InterPro IPR036565, Mur-like_cat_sf IPR004101, Mur_ligase_C IPR036615, Mur_ligase_C_dom_sf IPR013221, Mur_ligase_cen IPR005762, MurD |
Pfami | View protein in Pfam PF02875, Mur_ligase_C, 1 hit PF08245, Mur_ligase_M, 1 hit |
SUPFAMi | SSF53244, SSF53244, 1 hit SSF53623, SSF53623, 1 hit |
TIGRFAMsi | TIGR01087, murD, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MURD_ECOLI | |
Accessioni | P14900Primary (citable) accession number: P14900 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 209 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families