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Protein

UDP-N-acetylmuramoylalanine--D-glutamate ligase

Gene

murD

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

Functioni

Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).

Catalytic activityi

ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate.

Pathwayi: peptidoglycan biosynthesis

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 keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi112 – 118ATPSequence analysis7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Source: EcoCyc

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER
MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER
BRENDAi6.3.2.9 2026
SABIO-RKiP14900
UniPathwayiUPA00219

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC:6.3.2.9)
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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10620 murD

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4732
DrugBankiDB03801 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 keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001090132 – 438UDP-N-acetylmuramoylalanine--D-glutamate ligaseAdd BLAST437

Proteomic databases

EPDiP14900
PaxDbiP14900
PRIDEiP14900

Interactioni

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4261477, 566 interactors
DIPiDIP-10279N
IntActiP14900, 8 interactors
STRINGi316385.ECDH10B_0070

Chemistry databases

BindingDBiP14900

Structurei

Secondary structure

1438
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Helixi15 – 26Combined sources12
Turni27 – 29Combined sources3
Beta strandi33 – 40Combined sources8
Helixi44 – 46Combined sources3
Beta strandi53 – 57Combined sources5
Helixi60 – 64Combined sources5
Beta strandi67 – 71Combined sources5
Helixi75 – 78Combined sources4
Helixi80 – 87Combined sources8
Beta strandi91 – 93Combined sources3
Helixi95 – 102Combined sources8
Beta strandi107 – 111Combined sources5
Beta strandi113 – 115Combined sources3
Helixi116 – 129Combined sources14
Beta strandi134 – 142Combined sources9
Helixi144 – 147Combined sources4
Beta strandi154 – 158Combined sources5
Helixi161 – 165Combined sources5
Beta strandi173 – 177Combined sources5
Helixi185 – 187Combined sources3
Helixi191 – 200Combined sources10
Helixi201 – 203Combined sources3
Beta strandi207 – 212Combined sources6
Helixi216 – 218Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi229 – 231Combined sources3
Beta strandi233 – 243Combined sources11
Beta strandi246 – 251Combined sources6
Beta strandi254 – 258Combined sources5
Helixi259 – 261Combined sources3
Helixi267 – 282Combined sources16
Helixi287 – 296Combined sources10
Beta strandi303 – 310Combined sources8
Beta strandi313 – 317Combined sources5
Helixi324 – 331Combined sources8
Beta strandi340 – 347Combined sources8
Helixi350 – 352Combined sources3
Helixi354 – 359Combined sources6
Beta strandi362 – 371Combined sources10
Helixi374 – 378Combined sources5
Helixi382 – 384Combined sources3
Beta strandi385 – 387Combined sources3
Helixi391 – 398Combined sources8
Helixi399 – 401Combined sources3
Beta strandi407 – 410Combined sources4
Beta strandi413 – 416Combined sources4
Turni417 – 419Combined sources3
Beta strandi420 – 422Combined sources3
Helixi423 – 437Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E0DX-ray2.40A2-438[»]
1EEHX-ray1.90A2-438[»]
1UAGX-ray1.95A2-438[»]
2JFFX-ray1.89A2-438[»]
2JFGX-ray1.52A2-438[»]
2JFHX-ray1.97A2-438[»]
2UAGX-ray1.70A2-438[»]
2UUOX-ray2.50A2-438[»]
2UUPX-ray1.88A2-438[»]
2VTDX-ray1.94A1-438[»]
2VTEX-ray2.20A1-438[»]
2WJPX-ray1.60A2-438[»]
2X5OX-ray1.46A2-438[»]
2XPCX-ray1.49A2-438[»]
2Y1OX-ray1.49A1-438[»]
2Y66X-ray1.49A1-438[»]
2Y67X-ray1.85A1-438[»]
2Y68X-ray1.49A1-438[»]
3UAGX-ray1.77A2-438[»]
4UAGX-ray1.66A2-438[»]
5A5EX-ray1.84A2-438[»]
5A5FX-ray1.90A2-438[»]
ProteinModelPortaliP14900
SMRiP14900
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14900

Family & Domainsi

Sequence similaritiesi

Belongs to the MurCDEF family.Curated

Phylogenomic databases

eggNOGiENOG4105DMZ Bacteria
COG0771 LUCA
HOGENOMiHOG000049427
InParanoidiP14900
KOiK01925
OMAiVDKGNDY
PhylomeDBiP14900

Family and domain databases

Gene3Di3.40.1190.10, 1 hit
3.90.190.20, 1 hit
HAMAPiMF_00639 MurD, 1 hit
InterProiView protein in InterPro
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen
IPR005762 UDP-N-AcMur-Glu_ligase
PfamiView protein in Pfam
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit
SUPFAMiSSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
TIGRFAMsiTIGR01087 murD, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14900-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:438
Mass (Da):46,974
Last modified:January 23, 2007 - v3
Checksum:i11C64782C098F761
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28R → A in CAA35611 (PubMed:2129548).Curated1
Sequence conflicti174A → T in CAA35611 (PubMed:2129548).Curated1
Sequence conflicti276 – 277AL → RV in CAA35611 (PubMed:2129548).Curated2

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
PIRiS08396 CEECME
RefSeqiNP_414630.1, NC_000913.3
WP_000796481.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73199; AAC73199; b0088
BAB96656; BAB96656; BAB96656
GeneIDi944818
KEGGiecj:JW0086
eco:b0088
PATRICifig|1411691.4.peg.2192

Similar proteinsi

Entry informationi

Entry nameiMURD_ECOLI
AccessioniPrimary (citable) accession number: P14900
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 187 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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