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P14900

- MURD_ECOLI

UniProt

P14900 - MURD_ECOLI

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Protein
UDP-N-acetylmuramoylalanine--D-glutamate ligase
Gene
murD, b0088, JW0086
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate.UniRule annotation

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi112 – 1187ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Source: EcoCyc
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  4. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
ECOL316407:JW0086-MONOMER.
MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
SABIO-RKP14900.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10620. murD.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 438437UDP-N-acetylmuramoylalanine--D-glutamate ligaseUniRule annotation
PRO_0000109013Add
BLAST

Proteomic databases

PaxDbiP14900.
PRIDEiP14900.

Expressioni

Gene expression databases

GenevestigatoriP14900.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-554780,EBI-554780

Protein-protein interaction databases

DIPiDIP-10279N.
IntActiP14900. 8 interactions.
MINTiMINT-1269366.
STRINGi511145.b0088.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124
Helixi15 – 2612
Turni27 – 293
Beta strandi33 – 408
Helixi44 – 463
Beta strandi53 – 575
Helixi60 – 645
Beta strandi67 – 715
Helixi75 – 784
Helixi80 – 878
Beta strandi91 – 933
Helixi95 – 1028
Beta strandi107 – 1115
Beta strandi113 – 1153
Helixi116 – 12914
Beta strandi134 – 1429
Helixi144 – 1474
Beta strandi154 – 1585
Helixi161 – 1655
Beta strandi173 – 1775
Helixi185 – 1873
Helixi191 – 20010
Helixi201 – 2033
Beta strandi207 – 2126
Helixi216 – 2183
Beta strandi221 – 2233
Beta strandi229 – 2313
Beta strandi233 – 24311
Beta strandi246 – 2516
Beta strandi254 – 2585
Helixi259 – 2613
Helixi267 – 28216
Helixi287 – 29610
Beta strandi303 – 3108
Beta strandi313 – 3175
Helixi324 – 3318
Beta strandi340 – 3478
Helixi350 – 3523
Helixi354 – 3596
Beta strandi362 – 37110
Helixi374 – 3785
Helixi382 – 3843
Beta strandi385 – 3873
Helixi391 – 3988
Helixi399 – 4013
Beta strandi407 – 4104
Beta strandi413 – 4164
Turni417 – 4193
Beta strandi420 – 4223
Helixi423 – 43715

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP14900.
SMRiP14900. Positions 2-438.

Miscellaneous databases

EvolutionaryTraceiP14900.

Family & Domainsi

Sequence similaritiesi

Belongs to the MurCDEF family.

Phylogenomic databases

eggNOGiCOG0771.
HOGENOMiHOG000049427.
KOiK01925.
OMAiYCFGQDG.
OrthoDBiEOG6PKFCR.
PhylomeDBiP14900.

Family and domain databases

Gene3Di3.40.1190.10. 1 hit.
3.40.50.720. 1 hit.
3.90.190.20. 1 hit.
HAMAPiMF_00639. MurD.
InterProiIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR016040. NAD(P)-bd_dom.
IPR005762. UDP-N-AcMur-Glu_ligase.
[Graphical view]
PfamiPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
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

MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA    50
VERHTGSLND EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC 100
REAQAPIVAI TGSNGKSTVT TLVGEMAKAA GVNVGVGGNI GLPALMLLDD 150
ECELYVLELS SFQLETTSSL QAVAATILNV TEDHMDRYPF GLQQYRAAKL 200
RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL NHQQGETWLR 250
VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL 300
PHRFEVVLEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS 350
ADFSPLARYL NGDNVRLYCF GRDGAQLAAL RPEVAEQTET MEQAMRLLAP 400
RVQPGDMVLL SPACASLDQF KNFEQRGNEF ARLAKELG 438
Length:438
Mass (Da):46,974
Last modified:January 23, 2007 - v3
Checksum:i11C64782C098F761
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281R → A in CAA35611. 1 Publication
Sequence conflicti174 – 1741A → T in CAA35611. 1 Publication
Sequence conflicti276 – 2772AL → RV in CAA35611. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488393.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73199; AAC73199; b0088.
BAB96656; BAB96656; BAB96656.
GeneIDi12932483.
944818.
KEGGiecj:Y75_p0087.
eco:b0088.
PATRICi32115281. VBIEscCol129921_0092.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_488393.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P14900.
SMRi P14900. Positions 2-438.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10279N.
IntActi P14900. 8 interactions.
MINTi MINT-1269366.
STRINGi 511145.b0088.

Chemistry

BindingDBi P14900.
ChEMBLi CHEMBL4732.

Proteomic databases

PaxDbi P14900.
PRIDEi P14900.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73199 ; AAC73199 ; b0088 .
BAB96656 ; BAB96656 ; BAB96656 .
GeneIDi 12932483.
944818.
KEGGi ecj:Y75_p0087.
eco:b0088.
PATRICi 32115281. VBIEscCol129921_0092.

Organism-specific databases

EchoBASEi EB0615.
EcoGenei EG10620. murD.

Phylogenomic databases

eggNOGi COG0771.
HOGENOMi HOG000049427.
KOi K01925.
OMAi YCFGQDG.
OrthoDBi EOG6PKFCR.
PhylomeDBi P14900.

Enzyme and pathway databases

UniPathwayi UPA00219 .
BioCyci EcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
ECOL316407:JW0086-MONOMER.
MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
SABIO-RK P14900.

Miscellaneous databases

EvolutionaryTracei P14900.
PROi P14900.

Gene expression databases

Genevestigatori P14900.

Family and domain databases

Gene3Di 3.40.1190.10. 1 hit.
3.40.50.720. 1 hit.
3.90.190.20. 1 hit.
HAMAPi MF_00639. MurD.
InterProi IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR016040. NAD(P)-bd_dom.
IPR005762. UDP-N-AcMur-Glu_ligase.
[Graphical view ]
Pfami PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view ]
SUPFAMi SSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsi TIGR01087. murD. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli."
    Ikeda M., Wachi M., Ishino F., Matsuhashi M.
    Nucleic Acids Res. 18:1058-1058(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli."
    Mengin-Lecreulx D., van Heijenoort J.
    Nucleic Acids Res. 18:183-183(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Flouret B.
    Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively."
    Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M.
    J. Bacteriol. 171:6375-6378(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-438.
    Strain: K12.
  8. "Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli."
    Pratviel-Sosa F., Mengin-Lecreulx D., van Heijenoort J.
    Eur. J. Biochem. 202:1169-1176(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
    Strain: K12.
  9. "Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli."
    Bertrand J.A., Auger G., Fanchon E., Martin L., Blanot D., van Heijenoort J., Dideberg O.
    EMBO J. 16:3416-3425(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
  10. "'Open' structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase."
    Bertrand J.A., Fanchon E., Martin L., Chantalat L., Auger G., Blanot D., van Heijenoort J., Dideberg O.
    J. Mol. Biol. 301:1257-1266(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiMURD_ECOLI
AccessioniPrimary (citable) accession number: P14900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

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