UDP-N-acetylmuramoylalanine--D-glutamate ligase
Details
- Name
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Kind
- protein
- Synonyms
- 6.3.2.9
- D-glutamic acid-adding enzyme
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
- Gene Name
- murD
- UniProtKB Entry
- P14900Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016366|UDP-N-acetylmuramoylalanine--D-glutamate ligase MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLND EWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVT TLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNV TEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHL NHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGL PHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQF KNFEQRGNEFARLAKELG
- Number of residues
- 438
- Molecular Weight
- 46973.185
- Theoretical pI
- 4.96
- GO Classification
- FunctionsATP binding / identical protein binding / UDP-N-acetylmuramoylalanine-D-glutamate ligase activityProcessescell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / regulation of cell shapeComponentscytoplasm
- General Function
- Cell wall formation (Probable). Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (PubMed:1765076).
- Specific Function
- ATP binding
- Pfam Domain Function
- Mur_ligase_M (PF08245)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0016367|UDP-N-acetylmuramoylalanine--D-glutamate ligase (murD) ATGGCTGATTATCAGGGTAAAAATGTCGTCATTATCGGCCTGGGCCTCACCGGGCTTTCC TGCGTGGACTTTTTCCTCGCTCGCGGTGTGACGCCGCGCGTTATGGATACGCGTATGACA CCGCCTGGCCTGGATAAATTACCCGAAGCCGTAGAACGCCACACGGGCAGTCTGAATGAT GAATGGCTGATGGCGGCAGATCTGATTGTCGCCAGTCCCGGTATTGCACTGGCGCATCCA TCCTTAAGCGCTGCCGCTGATGCCGGAATCGAAATCGTTGGCGATATCGAGCTGTTCTGT CGCGAAGCACAAGCACCGATTGTGGCGATTACCGGTTCTAACGGCAAAAGCACGGTCACC ACGCTAGTGGGTGAAATGGCGAAAGCGGCGGGGGTTAACGTTGGTGTGGGTGGCAATATT GGCCTGCCTGCGTTGATGCTACTGGATGATGAGTGTGAACTGTACGTGCTGGAACTGTCG AGCTTCCAGCTGGAAACCACCTCCAGCTTACAGGCGGTAGCAGCGACCATTCTGAACGTG ACTGAAGATCATATGGATCGCTATCCGTTTGGTTTACAACAGTATCGTGCAGCAAAACTG CGCATTTACGAAAACGCGAAAGTTTGCGTGGTTAATGCTGATGATGCCTTAACAATGCCG ATTCGCGGTGCGGATGAACGCTGCGTCAGCTTTGGCGTCAACATGGGTGACTATCACCTG AATCATCAGCAGGGCGAAACCTGGCTGCGGGTTAAAGGCGAGAAAGTGCTGAATGTGAAA GAGATGAAACTTTCCGGGCAGCATAACTACACCAATGCGCTGGCGGCGCTGGCGCTGGCA GATGCTGCAGGGTTACCGCGTGCCAGCAGCCTGAAAGCGTTAACCACATTCACTGGTCTG CCGCATCGCTTTGAAGTTGTGCTGGAGCATAACGGCGTACGTTGGATTAACGATTCGAAA GCGACCAACGTCGGCAGTACGGAAGCGGCGCTGAATGGCCTGCACGTAGACGGCACACTG CATTTGTTGCTGGGTGGCGATGGTAAATCGGCGGACTTTAGCCCACTGGCGCGTTACCTG AATGGCGATAACGTACGTCTGTATTGTTTCGGTCGTGACGGCGCGCAGCTGGCGGCGCTA CGCCCGGAAGTGGCAGAACAAACCGAAACTATGGAACAGGCGATGCGCTTGCTGGCTCCG CGTGTTCAGCCGGGCGATATGGTTCTGCTCTCCCCAGCCTGTGCCAGCCTTGATCAGTTC AAGAACTTTGAACAACGAGGCAATGAGTTTGCCCGTCTGGCGAAGGAGTTAGGTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P14900 UniProtKB Entry Name MURD_ECOLI GenBank Protein ID 42060 GenBank Gene ID X51584 PDB ID(s) 1E0D, 1EEH, 1UAG, 2JFF, 2JFG, 2JFH, 2UAG, 2UUO, 2UUP, 2VTD, 2VTE, 2WJP, 2X5O, 2XPC, 2Y1O, 2Y66, 2Y67, 2Y68, 3UAG, 4UAG KEGG ID ecj:JW0086 NCBI Gene ID 944818 - General References
- Ikeda M, Wachi M, Ishino F, Matsuhashi M: Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli. Nucleic Acids Res. 1990 Feb 25;18(4):1058. [Article]
- Mengin-Lecreulx D, van Heijenoort J: Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli. Nucleic Acids Res. 1990 Jan 11;18(1):183. [Article]
- Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Ikeda M, Sato T, Wachi M, Jung HK, Ishino F, Kobayashi Y, Matsuhashi M: 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. J Bacteriol. 1989 Nov;171(11):6375-8. [Article]
- Pratviel-Sosa F, Mengin-Lecreulx D, van Heijenoort J: Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. Eur J Biochem. 1991 Dec 18;202(3):1169-76. [Article]
- Bertrand JA, Auger G, Fanchon E, Martin L, Blanot D, van Heijenoort J, Dideberg O: Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli. EMBO J. 1997 Jun 16;16(12):3416-25. [Article]
- Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O: "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. J Mol Biol. 2000 Sep 1;301(5):1257-66. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine experimental unknown target Details Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate experimental unknown target Details Lysine Nz-Carboxylic Acid experimental unknown target Details N-[(6-butoxynaphthalen-2-yl)sulfonyl]-L-glutamic acid experimental unknown target Details N-[(6-butoxynaphthalen-2-yl)sulfonyl]-D-glutamic acid experimental unknown target Details N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID experimental unknown target Details N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID experimental unknown target Details N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID experimental unknown target Details