Bifunctional protein GlmU
Details
- Name
- Bifunctional protein GlmU
- Synonyms
- 2.7.7.23
- Gene Name
- glmU
- Organism
- Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
- Amino acid sequence
>lcl|BSEQ0012983|Bifunctional protein GlmU MTKKALSAVILAAGKGTRMYSDLPKVLHTIAGKPMVKHVIDTAHQLGSENIHLIYGHGGD LMRTHLANEQVNWVLQTEQLGTAHAVQQAAPFFKDNENIVVLYGDAPLITKETLEKLIEA KPENGIALLTVNLDNPTGYGRIIRENGNVVAIVEQKDANAEQLNIKEVNTGVMVSDGASF KKWLARVGNNNAQGEYYLTDLIALANQDNCQVVAVQATDVMEVEGANNRLQLAALERYFQ NKQASKLLLEGVMIYDPARFDLRGTLEHGKDVEIDVNVIIEGNVKLGDRVKIGTGCVLKN VVIGNDVEIKPYSVLEDSIVGEKAAIGPFSRLRPGAELAAETHVGNFVEIKKSTVGKGSK VNHLTYVGDSEIGSNCNIGAGVITCNYDGANKFKTIIGDDVFVGSDTQLVAPVKVANGAT IGAGTTITRDVGENELVITRVAQRHIQGWQRPIKKK
- Number of residues
- 456
- Molecular Weight
- 49287.025
- Theoretical pI
- 6.59
- GO Classification
- Functionsglucosamine-1-phosphate N-acetyltransferase activity / magnesium ion binding / UDP-N-acetylglucosamine diphosphorylase activityProcessescell morphogenesis / cell wall organization / lipid A biosynthetic process / lipopolysaccharide biosynthetic process / peptidoglycan biosynthetic process / regulation of cell shape / UDP-N-acetylglucosamine biosynthetic processComponentscytoplasm
- General Function
- Udp-n-acetylglucosamine diphosphorylase activity
- Specific Function
- Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0012984|Bifunctional protein GlmU (glmU) ATGACAAAAAAAGCATTAAGTGCGGTAATTTTAGCAGCTGGAAAAGGAACGCGTATGTAT TCTGATTTACCCAAAGTTCTACATACAATCGCGGGTAAACCAATGGTAAAACACGTGATT GATACTGCCCATCAATTAGGCTCAGAAAATATTCATTTAATCTATGGTCACGGTGGGGAC TTAATGCGTACCCATCTTGCGAATGAACAAGTAAATTGGGTATTACAAACAGAACAACTT GGCACAGCACATGCAGTTCAACAAGCAGCACCTTTCTTTAAAGATAACGAAAACATTGTT GTGCTTTACGGCGATGCACCATTAATTACTAAAGAAACATTAGAAAAATTAATTGAAGCG AAACCAGAAAATGGCATTGCATTGCTTACCGTAAATTTAGATAACCCAACAGGCTATGGA CGAATTATCCGTGAAAATGGGAACGTTGTAGCCATTGTAGAACAAAAAGATGCGAATGCT GAGCAACTAAATATTAAAGAAGTCAATACTGGCGTTATGGTATCTGATGGTGCAAGTTTC AAAAAATGGCTAGCTCGTGTAGGCAATAATAATGCTCAAGGCGAATATTACTTAACGGAT CTTATTGCTCTCGCAAACCAAGATAATTGTCAAGTTGTTGCTGTACAAGCAACAGATGTC ATGGAAGTTGAAGGCGCAAATAATCGCTTACAATTAGCCGCACTTGAACGTTATTTCCAA AATAAACAAGCCTCCAAATTATTACTTGAAGGCGTAATGATCTACGATCCCGCTCGTTTT GACCTACGTGGAACATTAGAGCATGGAAAAGATGTGGAAATCGATGTTAATGTTATTATC GAAGGTAATGTTAAACTCGGTGATCGCGTAAAAATTGGCACAGGTTGCGTATTGAAAAAT GTTGTTATTGGCAATGATGTAGAAATAAAACCCTATTCAGTGCTAGAGGATTCTATAGTA GGAGAAAAAGCCGCAATTGGCCCATTTTCTCGTTTACGCCCAGGTGCAGAACTTGCAGCT GAAACGCATGTCGGTAACTTTGTAGAAATTAAAAAATCTACCGTTGGTAAAGGTTCTAAA GTAAATCACCTGACCTATGTTGGCGATTCAGAAATTGGCTCAAATTGTAATATTGGAGCG GGTGTCATAACCTGCAACTACGATGGTGCAAATAAATTTAAAACGATCATCGGTGATGAT GTGTTTGTGGGATCTGATACACAATTAGTCGCGCCAGTGAAAGTCGCAAATGGCGCAACT ATTGGTGCTGGGACTACAATTACACGTGATGTTGGCGAAAATGAATTAGTGATTACAAGA GTTGCTCAACGACATATTCAAGGTTGGCAACGACCAATAAAGAAAAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P43889 UniProtKB Entry Name GLMU_HAEIN GenBank Protein ID 3212176 GenBank Gene ID L42023 - General References
- Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb JF, Dougherty BA, Merrick JM, et al.: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science. 1995 Jul 28;269(5223):496-512. [Article]
- Mochalkin I, Lightle S, Zhu Y, Ohren JF, Spessard C, Chirgadze NY, Banotai C, Melnick M, McDowell L: Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU). Protein Sci. 2007 Dec;16(12):2657-66. [Article]
- Mochalkin I, Lightle S, Narasimhan L, Bornemeier D, Melnick M, Vanderroest S, McDowell L: Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site. Protein Sci. 2008 Mar;17(3):577-82. doi: 10.1110/ps.073271408. Epub 2008 Jan 24. [Article]
- Larsen NA, Nash TJ, Morningstar M, Shapiro AB, Joubran C, Blackett CJ, Patten AD, Boriack-Sjodin PA, Doig P: An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode. Biochem J. 2012 Sep 15;446(3):405-13. doi: 10.1042/BJ20120596. [Article]
- Doig P, Boriack-Sjodin PA, Dumas J, Hu J, Itoh K, Johnson K, Kazmirski S, Kinoshita T, Kuroda S, Sato TO, Sugimoto K, Tohyama K, Aoi H, Wakamatsu K, Wang H: Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping. Bioorg Med Chem. 2014 Nov 1;22(21):6256-69. doi: 10.1016/j.bmc.2014.08.017. Epub 2014 Sep 16. [Article]