Bifunctional protein GlmU
Details
- Name
- Bifunctional protein GlmU
- Kind
- protein
- Synonyms
- 2.7.7.23
- Gene Name
- glmU
- UniProtKB Entry
- Q97R46Swiss-Prot
- Organism
- Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
- NCBI Taxonomy ID
- 170187
- Amino acid sequence
>lcl|BSEQ0020655|Bifunctional protein GlmU MSNFAIILAAGKGTRMKSDLPKVLHKVAGISMLEHVFRSVGAIQPEKTVTVVGHKAELVE EVLAGQTEFVTQSEQLGTGHAVMMTEPILEGLSGHTLVIAGDTPLITGESLKNLIDFHIN HKNVATILTAETDNPFGYGRIVRNDNAEVLRIVEQKDATDFEKQIKEINTGTYVFDNERL FEALKNINTNNAQGEYYITDVIGIFRETGEKVGAYTLKDFDESLGVNDRVALATAESVMR RRINHKHMVNGVSFVNPEATYIDIDVEIASEVQIEANVTLKGQTKIGAETVLTNGTYVVD STIGAGAVITNSMIEESSVADGVIVGPYAHIRPNSSLGAQVHIGNFVEVKGSSIGENTKA GHLTYIGNCEVGSNVNFGAGTITVNYDGKNKYKTVIGNNVFVGSNSTIIAPVELGDNSLV GAGSTITKDVPADAIAIGRGRQINKDEYATRLPHHPKNQ
- Number of residues
- 459
- Molecular Weight
- 49344.4
- Theoretical pI
- 5.43
- 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
- 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.
- Specific Function
- glucosamine-1-phosphate N-acetyltransferase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0020656|Bifunctional protein GlmU (glmU) ATGTCAAATTTTGCCATTATTTTAGCAGCGGGTAAAGGGACTCGCATGAAATCTGATTTG CCAAAAGTTTTGCACAAGGTTGCGGGTATTTCTATGTTGGAACATGTTTTCCGTAGTGTG GGAGCTATCCAACCTGAAAAGACAGTAACAGTTGTAGGACACAAGGCAGAATTGGTTGAG GAGGTCTTGGCTGGACAGACAGAATTTGTGACTCAATCTGAACAGTTGGGAACTGGTCAT GCAGTTATGATGACAGAGCCTATCTTAGAAGGTTTGTCAGGACACACCTTGGTCATTGCA GGAGATACTCCTTTAATCACTGGTGAAAGCTTGAAAAACTTGATTGATTTCCATATCAAT CATAAAAATGTGGCCACTATCTTGACTGCTGAAACGGATAATCCTTTTGGTTATGGACGA ATTGTTCGTAATGACAATGCTGAGGTTCTTCGTATTGTTGAGCAGAAGGATGCTACAGAT TTTGAAAAGCAAATCAAGGAAATCAACACTGGAACATACGTCTTTGACAACGAGCGTTTG TTTGAGGCTTTGAAAAATATCAATACCAATAACGCTCAAGGCGAATACTATATTACAGAC GTCATTGGTATTTTCCGTGAAACTGGTGAAAAAGTTGGCGCTTATACTTTGAAAGATTTT GATGAAAGTCTTGGGGTAAATGACCGTGTGGCGCTTGCGACAGCTGAGTCAGTTATGCGT CGTCGCATCAATCATAAACACATGGTCAACGGTGTTAGCTTTGTCAATCCAGAAGCAACT TATATCGATATTGATGTTGAGATTGCTTCGGAAGTTCAAATCGAAGCCAATGTTACCTTG AAAGGGCAAACGAAAATTGGTGCTGAGACTGTTTTGACAAACGGTACTTATGTAGTGGAC AGCACTATCGGAGCAGGAGCGGTCATTACCAATTCTATGATTGAGGAAAGTAGTGTTGCA GACGGTGTGATAGTCGGTCCTTATGCTCACATTCGTCCAAATTCAAGTCTGGGTGCCCAA GTTCATATTGGTAACTTTGTTGAGGTGAAAGGATCTTCAATCGGTGAGAATACCAAGGCT GGTCATTTGACTTATATCGGAAACTGTGAAGTGGGAAGCAACGTTAATTTCGGTGCTGGA ACTATTACAGTCAACTATGACGGCAAAAACAAATACAAGACAGTCATTGGAAACAATGTC TTTGTTGGTTCAAATTCAACCATTATTGCACCAGTAGAACTTGGTGACAATTCCCTCGTT GGTGCTGGTTCAACTATTACTAAAGACGTGCCAGCAGATGCTATTGCTATTGGTCGCGGT CGTCAGATCAATAAAGACGAATATGCAACACGTCTTCCTCATCATCCTAAGAACCAGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q97R46 UniProtKB Entry Name GLMU_STRPN GenBank Gene ID AE005672 PDB ID(s) 1G95, 1G97, 1HM0, 1HM8, 1HM9 KEGG ID spn:SP_0988 - General References
- Tettelin H, Nelson KE, Paulsen IT, Eisen JA, Read TD, Peterson S, Heidelberg J, DeBoy RT, Haft DH, Dodson RJ, Durkin AS, Gwinn M, Kolonay JF, Nelson WC, Peterson JD, Umayam LA, White O, Salzberg SL, Lewis MR, Radune D, Holtzapple E, Khouri H, Wolf AM, Utterback TR, Hansen CL, McDonald LA, Feldblyum TV, Angiuoli S, Dickinson T, Hickey EK, Holt IE, Loftus BJ, Yang F, Smith HO, Venter JC, Dougherty BA, Morrison DA, Hollingshead SK, Fraser CM: Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science. 2001 Jul 20;293(5529):498-506. [Article]
- Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y: Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture. J Biol Chem. 2001 Apr 13;276(15):11844-51. Epub 2000 Dec 15. [Article]
- Kostrewa D, D'Arcy A, Takacs B, Kamber M: Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution. J Mol Biol. 2001 Jan 12;305(2):279-89. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Uridine-Diphosphate-N-Acetylglucosamine experimental unknown target Details