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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR1114 IGR1112 IGR1113 IGR1111 IGR1110 HD1513 glmU, - HD1511 pmm,pgm, - HD1507 acrB, - HD1512 HD1505 HD1508 HD1513 glmU, - HD1511 pmm,pgm, - HD1507 acrB, - HD1512 HD1505 HD1508 Type: tandem, Name:  - 16 HD1513 glmU, - HD1511 pmm,pgm, - HD1507 acrB, - HD1512 HD1505 HD1509 HD1508 HD1509
* Calculated from Protein Sequence

Gene ID: HD1511

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
glmU  

Definition:
UDP-N-acetylglucosamine pyrophosphorylase (bifunctional enzyme)

Gene Start:
1254799

Gene Stop:
1253429

Gene Length:
1371

Molecular Weight*:
49262

pI*:
7.90

Net Charge*:
3.67

EC:
2.3.1.57  2.7.7.23  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Sugar-nucleotide biosynthesis and conversions  

Pathway: pathway table
Aminosugars metabolism
Arginine and proline metabolism

Primary Evidence:
NULL

Secondary Evidence:
Olsen LR, Roderick SL.
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites.
Biochemistry. 2001 Feb 20;40(7):1913-21.
PMID: 11329257

Olsen LR, Tian Y, Roderick SL.
Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):296-7.
PMID: 11173485

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.
PMID: 11118459

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.
PMID: 11124906

Pompeo F, Bourne Y, van Heijenoort J, Fassy F, Mengin-Lecreulx D.
Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth.
J Biol Chem. 2001 Feb 9;276(6):3833-9.
PMID: 11084021

Comment:
Acetylates GLC-N-1-P to yield GLCNAC-1-P and also synthesizes UDP-GLCNAC (GenBank).



Blast Summary:  PSI-Blast Search
Residues 1 to 456 are 69% ( EScore : 0.0 ) identical to sp|P43889|GLMU_HAEIN UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE between residues 1 and 456 in [Haemophilus influenzae Rd]
Residues 7 to 456 are 64% ( EScore : 1e-172 ) identical to sp|P17114|GLMU_ECOLI UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE between residues 7 and 456 in [Escherichia coli]
Residues 7 to 456 are 64% ( EScore : 1e-172 ) identical to emb|CAA25784.1| (X01631) Eco urf 1 protein between residues 7 and 456 in [Escherichia coli]
Residues 1 to 456 are 50% ( EScore : 1e-125 ) identical to sp|Q50986|GLMU_NEIGO UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE between residues 1 and 455 in [Neisseria gonorrhoeae]
Residues 1 to 456 are 49% ( EScore : 1e-122 ) identical to gb|AAF40509.1| (AE002362) UDP-N-acetylglucosamine pyrophosphorylase between residues 1 and 455 in [Neisseria meningitidis MC58]
Residues 1 to 456 are 49% ( EScore : 1e-121 ) identical to emb|CAB83591.1| (AL162752) UDP-N-acetylglucosamine pyrophosphorylase between residues 1 and 455 in [Neisseria meningitidis]
Residues 5 to 455 are 45% ( EScore : 1e-110 ) identical to gb|AAF83950.1|AE003949_14 UDP-N-acetylglucosamine pyrophosphorylase between residues 6 and 456 in [Xylella fastidiosa]
Residues 181 to 456 are 60% ( EScore : 2e-97 ) identical to gb|AAA62081.1| (L10328) similar to Bacillus subtilis tms; similarity also includes f190 between residues 2 and 277 in [Escherichia coli]
Residues 5 to 451 are 40% ( EScore : 1e-87 ) identical to pir||E75473 UDP-N-acetylglucosamine pyrophosphorylase - Deinococcus radiodurans between residues 10 and 459 in [Deinococcus radiodurans]
Residues 9 to 456 are 38% ( EScore : 2e-85 ) identical to pir||S66080 UDP-N-acetylglucosamine pyrophosphorylase gcaD - Bacillus subtilis >467439|dbj|BAA05285.1| between residues 7 and 456 in [Bacillus subtilis]

COGS Summary:  COGS Search
BeTs to 8 clades of COG1207
COG name: N-acetylglucosamine-1-phosphate uridyltransferase (GlmU); Contains nucleotidyltransferase and I-patch acetyltransferase domains
Functional Class:  M
The phylogenetic pattern of COG1207 is -----qvcebrhuj------x
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001451 (Bacterial transferase hexapeptide repeat) with a combined E-value of 3e-12.
    IPB001451    397-432
    IPB001451    268-303
    IPB001451    314-349
    IPB001451    274-309
    IPB001451    320-355
    IPB001451    403-438
***** IPB001228 (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) with a combined E-value of 4.4e-10.
    IPB001228A    8-40


ProDom Summary:  Protein Domain Search
Residues 7-120 are 82% similar to a (TRANSFERASE COMPLETE PROTEOME BIOSYNTHESIS) protein domain (PD000318) which is seen in Q9CK29_PASMU.

Residues 290-344 are 67% similar to a (ADP-GLUCOSE TRANSFERASE PYROPHOSPHORYLASE) protein domain (PD000882) which is seen in GLMU_HAEIN.

Residues 345-391 are 74% similar to a (COMPLETE PROTEOME PYROPHOSPHORYLASE) protein domain (PD203566) which is seen in Q9KNH7_VIBCH.

Residues 121-216 are 73% similar to a (UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE) protein domain (PD009670) which is seen in GLMU_HAEIN.

Residues 217-287 are 70% similar to a (UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE) protein domain (PD172814) which is seen in GLMU_HAEIN.

Residues 279-329 are 54% similar to a (ACYLTRANSFERASE PROTEOME COMPLETE) protein domain (PD359885) which is seen in Q9KNH7_VIBCH.

Residues 366-449 are 64% similar to a (COMPLETE PROTEOME TRANSFERASE ACYLTRANSFERASE LIPID) protein domain (PD000343) which is seen in GLMU_HAEIN.

Residues 139-214 are 49% similar to a (TRANSFERASE PYROPHOSPHORYLASE ADP-GLUCOSE) protein domain (PD001252) which is seen in Q9CEF8_LACLA.



Paralogs:  Local Blast Search

HD1511 is paralogously related to HD1189 (8e-07), HD0630 (9e-06) and HD0688 (4e-05).


Pfam Summary:  Pfam Search
Residues 7 to 230 (E-value = 1.5e-08) place HD1511 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)

PDB Hit:
pdb|1FWY|A Chain A, Crystal Structure Of N-Acetylglucosamine 1-... 444 7e-126

Gene Protein Sequence:
MKMTPFSVVILAAGKGTRMYSDLPKVLHPIAGKSMVKHVIDTVKQMDAKQ
IHLVYGHGGDLLKTHLKTEPLNWVLQAEQLGTGHAMQQAATFFADDENIL
MLYGDTPLITAQTLTRLIAAKPANGIALLTVELADPTGYGRIIRQNGSVV
AIVEQKDASPTQLTICEVNTGVMVASGASFKKWLSRLNNQNAQGEYYITD
IIAMANQEGYSVQAVQANTLMEVEGANNHLQLAALERFYQQTQAEKLLLS
GVSLMDPHRFDLRGSLQYGKDIQIDVNVILEGEVKLGNRVRIGAGCILKN
CVVGDDVDIKPYSVFENAIIGNKAQVGPFARLRPGAKLEAESHVGNFVEI
KNAHIGKGSKVNHLAYVGDAEVGENCNLGAGVITCNYDGANKFKTTIGNN
VFVGSDVQLIAPVNIADGATIGAGATITKNIAENELVISRVPQRHIQGWQ
RPTKKK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAATGACCCCATTTAGCGTAGTGATTTTAGCCGCCGGTAAAGGCAC
ACGAATGTACTCAGATTTACCTAAAGTACTGCATCCTATTGCAGGTAAAT
CAATGGTCAAACACGTGATTGATACCGTCAAACAAATGGACGCCAAACAA
ATTCATTTAGTGTATGGGCACGGCGGTGACTTATTAAAAACACATTTAAA
AACAGAGCCACTCAATTGGGTTTTACAGGCAGAGCAATTAGGTACCGGTC
ACGCCATGCAACAAGCGGCTACTTTTTTTGCAGATGATGAAAATATTTTA
ATGTTATATGGCGATACGCCATTAATTACAGCACAAACCTTAACCCGCCT
TATCGCAGCAAAACCGGCAAATGGCATTGCATTATTAACAGTAGAATTAG
CAGATCCGACTGGTTATGGCAGAATTATTCGACAAAATGGCTCTGTAGTG
GCAATTGTAGAGCAAAAAGATGCTAGCCCAACCCAATTAACTATTTGTGA
AGTTAATACCGGTGTTATGGTCGCAAGTGGCGCCAGTTTTAAAAAATGGT
TAAGCCGTTTAAATAATCAGAATGCCCAAGGCGAATATTACATTACTGAT
ATTATTGCAATGGCAAATCAAGAAGGTTATAGCGTGCAAGCTGTTCAAGC
CAACACTTTAATGGAAGTAGAAGGCGCAAATAACCATCTACAATTAGCCG
CTTTAGAACGTTTTTACCAACAAACACAAGCAGAAAAATTATTATTATCC
GGCGTCAGTTTAATGGACCCACATCGCTTTGATCTTCGAGGTAGCCTACA
ATACGGAAAAGACATTCAAATTGATGTAAACGTAATCCTTGAAGGTGAAG
TTAAATTAGGTAACAGAGTACGTATCGGCGCGGGCTGTATTTTAAAAAAC
TGTGTGGTGGGTGATGATGTAGATATTAAACCTTATTCAGTTTTTGAAAA
TGCAATTATTGGCAATAAAGCACAAGTAGGGCCTTTCGCACGTTTACGTC
CCGGAGCTAAGCTTGAAGCAGAAAGCCACGTAGGCAACTTTGTTGAAATT
AAAAATGCTCACATTGGTAAAGGCTCAAAAGTCAATCATTTAGCTTATGT
CGGCGATGCTGAAGTGGGCGAAAATTGCAATTTAGGTGCCGGAGTCATTA
CCTGTAATTATGATGGCGCAAATAAATTCAAAACGACTATTGGCAATAAT
GTATTTGTTGGATCGGATGTACAGCTCATTGCCCCCGTGAACATTGCAGA
TGGCGCAACAATTGGTGCCGGTGCAACTATTACAAAAAATATCGCCGAAA
ATGAACTGGTGATTAGTCGTGTACCACAACGGCATATTCAAGGTTGGCAA
CGGCCAACAAAGAAAAAATAA


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