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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR485 IGR483 IGR484 IGR481 IGR480 IGR488 IGR489 IGR486 IGR487 IGR482 yadR, - HD0684 HD0682 tyrS, - HD0693 rpS21,rpsU,rs21, - HD0689 neuA,siaB, - HD0685 rmlA, - HD0688 lst, - HD0686 menA, - HD0683 rmlB, - HD0687 dnaG, - HD0690 rpoD, - HD0691 yadR, - HD0684 HD0682 tyrS, - HD0693 rpS21,rpsU,rs21, - HD0689 neuA,siaB, - HD0685 rmlA, - HD0688 lst, - HD0686 menA, - HD0683 rmlB, - HD0687 dnaG, - HD0690 rpoD, - HD0691 yadR, - HD0684 HD0682 tyrS, - HD0693 rpS21,rpsU,rs21, - HD0689 neuA,siaB, - HD0685 rmlA, - HD0688 lst, - HD0686 menA, - HD0683 rmlB, - HD0687 dnaG, - HD0690 rpoD, - HD0691
* Calculated from Protein Sequence

Gene ID: HD0688

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
rmlA  

Definition:
glucose-1-phosphate thymidyltransferase

Gene Start:
543372

Gene Stop:
544259

Gene Length:
888

Molecular Weight*:
33169

pI*:
6.60

Net Charge*:
-1.40

EC:
2.7.7.24  

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

Pathway: pathway table
Nucleotide sugars metabolism

Primary Evidence:
Tullius,M.V., Munson,R.S. Jr., Wang,J. and Gibson,B.W.
Purification, cloning, and expression of a cytidine
5'-monophosphate N-acetylneuraminic acid synthetase from
Haemophilus ducreyi
J. Biol. Chem. 271 (26), 15373-15380 (1996)
MEDLINE: 96279048

Bozue,J.A., Tullius,M.V., Wang,J., Gibson,B.W. and Munson,R.S. Jr.
Haemophilus ducreyi produces a novel sialyltransferase.
Identification of the sialyltransferase gene and construction of
mutants deficient in the production of the sialic acid-containing
glycoform of the lipooligosaccharide
J. Biol. Chem. 274 (7), 4106-4114 (1999)
MEDLINE: 99134335

Secondary Evidence:
Marolda,C.L. and Valvano,M.A.
Genetic analysis of the dTDP-rhamnose biosynthesis region of the
Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of
functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene
J. Bacteriol. 177 (19), 5539-5546 (1995)
Medline: 96032389

Yoshida,Y., Nakano,Y., Yamashita,Y. and Koga,T.
Identification of a genetic locus essential for serotype b-specific antigen synthesis in Actinobacillus actinomycetemcomitans
Infect. Immun. 66 (1), 107-114 (1998)
MEDLINE: 98084462

Yoshida,Y., Nakano,Y., Nezu,T., Yamashita,Y. and Koga,T.
A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose
J. Biol. Chem. 274 (24), 16933-16939 (1999)
MEDLINE: 99287888

Sivaraman J, Sauve V, Matte A, Cygler M.
Crystal Structure of Escherichia coli Glucose-1-Phosphate Thymidylyltransferase (RffH) Complexed with dTTP and Mg2+
J Biol Chem. 2002 Nov 15;277(46):44214-44219.
PMID: 12171937

Graninger M, Kneidinger B, Bruno K, Scheberl A, Messner P.
Homologs of the Rml enzymes from Salmonella enterica are responsible for dTDP-beta-L-rhamnose biosynthesis in the
gram-positive thermophile Aneurinibacillus thermoaerophilus DSM 10155.
Appl Environ Microbiol. 2002 Aug;68(8):3708-15.
PMID: 12147463


Comment:
This protein is homologous to rfbA in other E.coli strains (see Marolda and Valvano).

Blast Summary:  PSI-Blast Search
This sequence corresponds to the previously reported gi 6677602 in GenBank.

Many very strong hits in gapped BLAST to glucose-1-phosphate thymidyltransferase (dTDP-glucose synthase, dTDP-glucose phosphorylase) proteins; e.g., residues 2-289 are 71% similar to RFBA_NEIME [1710099], residues 2-291 are 71% similar to the sequence for glucose-1-phosphate thymidylyltransferase in Actinobacillus actinomycetemcomitans [7592816], residues 2-287 are 70% simiilar to RFBA_NEIGO [585825], and residues 2-293 are 66% similar to RFFH_ECOLI [2507298].

COGS Summary:  COGS Search
BeTs to 8 clades of COG1209
COG name: dTDP-glucose pyrophosphorylase
Functional Class: M
The phylogenetic pattern of COG1209 is a-tk--vcEbr----------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 3-143 are 60% similar to a (TRANSFERASE COMPLETE PROTEOME BIOSYNTHESIS) protein domain (PD000318) which is seen in Q9RZB2_DEIRA.

Residues 26-109 are identical to a (TRANSFERASE GLUCOSE-1-PHOSPHATE) protein domain (PD307342) which is seen in Q9X4A3_HAEDU.

Residues 245-293 are identical to a (TRANSFERASE GLUCOSE-1-PHOSPHATE) protein domain (PD002767) which is seen in Q9X4A3_HAEDU.

Residues 110-143 are identical to a (TRANSFERASE GLUCOSE-1-PHOSPHATE) protein domain (PD415991) which is seen in Q9X4A3_HAEDU.

Residues 144-240 are 98% similar to a (TRANSFERASE GLUCOSE-1-PHOSPHATE) protein domain (PD000406) which is seen in Q9X4A3_HAEDU.



Paralogs:  Local Blast Search
HD0688 is paralogously related to HD1431 (5e-12) and HD1511 (2e-05).


Pfam Summary:  Pfam Search
Residues 3 to 241 (E-value = 1.2e-104) place HD0688 in the NTP_transferase family which is described as Nucleotidyl transferase (PF00483)

PDB Hit:
pdb|1FXO|A Chain A, The Structural Basis Of The Catalytic Mecha... 358 5e-100
pdb|1G23|A Chain A, The Structural Basis Of The Catalytic Mecha... 352 3e-098

Gene Protein Sequence:
MMKGIILAGGSGTRLYPITRGISKQLLPVYNKPMIYYPLSVLMLAGIREI
LVITTPVDHQHFKALLGDGSHFGIHIDYAIQAKPAGLAEAFIIGEPFIGK
DNVCLVLGDNIFYGQGFTQILSVAANRQQGATLFGYQVNNPARFGVVEFD
QDLRILTLEEKPQKPKSDWAVTGLYFYDNRVIEFAKQVTPSARGELEITD
INQRYLQEGMLHLQLLGRGFAWFDTGTYDSLHEAAAFVKTIEHLQKLQVA
CLEEIAWRKGWLTDIDVITLAEPMIQNEYGQYLLALVQQQRKYKA$

Gene Nucleotide Sequence:  Sequence Viewer
ATGATGAAAGGGATTATTTTAGCGGGCGGATCTGGCACACGTTTATACCC
AATTACTCGCGGGATCTCTAAACAGTTATTGCCGGTGTATAATAAGCCAA
TGATTTATTATCCACTTTCAGTATTAATGTTGGCAGGGATCCGAGAGATT
TTGGTGATCACCACACCCGTGGATCATCAGCATTTTAAAGCATTATTAGG
AGATGGCAGTCATTTCGGTATTCACATTGATTATGCTATTCAAGCTAAGC
CTGCAGGATTAGCAGAAGCGTTTATTATTGGTGAGCCATTTATCGGCAAA
GATAATGTTTGTTTGGTATTAGGCGATAATATCTTTTATGGGCAAGGTTT
TACTCAAATTCTATCGGTTGCGGCAAATCGCCAGCAAGGTGCTACTCTTT
TTGGTTATCAAGTGAATAATCCCGCGCGCTTTGGCGTTGTGGAGTTTGAT
CAAGATTTACGTATTTTAACATTGGAAGAAAAGCCACAAAAGCCTAAATC
TGATTGGGCGGTTACCGGTCTTTATTTTTACGATAATCGCGTCATTGAGT
TTGCTAAGCAAGTCACCCCTTCAGCACGTGGAGAACTTGAAATCACGGAT
ATTAATCAACGCTATTTACAAGAAGGTATGCTACATTTGCAATTGCTTGG
TCGCGGATTTGCTTGGTTTGATACCGGCACTTATGATAGTTTGCATGAAG
CGGCCGCTTTTGTAAAAACTATTGAGCATTTGCAGAAGTTACAGGTAGCT
TGTTTGGAAGAGATTGCGTGGCGTAAAGGTTGGTTGACTGATATCGATGT
AATCACTTTGGCTGAGCCGATGATACAAAATGAATATGGTCAGTACTTAT
TAGCTTTAGTACAACAACAGCGTAAATATAAGGCTTAA


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