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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR617 IGR615 IGR618 IGR619 IGR620 IGR622 IGR616 IGR623 IGR621 HD0868 sapF, - HD0863 fba, - HD0864 pgk, - HD0865 HD0866 parE, - HD0870 HD0869 HD0872 lolD,devA, - HD0860 lolE, - HD0861 lolC, - HD0858 HD0868 sapF, - HD0863 fba, - HD0864 pgk, - HD0865 HD0866 parE, - HD0870 HD0869 HD0872 lolD,devA, - HD0860 lolE, - HD0861 lolC, - HD0858 HD0868 sapF, - HD0863 fba, - HD0864 pgk, - HD0865 HD0866 parE, - HD0870 HD0869 HD0872 lolD,devA, - HD0860 lolE, - HD0861 lolC, - HD0858
* Calculated from Protein Sequence

Gene ID: HD0865

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
pgk  

Definition:
phosphoglycerate kinase

Gene Start:
692106

Gene Stop:
690931

Gene Length:
1176

Molecular Weight*:
41513

pI*:
5.10

Net Charge*:
-8.90

EC:
2.7.2.3  

Functional Class:
Energy metabolism; Glycolysis and gluconeogenesis  

Pathway: pathway table
Carbon fixation
Glycolysis /Gluconeogenesis

Secondary Evidence:
Alefounder,P.R. and Perham,R.N.
Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli.
Mol. Microbiol. 3(6): 723-732. 1989.
Medline: 89313302.

Bond CS, White MF, Hunter WN.
Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex.
J Mol Biol. 2002 Mar 8;316(5):1071-81.
PMID: 11884145

Bond CS, White MF, Hunter WN.
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase.
J Biol Chem. 2001 Feb 2;276(5):3247-53.
PMID: 11038361


Comment:
0

Blast Summary:  PSI-Blast Search
Numerous significant hits using gapped BLAST to phosphoglycerate kinases from H. influenzae (1172458), E. coli (129920), Pseudomonas sp. (6468411), N. meningitidis (7379019), among others.

HD0865 is similar to predicted phosphoglycerate kinases from C. trachomatis (CT693), T. pallidum (TP0538), M. genitalium (MG300), M. pneumoniae (MP0412), C. pneumoniae (CPn0679), and U. urealyticum (UU279).

COGS Summary:  COGS Search
BeTs to 16 clades of COG0126
COG name: 3-phosphoglycerate kinase
Functional Class:  G
The phylogenetic pattern of COG0126 is amtkyqvcebrhujgpolin-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001576 (Phosphoglycerate kinase family) with a combined E-value of 2.3e-125.
    IPB001576A    10-36
    IPB001576B    54-63
    IPB001576C    105-119
    IPB001576D    135-155
    IPB001576E    164-210
    IPB001576F    244-264
    IPB001576G    285-323
    IPB001576H    341-385


ProDom Summary:  Protein Domain Search
Residues 6-386 are 80% similar to a (KINASE PHOSPHOGLYCERATE TRANSFERASE) protein domain (PD000619) which is seen in PGK_PASMU.



Paralogs:  Local Blast Search

HD0865 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 1 to 389 (E-value = 8e-191) place HD0865 in the PGK family which is described as Phosphoglycerate kinase (PF00162)

PDB Hit:
pdb|1PHP| 3-Phosphoglycerate Kinase (Pgk) (E.C.2.7.2.3) 301 1e-082
pdb|1VPE| Crystallographic Analysis Of Phosphoglycerate Kina... 275 8e-075
pdb|16PK| Phosphoglycerate Kinase From Trypanosoma Brucei Bi... 242 4e-065

Gene Protein Sequence:
MSVKKMADLDLTGKRLFIRADLNVPVKEGKITSDARIRATIPTLKLALQK
GAKVMVTSHLGRPTEGVFEEANSLQPVVDYLNASDLGVPVRLVRDYLDGV
EVNQNEIVVLENVRINKGEKKNDAELAKKYAALCDIFVMDAFGTAHRAEC
STYGIAEFAPIACAGPLLAAELEALGKALKEPQRPMLAIVGGSKVSTKLT
VLDSLSKIADQLIVGGGIANIFIAAEGHNVGKSLYEADLIPEAKRLASTT
HIPVPVDVRVGTEFSETATATEKLVSEVTADESIFDIGDKSAEELAHIIK
SAKTIFWNGPVGVFEFANFRKGTEIISNAIAEATANGAFSIAGGGDTLAA
IDLFGIADKISYISTGGGAFLEFVEGKVLPAVEILEKRANS$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCCGTTAAAAAAATGGCTGACCTTGATTTAACTGGTAAACGTTTATT
CATTCGTGCTGATCTTAACGTCCCCGTAAAGGAAGGTAAAATCACCTCAG
ATGCTCGTATTCGAGCTACAATCCCGACGTTAAAATTAGCCTTACAAAAA
GGTGCGAAAGTGATGGTGACATCACACTTAGGTCGTCCAACTGAAGGCGT
ATTTGAAGAAGCAAATTCATTACAACCTGTAGTTGATTACTTAAATGCAT
CTGATTTAGGTGTGCCTGTACGGCTAGTGCGTGACTATTTAGATGGTGTA
GAAGTCAACCAAAATGAAATTGTTGTCCTTGAAAATGTGCGCATAAATAA
AGGCGAGAAAAAAAATGATGCTGAACTAGCAAAAAAATATGCTGCCTTAT
GCGATATTTTTGTTATGGACGCATTTGGTACTGCACACCGCGCAGAATGC
TCAACCTATGGCATAGCAGAATTTGCACCTATAGCTTGTGCAGGGCCATT
ATTGGCAGCCGAGCTTGAAGCATTAGGTAAAGCATTAAAAGAACCACAGC
GCCCAATGTTAGCAATTGTAGGTGGTTCAAAAGTGTCAACCAAACTAACC
GTTTTAGATAGCCTCTCAAAAATTGCTGATCAACTGATTGTCGGGGGGGG
CATTGCCAACATATTCATTGCGGCAGAAGGGCATAATGTAGGTAAATCCT
TATATGAAGCTGATTTAATCCCAGAAGCAAAACGATTAGCGTCAACCACT
CATATTCCTGTTCCTGTTGATGTGCGTGTAGGTACAGAATTTTCTGAAAC
AGCCACAGCAACCGAAAAATTAGTATCAGAAGTGACCGCCGATGAATCTA
TCTTCGATATTGGCGACAAATCCGCTGAAGAATTAGCTCATATTATTAAA
TCCGCGAAAACGATTTTTTGGAATGGCCCTGTAGGGGTCTTTGAATTCGC
GAACTTCCGTAAAGGAACGGAAATTATCTCAAATGCAATTGCAGAAGCCA
CTGCAAATGGGGCATTTTCTATCGCAGGTGGTGGCGATACATTGGCTGCA
ATTGATTTATTTGGCATTGCCGATAAAATTTCTTATATCTCAACCGGCGG
CGGTGCTTTCTTAGAATTTGTAGAAGGCAAAGTATTACCTGCTGTTGAAA
TTTTAGAAAAACGTGCAAACAGCTAA


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