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Mycoplasma genitalium Search Results

Record: 1 of 1  
MiniMap tRNA-Asp-1 tRNA-Phe-1 tRNA-Pro-1 tRNA-Met-3 tRNA-Met-2 tRNA-Met-1 tRNA-Cys-1 tRNA-Ser-2 IGR156 IGR158 IGR155 IGR157 MG211.1 MG211 pfk, - MG215 MG217 MG213 pyk, - MG216 hmw2, - MG218 MG211.1 MG211 pfk, - MG215 MG217 MG213 pyk, - MG216 hmw2, - MG218 Type: tandem, Name:  - 5 Type: tandem, Name:  - 6 Type: direct, Name:  - 24 Type: inverted, Name:  - 56 Type: direct, Name:  - 24 Type: inverted, Name:  - 56 pfk, - MG215 MG217 MG213 pyk, - MG216 hmw2, - MG218 MG214 plsC, - MG212 MG214 plsC, - MG212 MG211 MG211.1
* Calculated from Protein Sequence

Gene ID: MG216

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pyk  

Definition:
pyruvate kinase

Gene Start:
255594

Gene Stop:
257117

Gene Length:
1524

Molecular Weight*:
57323

pI*:
10.04

Net Charge*:
17.95

EC:
2.7.1.40  

Functional Class:
Energy metabolism; Glycolysis and Gluconeogenesis  

Pathway: pathway table
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis
Carbohydrate Metabolism; Pyruvate metabolism
Energy Metabolism; Methane metabolism

Primary Evidence:
Manolukas JT, Barile MF, Chandler DK, Pollack JD. 1988. Presence of anaplerotic reactions and transamination, and the absence of the tricarboxylic acid cycle in mollicutes. J Gen. Microbiol. 134 (Pt 3):791-800. Medline: 3141576.

Secondary Evidence:
Bledig SA, Ramseier TM, Saier MH Jr. 1996. FruR mediates catabolite activation of pyruvate kinase (pykF) gene expression in Escherichia coli. J Bacteriol 178(1):280-3. Medline: 8550429.

Ponce E, Flores N, Martinez A, Valle F, Bolivar F. 1995. Cloning of the two pyruvate kinase isoenzyme structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis. J Bacteriol 177(19):5719-22. Medline: 7559366.

Valentini G, Stoppini M, Iadarola P, Malcovati M, Ferri G, Speranza ML. 1993. Divergent binding sites in pyruvate kinases I and II from Escherichia coli. Biol Chem Hoppe Seyler 374(1):69-74. Medline: 8439398.

Valentini G, Stoppini M, Speranza ML, Malcovati M, Ferri G. 1991. Bacterial pyruvate kinases have a shorter N-terminal domain. Biol Chem Hoppe Seyler 372(2):91-3. Medline: 1859631.

Garrido-Pertierra A, Cooper RA. 1983. Evidence for two distinct pyruvate kinase genes in Escherichia coli K-12. FEBS Lett 162(2):420-2. Medline: 6354749.

Malcovati M, Kornberg HL. 1969. Two types of pyruvate kinase in Escherichia coli K12. Biochim Biophys Acta 178(2):420-3. Medline: 4890755.

Comment:
In E. coli, pyruvate kinase becomes sensitive to tryptic attack and thermolabile after binding of the allosteric activator fructose 1,6-bisphosphate. When phosphoenolpyruvate and Mg2+ bind to pyruvate kinase, it transforms pyruvate kinase into a highly thermostable conformation (Speranza ML, et al., 1992. Medline: 1500282). In E. coli, pyruvate kinase is inhibited by Li+ (Umeda K, et al., 1984. Medline: 6389501).

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to pyruvate kinase sequences, e.g.
residues 1-508 are 78% similar to the predicted KPYC_MYCPN. Residues 5-371 are 40% similar to the B.subtils enzyme (Z99118).
MG216 is significantly similar to the predicted pyruvate kinase from B. burgdorferi (AE001141).

MG216 is orthologously related to MP0533: residues 1-508 of MG216 are 78% similar to residues 1-508 of MP0533, a predicted pyruvate kinase from M. pneumoniae. MG216 is significantly similar to predicted pyruvate kinases from U. urealyticum (UU186), C. trachmoatis (CT332), and C. pneumoniae (CPn0097).

COGS Summary:  COGS Search
The phylogenetic pattern of COG0469 is EhgpCmY-.
COG name: Pyruvate kinase.
Functional Class: C
BeTs to e-g-cmy-.


Blocks Summary:  Blocks Search
Residues 32-459 span eight regions that are members of blocks
BL00110A-G (pyruvate kinase).

ProDom Summary:  Protein Domain Search
Residues 1-46, 47-365, 377-508 constitute defined domains of
KPYK_MYCGE. Residues 39-366 are 39% similar to a pyk domain of
KPYK_CORGL and residues 462-500 are 35% similar to a domain of
KYPK_METJA.

Paralogs:  Local Blast Search
No evidence of paralogs in M. genitalium.

Pfam Summary:  Pfam Search
Residues 5 to 374 (E-value = 5.9e-121) place MG216 in the PK family which is described as Pyruvate kinase, barrel domain (PF00224)

PDB Hit:
gi|1310978|pdb|1PKY|A Chain A, Pyruvate Kinase From E. Coli In The T-State Allostery Mol_id: 1; Molecule: Pyruvate Kinase; Chain: A, B, C, D; Ec: 2.7.1.40.

Gene Protein Sequence:
MIDHLKRTKIIATCGPALTKSLVSLKMLDDNEYAAIKKVAYANIEAIIKS
GVSVIRLNFSHGTHEEQQVRIKIVRDVAKAMNIPVSIMLDTNGPEIRIVE
TKKEGLKITKDSEVIINTMSKMIASDNQFAVSDASGKYNMVNDVNIGQKI
LVDDGKLTLVVTRVDKQHNQVICVAKNDHTVFTKKRLNLPNAQYSIPFLS
EKDLKDIDFGLSQGIDYIAASFVNTVADIKQLRDYLKLKNASGVKIIAKI
ESNHALNNIDKIIKASDGIMVARGDLGLEIPYYQVPYWQRYMIKACRFFN
KRSITATQMLDSLEKNIQPTRAEVTDVYFAVDRGNDATMLSGETASGLYP
LNAVAVMQKIDKQSETFFDYQYNVNYYLKNSTANKSRFWHNVVLPLTKKT
VPKRKLVNSAFKYDFIVYPTNNINRIYALSNARLAAAVIILTNNKRVYTG
HGVDYGIFCYLIDKNPNQLTKAELIELAWKAINHYQAYGDLEKLKQCLAV
YNETIINL

Gene Nucleotide Sequence:  Sequence Viewer
ATGATTGACCATTTAAAAAGAACAAAGATAATCGCTACCTGTGGCCCAGC
TTTAACAAAAAGCTTGGTTAGCTTAAAGATGCTTGATGATAATGAGTATG
CAGCTATTAAAAAGGTTGCTTATGCCAACATTGAAGCAATTATTAAAAGT
GGGGTTAGTGTGATTAGGCTTAACTTCTCTCATGGTACCCATGAAGAACA
ACAAGTGAGGATCAAGATAGTAAGGGATGTAGCGAAAGCAATGAACATCC
CTGTTTCTATTATGTTAGATACAAATGGTCCTGAGATCAGGATAGTAGAA
ACTAAAAAAGAGGGTTTGAAAATCACCAAAGATAGTGAAGTGATTATCAA
CACCATGAGTAAAATGATCGCTAGTGACAACCAGTTTGCTGTCAGTGATG
CTAGTGGCAAATACAACATGGTTAATGATGTGAATATAGGTCAGAAAATC
CTTGTTGATGATGGTAAGTTAACCCTGGTTGTCACAAGGGTTGACAAACA
ACATAACCAGGTTATCTGTGTTGCAAAAAACGACCACACAGTTTTCACTA
AAAAAAGACTTAACCTACCCAACGCACAGTACTCTATCCCTTTTCTCAGT
GAAAAGGATCTGAAGGATATTGACTTTGGTTTAAGCCAAGGTATTGACTA
TATTGCTGCCTCTTTTGTTAATACTGTTGCAGATATTAAACAACTGAGAG
ATTATCTGAAATTAAAGAATGCTAGTGGGGTGAAGATCATCGCTAAGATT
GAATCTAATCATGCTTTAAATAACATTGATAAGATCATTAAAGCTAGCGA
TGGGATTATGGTTGCTAGGGGTGATTTGGGCCTTGAAATCCCTTATTACC
AAGTCCCTTACTGACAAAGGTACATGATTAAAGCTTGTCGCTTTTTTAAC
AAGCGTTCTATTACTGCAACCCAAATGCTTGATTCACTAGAAAAAAACAT
CCAACCAACCCGAGCTGAAGTGACTGATGTTTACTTTGCAGTTGATCGGG
GTAATGATGCAACTATGTTAAGTGGGGAAACTGCTAGTGGGCTTTACCCT
TTAAATGCAGTAGCGGTGATGCAAAAGATTGATAAACAATCAGAAACCTT
CTTTGATTACCAGTATAACGTTAACTATTATTTGAAAAACTCCACGGCAA
ATAAAAGTAGGTTTTGACACAACGTTGTTTTACCTTTAACAAAAAAGACT
GTTCCTAAAAGAAAACTTGTTAACAGTGCCTTTAAGTATGACTTTATTGT
CTATCCTACTAATAACATTAACAGGATCTATGCATTATCAAACGCACGCT
TAGCAGCAGCAGTTATTATTTTAACCAACAACAAACGGGTTTACACTGGC
CATGGTGTTGATTATGGGATCTTCTGTTATTTAATTGATAAAAACCCCAA
CCAGCTAACCAAAGCTGAACTGATTGAACTTGCTTGAAAAGCAATTAACC
ACTATCAGGCTTATGGTGATTTAGAAAAACTCAAACAGTGTTTAGCTGTC
TATAATGAAACAATTATCAATCTT


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