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Links from Protein

Items: 13

1.

pyruvate kinase alpha/beta domain-containing protein

Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, 3,4]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site [2,4,5]. [1]. 9308890. Ligand-induced domain movement in pyruvate kinase: structure of. the enzyme from rabbit muscle with Mg2+, K+, and. L-phospholactate at 2.7 A resolution.. Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH;. Arch Biochem Biophys 1997;345:199-206.. [2]. 10751408. The allosteric regulation of pyruvate kinase.. Valentini G, Chiarelli L, Fortin R, Speranza ML, Galizzi A,. Mattevi A;. J Biol Chem. 2000;275:18145-18152.. [3]. 12798932. Pyruvate kinase: current status of regulatory and functional. properties.. Munoz ME, Ponce E;. Comp Biochem Physiol B Biochem Mol Biol. 2003;135:197-218.. [4]. 11960989. Structure and function of human erythrocyte pyruvate kinase.. Molecular basis of nonspherocytic hemolytic anemia.. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A,. Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A;. J Biol Chem. 2002;277:23807-23814.. [5]. 29748232. An allostatic mechanism for M2 pyruvate kinase as an amino-acid. sensor.. Yuan M, McNae IW, Ch. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-08-14
Family Accession:
NF014886.5
Method:
HMM
2.

aldolase/citrate lyase family protein

This family includes 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase and 4-hydroxy-2-oxovalerate aldolase. [1]. 9073078. The bphDEF meta-cleavage pathway genes involved in. biphenyl/polychlorinated biphenyl degradation are located on a. linear plasmid and separated from the initial bphACB genes in. Rhodococcus sp. strain RHA1.. Masai E, Sugiyama K, Iwashita N, Shimizu S, Hauschild JE, Hatta. T, Kimbara K, Yano K, Fukuda M;. Gene 1997;187:141-149.. [2]. 8529896. Sequence of the Escherichia coli C homoprotocatechuic acid. degradative operon completed with that of the. 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase-encoding gene. (hpcH).. Stringfellow JM, Turpin B, Cooper RA;. Gene 1995;166:73-76. (from Pfam)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Date:
2024-08-14
Family Accession:
NF015297.5
Method:
HMM
3.

pyruvate kinase

This is the barrel domain of pyruvate kinases. This domain represents the beta/alpha barrel and the small beta-barrel domain inserted within it. The active site is found in a cleft between the two domains [1,2,3,4]. [1]. 9308890. Ligand-induced domain movement in pyruvate kinase: structure of. the enzyme from rabbit muscle with Mg2+, K+, and. L-phospholactate at 2.7 A resolution.. Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH;. Arch Biochem Biophys 1997;345:199-206.. [2]. 12798932. Pyruvate kinase: current status of regulatory and functional. properties.. Munoz ME, Ponce E;. Comp Biochem Physiol B Biochem Mol Biol. 2003;135:197-218.. [3]. 11960989. Structure and function of human erythrocyte pyruvate kinase.. Molecular basis of nonspherocytic hemolytic anemia.. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A,. Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A;. J Biol Chem. 2002;277:23807-23814.. [4]. 29748232. An allostatic mechanism for M2 pyruvate kinase as an amino-acid. sensor.. Yuan M, McNae IW, Chen Y, Blackburn EA, Wear MA, Michels PAM,. Fothergill-Gilmore LA, Hupp T, Walkinshaw MD;. Biochem J. 2018;475:1821-1837. (from Pfam)

GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
pyruvate kinase activity (GO:0004743)
Biological Process:
glycolytic process (GO:0006096)
Molecular Function:
potassium ion binding (GO:0030955)
Date:
2024-08-14
Family Accession:
NF012449.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

pyruvate kinase

pyruvate kinase catalyzes the phosphorylation of pyruvate to form phosphoenolpyruvate and functions in regulating glycolysis

Date:
2023-03-02
Family Accession:
11481784
Method:
Sparcle
11.

pyruvate kinase

Catalyzes the formation of phosphoenolpyruvate from pyruvate

Date:
2020-10-26
Family Accession:
NF004491.0
Method:
HMM
12.

pyruvate kinase

This enzyme is a homotetramer. Some forms are active only in the presence of fructose-1,6-bisphosphate or similar phosphorylated sugars.

Gene:
pyk
GO Terms:
Molecular Function:
magnesium ion binding (GO:0000287)
Molecular Function:
pyruvate kinase activity (GO:0004743)
Biological Process:
glycolytic process (GO:0006096)
Molecular Function:
potassium ion binding (GO:0030955)
Date:
2024-05-16
Family Accession:
TIGR01064.1
Method:
HMM
13.

pyruvate kinase

Catalyzes the formation of phosphoenolpyruvate from pyruvate

Date:
2020-10-26
Family Accession:
NF004978.0
Method:
HMM
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