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Links from Protein

Items: 13

1.

methionine gamma-lyase family protein

This is a putative pyridoxal 5'-phosphate-dependent methionine gamma-lyase enzyme involved in methionine catabolism. [1]. 9190812. Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida. Inoue H, Inagaki K, Eriguchi SI, Tamura T, Esaki N, Soda K, Tanaka H;. J Bacteriol. 1997;179:3956-3962. [2]. 9488680. The primitive protozoon Trichomonas vaginalis contains two methionine gamma-lyase genes that encode members of the gamma-family of pyridoxal 5'-phosphate-dependent enzymes. McKie AE, Edlind T, Walker J, Mottram JC, Coombs GH;. J Biol Chem. 1998;273:5549-5556. (from Pfam)

Date:
2024-10-16
Family Accession:
NF018540.5
Method:
HMM
2.

aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2024-08-14
Family Accession:
NF012382.5
Method:
HMM
3.

PLP-dependent transferase

This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor. [1]. 8831789. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A;. J Mol Biol 1996;262:202-224. [2]. 9843488. Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution. Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A;. EMBO J 1998;17:6827-6838. (from Pfam)

GO Terms:
Biological Process:
transsulfuration (GO:0019346)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2024-10-16
Family Accession:
NF013237.5
Method:
HMM
4.

DegT/DnrJ/EryC1/StrS family aminotransferase

The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA Swiss:P72454, StsC Swiss:P77952 and StsS [1]. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyses the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin [1]. [1]. 9238101. Identification of stsC, the gene encoding the L-glutamine:scyllo-inosose aminotransferase from streptomycin-producing Streptomycetes. Ahlert J, Distler J, Mansouri K, Piepersberg W;. Arch Microbiol 1997;168:102-113. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013227.5
Method:
HMM
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.
new record, indexing in progress
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11.
new record, indexing in progress
Family Accession:
12.

cystathionine gamma-synthase

cystathionine gamma-synthase catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction

Date:
2019-05-06
Family Accession:
10792984
Method:
Sparcle
13.

cystathionine gamma-synthase

Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine

GO Terms:
Biological Process:
transsulfuration (GO:0019346)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2021-07-30
Family Accession:
NF005871.0
Method:
HMM
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