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Items: 10

1.

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

2.

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

3.
new record, indexing in progress
Family Accession:
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.

PLP-dependent aminotransferase family protein; bifunctional SDR family oxidoreductase/aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation| bifunctional extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase/aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

Date:
2017-03-02

Family Accession:
10797561
Method:
Sparcle

9.

glycine C-acetyltransferase

Catalyzes the formation of 2-amino-3-oxobutanoate from acetyl-CoA and glycine

GO Terms:
Molecular Function:
glycine C-acetyltransferase activity (GO:0008890)
Biological Process:
biosynthetic process (GO:0009058)
Molecular Function:
pyridoxal phosphate binding (GO:0030170)
Date:
2021-07-30

Family Accession:
NF005394.0
Method:
HMM

10.

BioF/Kbl family PLP-dependent acyltransferase

This HMM represents a family of pyridoxal phosphate-dependent acyltransferases, including a bifunctional protein from Thermus thermophilus shown to act both as a BioF (8-amino-7-oxononanoate synthase, EC 2.3.1.47) and as glycine C-acetyltransferase (EC 2.3.1.29). This enzyme family is also similar to 5-aminolevulinate synthase (EC 2.3.1.37). All those enzymes transfer an R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly or Ala), in two cases with release of CO2. Because of uncertainties about which member proteins will carry which activities, the functional name is deliberately left somewhat vague.

Date:
2021-03-24

Family Accession:
TIGR01825.1
Method:
HMM

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