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Links from Protein

Items: 20

1.

ketoacyl-synthetase C-terminal extension domain-containing protein

KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human. (from Pfam)

Date:
2024-08-14
Family Accession:
NF027522.5
Method:
HMM
2.

Beta-ketoacyl synthase, C-terminal domain

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. [1]. 9482715. Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y;. EMBO J 1998;17:1183-1191. (from Pfam)

Date:
2024-10-16
Family Accession:
NF014819.5
Method:
HMM
3.

phosphopantetheine-binding protein

A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012759.5
Method:
HMM
4.

thioesterase domain-containing protein

Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa. [1]. 9560421. Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis. Schneider A, Marahiel MA;. Arch Microbiol 1998;169:404-410. (from Pfam)

GO Terms:
Biological Process:
biosynthetic process (GO:0009058)
Date:
2024-10-16
Family Accession:
NF013166.5
Method:
HMM
5.

beta-ketoacyl synthase N-terminal-like domain-containing protein

The structure of beta-ketoacyl synthase is similar to that of the thiolase family (Pfam:PF00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine [1]. [1]. 9482715. Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes. Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y;. EMBO J 1998;17:1183-1191. (from Pfam)

Date:
2024-10-16
Family Accession:
NF012337.5
Method:
HMM
6.

acyltransferase domain-containing protein

Date:
2024-08-14
Family Accession:
NF012901.5
Method:
HMM
7.
new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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11.
new record, indexing in progress
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new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.
new record, indexing in progress
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18.
new record, indexing in progress
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19.

polyketide synthase Pks13

Gene:
pks13
GO Terms:
Biological Process:
mycolic acid biosynthetic process (GO:0071768)
Date:
2021-11-19
Family Accession:
NF040607.1
Method:
HMM
20.

type I polyketide synthase

type I polyketide synthase assembles complex polyketides via the head-to-tail fusion of acyl and malonyl building blocks

Date:
2021-02-12
Family Accession:
12220201
Method:
Sparcle
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