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Items: 15

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.

CurL-like, PKS C-terminal

This entry represents the polyketide synthase C-terminal extension from cyanobacterial CurL polyketide synthase and similar proteins from other bacteria and fungi [1-5]. Paper describing PDB structure 2hg4. [1]. 16844787. The 2.7-Angstrom crystal structure of a 194-kDa homodimeric fragment of the 6-deoxyerythronolide B synthase. Tang Y, Kim CY, Mathews II, Cane DE, Khosla C;. Proc Natl Acad Sci U S A. 2006;103:11124-11129. Paper describing PDB structure 2qo3. [2]. 17719492. Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase. Tang Y, Chen AY, Kim CY, Cane DE, Khosla C;. Chem Biol. 2007;14:931-943. Paper describing PDB structure 4kc5. [3]. 24048471. Vinylogous chain branching catalysed by a dedicated polyketide synthase module. Bretschneider T, Heim JB, Heine D, Winkler R, Busch B, Kusebauch B, Stehle T, Zocher G, Hertweck C;. Nature. 2013;502:124-128. Paper describing PDB structure 4mz0. [4]. 24183970. Cyanobacterial polyketide synthase docking domains: a tool for engineering natural product biosynthesis. Whicher JR, Smaga SS, Hansen DA, Brown WC, Gerwick WH, Sherman DH, Smith JL;. Chem Biol. 2013;20:1340-1351. Paper describing PDB structure 4na1. [5]. 24508341. A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase. Gay DC, Gay G, Axelrod AJ, Jenner M, Kohlhaas C, Kampa A, Oldham NJ, Piel J, Keatinge-Clay AT;. Structure. 2014;22:444-451. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046877.1
Method:
HMM
3.

RhiE-like, KS-MAT linker domain

This entry represents a linker domain found in polyketide synthases, which connects the N-terminal domains with the B-domain as described in RhiE [1-3]. Paper describing PDB structure 4kc5. [1]. 24048471. Vinylogous chain branching catalysed by a dedicated polyketide synthase module. Bretschneider T, Heim JB, Heine D, Winkler R, Busch B, Kusebauch B, Stehle T, Zocher G, Hertweck C;. Nature. 2013;502:124-128. Paper describing PDB structure 4na1. [2]. 24508341. A close look at a ketosynthase from a trans-acyltransferase modular polyketide synthase. Gay DC, Gay G, Axelrod AJ, Jenner M, Kohlhaas C, Kampa A, Oldham NJ, Piel J, Keatinge-Clay AT;. Structure. 2014;22:444-451. Paper describing PDB structure 4tkt. [3]. 26420866. Structural and evolutionary relationships of "AT-less" type I polyketide synthase ketosynthases. Lohman JR, Ma M, Osipiuk J, Nocek B, Kim Y, Chang C, Cuff M, Mack J, Bigelow L, Li H, Endres M, Babnigg G, Joachimiak A, Phillips GN Jr, Shen B;. Proc Natl Acad Sci U S A. 2015;112:12693-12698. Paper describing PDB structure 5e5n. [4]. 26724270. The LINKS motif zippers trans-acyltransferase polyketide synthase assembly lines into a biosynthetic megacomplex. Gay DC, Wagner DT, Meinke JL, Zogzas CE, Gay GR, Keatinge-Clay AT;. J Struct Biol. 2016;193:196-205. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046639.1
Method:
HMM
4.

polyketide synthase docking domain-containing protein

Polyketide synthase (PKS) catalyzes the biosynthesis of polyketides, which are structurally and functionally diverse natural products in microorganisms and plants [1]. Type I modular PKSs are the large, multifunctional enzymes responsible for the production of a diverse family of structurally rich and often biologically active natural products. The efficiency of acyl transfer at the interfaces of the individual PKS proteins is thought to be governed by helical regions, termed docking domains (dd). Two such N-terminal domains dimerise to form amphipathic parallel alpha-helical coiled coils: dimerisation is essential for protein function [1]. [1]. 12954331. The structure of docking domains in modular polyketide synthases. Broadhurst RW, Nietlispach D, Wheatcroft MP, Leadlay PF, Weissman KJ;. Chem Biol. 2003;10:723-731. [2]. 26611533. Multimodular type I polyketide synthases in algae evolve by module duplications and displacement of AT domains in trans. Shelest E, Heimerl N, Fichtner M, Sasso S;. BMC Genomics. 2015;16:1015. [3]. 19146481. Structural basis for binding specificity between subclasses of modular polyketide synthase docking domains. Buchholz TJ, Geders TW, Bartley FE 3rd, Reynolds KA, Smith JL, Sherman DH;. ACS Chem Biol. 2009;4:41-52. (from Pfam)

GO Terms:
Molecular Function:
transferase activity (GO:0016740)
Date:
2024-10-16
Family Accession:
NF020559.5
Method:
HMM
5.

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
6.

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
7.

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
8.

acyltransferase domain-containing protein

Date:
2024-08-14
Family Accession:
NF012901.5
Method:
HMM
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.
new record, indexing in progress
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14.
new record, indexing in progress
Family Accession:
15.

type I polyketide synthase

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

Date:
2024-10-01
Family Accession:
12098227
Method:
Sparcle
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