A0A5Q0GYB2 · A0A5Q0GYB2_SACSY
- ProteinType I polyketide synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids4092 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
Function
function
Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain.
Catalytic activity
- (2E)-butenoyl-[ACP] + H+ + NADPH = butanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- (2E)-decenoyl-[ACP] + H+ + NADPH = decanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- (2E)-dodecenoyl-[ACP] + H+ + NADPH = dodecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- (2E)-hexadecenoyl-[ACP] + H+ + NADPH = hexadecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- (2E)-hexenoyl-[ACP] + H+ + NADPH = hexanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- (2E)-octadecenoyl-[ACP] + H+ + NADPH = NADP+ + octadecanoyl-[ACP]This reaction proceeds in the forward direction.
- (2E)-octenoyl-[ACP] + H+ + NADPH = NADP+ + octanoyl-[ACP]This reaction proceeds in the forward direction.
- (2E)-tetradecenoyl-[ACP] + H+ + NADPH = NADP+ + tetradecanoyl-[ACP]This reaction proceeds in the forward direction.
- (3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- (3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] + H2OThis reaction proceeds in the forward direction.
- 3-oxobutanoyl-[ACP] + H+ + NADPH = (3R)-hydroxybutanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxodecanoyl-[ACP] + H+ + NADPH = (3R)-hydroxydecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxododecanoyl-[ACP] + H+ + NADPH = (3R)-hydroxydodecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxohexadecanoyl-[ACP] + H+ + NADPH = (3R)-hydroxyhexadecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxohexanoyl-[ACP] + H+ + NADPH = (3R)-hydroxyhexanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxooctadecanoyl-[ACP] + H+ + NADPH = (3R)-hydroxyoctadecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxooctanoyl-[ACP] + H+ + NADPH = (3R)-hydroxyoctanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- 3-oxotetradecanoyl-[ACP] + H+ + NADPH = (3R)-hydroxytetradecanoyl-[ACP] + NADP+This reaction proceeds in the forward direction.
- H+ + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- H+ + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- acetyl-[ACP] + H+ + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- butanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- decanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxododecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
- dodecanoyl-[ACP] + H+ + malonyl-[ACP] = 3-oxotetradecanoyl-[ACP] + CO2 + holo-[ACP]This reaction proceeds in the forward direction.
Pathway
Antibiotic biosynthesis.
Lipid metabolism.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 898 | Proton acceptor; for dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1044 | Proton donor; for dehydratase activity | ||||
Sequence: D | ||||||
Active site | 2803 | Proton acceptor; for dehydratase activity | ||||
Sequence: H | ||||||
Active site | 2964 | Proton donor; for dehydratase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity | |
Molecular Function | 3-oxoacyl-[acyl-carrier-protein] synthase activity | |
Molecular Function | [acyl-carrier-protein] S-acetyltransferase activity | |
Molecular Function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity | |
Molecular Function | fatty acid synthase activity | |
Molecular Function | fatty acyl-[ACP] hydrolase activity | |
Molecular Function | phosphopantetheine binding | |
Molecular Function | zinc ion binding | |
Biological Process | DIM/DIP cell wall layer assembly | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | macrolide biosynthetic process | |
Biological Process | toxin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Saccharothrix
Accessions
- Primary accessionA0A5Q0GYB2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-455 | Ketosynthase family 3 (KS3) | ||||
Sequence: GEPIAIVGTGCRLPGGVTGPADLWRLVSEGVDAVSLFPTDRGWDVDALYAPGSDRPGTSHTRHGGFLHDAAEFDPGLFGVSPREALAMDPQQRLVLETTWEALEHAAIDPLSLRGSRTGVFTGVMYADYAGRLHRAPAGFEGQLSLGSAPSVVSGRVSYTFGLEGPAVTVDTACSSSLVALHLAVQALRRGECSLALAGGVTVMSTPVTYLDFSRQGGLAPDGRCKAFAAAADGTGFSEGVGVLVLERLSDARRHGHPVLALVRGTAVNQDGASSRLTAPSGPAQQRVIRQALADARLAPADVDVVEAHGTGTTLGDPVEAHALLATYGQDRAEPLWLGTVKSNIGHTQAAAGVAGVVKMVLALRHGVLPRSLHVDRPSPRIDWSRGAVELLTEQRPWPGPVRRAGVSSFGASGTNAHVVLEQ | ||||||
Region | 866-981 | N-terminal hotdog fold | ||||
Sequence: RDADDVTAVEVAGDGLLLTRELSLSSHPWLADHVVLGSVLVPGTALLELAVLACDRAGRDRVAELTLHAPVVVPATGAVEVQVRLDGRGALTVHSRAGGEWVHHAGGSLSDGAAAP | ||||||
Domain | 866-1121 | PKS/mFAS DH | ||||
Sequence: RDADDVTAVEVAGDGLLLTRELSLSSHPWLADHVVLGSVLVPGTALLELAVLACDRAGRDRVAELTLHAPVVVPATGAVEVQVRLDGRGALTVHSRAGGEWVHHAGGSLSDGAAAPARLVDWPPTGAVALDVAGHYERLAGAGLRYGPAFRGLRAAWRRDDEVFAEVALPDAPLPALLDAALHAIGLGPWGEAGLAQLPFAWGDVTLHATGATAIRVRIAPAGPGAVAIDVADATGMPVATIGSLALRPAAVDPRH | ||||||
Region | 992-1121 | C-terminal hotdog fold | ||||
Sequence: AVALDVAGHYERLAGAGLRYGPAFRGLRAAWRRDDEVFAEVALPDAPLPALLDAALHAIGLGPWGEAGLAQLPFAWGDVTLHATGATAIRVRIAPAGPGAVAIDVADATGMPVATIGSLALRPAAVDPRH | ||||||
Domain | 1829-1904 | Carrier | ||||
Sequence: DALLDLVREHAATVLGFGSAAEVEPGRAFRDLGFDSLTSVELRNRLDAATGLRLPPTLVFDHPTPTALAALLHREL | ||||||
Domain | 1921-2325 | Ketosynthase family 3 (KS3) | ||||
Sequence: DEPIAVVAMSCRLPGGVDSPEDLWDLVAAGGDAIADFPADRGWATGDLGPRGGGFRYDAAEFDAGFFGISPREALAMDPQQRMLLEGAWEVFERAGIVPASLRGEPVGVYVGAIHNGYAETLGDAREEVEGHLVTGTMNSVASGRLAYTFGLEGPAITVDTACSSSLVAIHLASQALRQGECSLAVAGGVTVSATPDIFTEFGRQGALSADGRCKAFSADADGFGVADGLGLVLLERLSDARRNGHPVLAVVRGSAVNQDGASNGLTAPSGPAQQRVIRRALANAGLRPSEVDVVEAHGTGTRLGDQIEAQALAAVYGPVRVGTVKSNIGHAQAAAGVAGVLKVVQALRHGVLPRTLHVGTPLPEAGDLRLLDRAERWRTDGRPRRAGVSSFGISGTNAHLVLEQ | ||||||
Region | 2771-2893 | N-terminal hotdog fold | ||||
Sequence: HPLLGAAVPLAGSAGLVCTGLLSPGTQPWLADHVVSGAVLFPGTGFVELVGHVGGQVGCGSVADLTLTAPLVLPARDGVRVQVAVGEPDGSGTRPVTVHARRSDDDPWTRHATGRVRPGRPPA | ||||||
Domain | 2771-3037 | PKS/mFAS DH | ||||
Sequence: HPLLGAAVPLAGSAGLVCTGLLSPGTQPWLADHVVSGAVLFPGTGFVELVGHVGGQVGCGSVADLTLTAPLVLPARDGVRVQVAVGEPDGSGTRPVTVHARRSDDDPWTRHATGRVRPGRPPAFDLVQWPPAGAEALDPAGHYELLAGAGLAYGPVFRGLTAAWRRGDELFAEVRLPASVRDADRYGLHPAALDAALHVLGHAGGGPAWPFEWSGVSLHATGASVLRVRLVPAGADAFAVEVADGTGSPVMSVESLAFRPVAGAGPD | ||||||
Region | 2855-2893 | Disordered | ||||
Sequence: VGEPDGSGTRPVTVHARRSDDDPWTRHATGRVRPGRPPA | ||||||
Compositional bias | 2868-2883 | Basic and acidic residues | ||||
Sequence: VHARRSDDDPWTRHAT | ||||||
Region | 2904-3037 | C-terminal hotdog fold | ||||
Sequence: AEALDPAGHYELLAGAGLAYGPVFRGLTAAWRRGDELFAEVRLPASVRDADRYGLHPAALDAALHVLGHAGGGPAWPFEWSGVSLHATGASVLRVRLVPAGADAFAVEVADGTGSPVMSVESLAFRPVAGAGPD | ||||||
Domain | 3733-3808 | Carrier | ||||
Sequence: RALVDLVRGHAAAVLGHADPAAVAPERAFVQVGFDSLTAMELRNGLNAATGLRLPTSAVFDHHTPTGLARRLLDEL |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length4,092
- Mass (Da)428,000
- Last updated2020-04-22 v1
- Checksum307453D8A0D0A3E5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 2868-2883 | Basic and acidic residues | ||||
Sequence: VHARRSDDDPWTRHAT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP034550 EMBL· GenBank· DDBJ | QFZ18939.1 EMBL· GenBank· DDBJ | Genomic DNA |