UniProtKB - P9WNG3 (FABH_MYCTU)
Protein
3-oxoacyl-[acyl-carrier-protein] synthase 3
Gene
fabH
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for long chain acyl-CoA such as myristoyl-CoA. Does not use acyl-CoA as primer. Its substrate specificity determines the biosynthesis of mycolic acid fatty acid chain, which is characteristic of mycobacterial cell wall.1 Publication
Miscellaneous
Inhibited by thiolactomycin. Not sensitive to cerulenin.
Was identified as a high-confidence drug target.1 Publication
Catalytic activityi
- EC:2.3.1.180UniRule annotation
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotationView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 122 | 1 Publication | 1 | |
Active sitei | 258 | 1 Publication | 1 | |
Active sitei | 289 | 1 Publication | 1 |
GO - Molecular functioni
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: MTBBASE
- beta-ketoacyl-acyl-carrier-protein synthase III activity Source: MTBBASE
- fatty-acyl-CoA binding Source: MTBBASE
GO - Biological processi
- fatty acid biosynthetic process Source: MTBBASE
- fatty acid elongation Source: MTBBASE
- lipid biosynthetic process Source: MTBBASE
- long-chain fatty-acyl-CoA metabolic process Source: MTBBASE
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Chemistry databases
SwissLipidsi | SLP:000000966 |
Names & Taxonomyi
Protein namesi | Recommended name: 3-oxoacyl-[acyl-carrier-protein] synthase 3UniRule annotation (EC:2.3.1.180UniRule annotation)Alternative name(s): 3-oxoacyl-[acyl-carrier-protein] synthase IIIUniRule annotation Beta-ketoacyl-ACP synthase IIIUniRule annotation Short name: KAS IIIUniRule annotation MtFabH |
Gene namesi | Name:fabH Ordered Locus Names:Rv0533c ORF Names:MTCY25D10.12c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0533c |
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL3640 |
DrugBanki | DB08712, 11-[(MERCAPTOCARBONYL)OXY]UNDECANOIC ACID DB08171, 11-MERCAPTOUNDECANOIC ACID DB07611, DECANE-1-THIOL DB07650, Decyl formate DB03264, Dodecyl-Coa DB03017, Lauric acid DB08684, O-Decyl Hydrogen Thiocarbonate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000110443 | 2 – 335 | 3-oxoacyl-[acyl-carrier-protein] synthase 3Add BLAST | 334 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylthreonineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | P9WNG3 |
PTM databases
iPTMneti | P9WNG3 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation1 PublicationProtein-protein interaction databases
STRINGi | 83332.Rv0533c |
Chemistry databases
BindingDBi | P9WNG3 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P9WNG3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 259 – 263 | ACP-bindingUniRule annotation | 5 |
Domaini
The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH.UniRule annotation
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0332, Bacteria |
OMAi | WGSEGDK |
PhylomeDBi | P9WNG3 |
Family and domain databases
CDDi | cd00830, KAS_III, 1 hit |
Gene3Di | 3.40.47.10, 2 hits |
HAMAPi | MF_01815, FabH, 1 hit |
InterProi | View protein in InterPro IPR013751, ACP_syn_III IPR013747, ACP_syn_III_C IPR004655, FabH_synth IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF08545, ACP_syn_III, 1 hit PF08541, ACP_syn_III_C, 1 hit |
SUPFAMi | SSF53901, SSF53901, 1 hit |
TIGRFAMsi | TIGR00747, fabH, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WNG3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTEIATTSGA RSVGLLSVGA YRPERVVTND EICQHIDSSD EWIYTRTGIK
60 70 80 90 100
TRRFAADDES AASMATEACR RALSNAGLSA ADIDGVIVTT NTHFLQTPPA
110 120 130 140 150
APMVAASLGA KGILGFDLSA GCAGFGYALG AAADMIRGGG AATMLVVGTE
160 170 180 190 200
KLSPTIDMYD RGNCFIFADG AAAVVVGETP FQGIGPTVAG SDGEQADAIR
210 220 230 240 250
QDIDWITFAQ NPSGPRPFVR LEGPAVFRWA AFKMGDVGRR AMDAAGVRPD
260 270 280 290 300
QIDVFVPHQA NSRINELLVK NLQLRPDAVV ANDIEHTGNT SAASIPLAMA
310 320 330
ELLTTGAAKP GDLALLIGYG AGLSYAAQVV RMPKG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43271.1 |
PIRi | H70545 |
RefSeqi | NP_215047.1, NC_000962.3 WP_003402861.1, NZ_NVQJ01000036.1 |
Genome annotation databases
EnsemblBacteriai | CCP43271; CCP43271; Rv0533c |
GeneIDi | 23493368 887381 |
KEGGi | mtu:Rv0533c mtv:RVBD_0533c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43271.1 |
PIRi | H70545 |
RefSeqi | NP_215047.1, NC_000962.3 WP_003402861.1, NZ_NVQJ01000036.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1HZP | X-ray | 2.10 | A/B | 1-335 | [»] | |
1M1M | X-ray | 2.70 | A/B | 1-335 | [»] | |
1U6E | X-ray | 1.85 | A/B | 1-335 | [»] | |
1U6S | X-ray | 2.30 | A/B | 1-335 | [»] | |
2AHB | X-ray | 2.00 | A/B | 1-335 | [»] | |
2AJ9 | X-ray | 2.50 | A/B | 1-335 | [»] | |
2QNX | X-ray | 2.70 | A/B | 1-335 | [»] | |
2QNY | X-ray | 2.15 | A/B | 1-335 | [»] | |
2QNZ | X-ray | 2.30 | A/B | 1-335 | [»] | |
2QO0 | X-ray | 1.85 | A/B | 1-335 | [»] | |
2QO1 | X-ray | 2.60 | A/B | 1-335 | [»] | |
2QX1 | X-ray | 2.60 | A/B | 1-335 | [»] | |
SMRi | P9WNG3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv0533c |
Chemistry databases
BindingDBi | P9WNG3 |
ChEMBLi | CHEMBL3640 |
DrugBanki | DB08712, 11-[(MERCAPTOCARBONYL)OXY]UNDECANOIC ACID DB08171, 11-MERCAPTOUNDECANOIC ACID DB07611, DECANE-1-THIOL DB07650, Decyl formate DB03264, Dodecyl-Coa DB03017, Lauric acid DB08684, O-Decyl Hydrogen Thiocarbonate |
SwissLipidsi | SLP:000000966 |
PTM databases
iPTMneti | P9WNG3 |
Proteomic databases
PaxDbi | P9WNG3 |
Genome annotation databases
EnsemblBacteriai | CCP43271; CCP43271; Rv0533c |
GeneIDi | 23493368 887381 |
KEGGi | mtu:Rv0533c mtv:RVBD_0533c |
Organism-specific databases
TubercuListi | Rv0533c |
Phylogenomic databases
eggNOGi | COG0332, Bacteria |
OMAi | WGSEGDK |
PhylomeDBi | P9WNG3 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Miscellaneous databases
PROi | PR:P9WNG3 |
Family and domain databases
CDDi | cd00830, KAS_III, 1 hit |
Gene3Di | 3.40.47.10, 2 hits |
HAMAPi | MF_01815, FabH, 1 hit |
InterProi | View protein in InterPro IPR013751, ACP_syn_III IPR013747, ACP_syn_III_C IPR004655, FabH_synth IPR016039, Thiolase-like |
Pfami | View protein in Pfam PF08545, ACP_syn_III, 1 hit PF08541, ACP_syn_III_C, 1 hit |
SUPFAMi | SSF53901, SSF53901, 1 hit |
TIGRFAMsi | TIGR00747, fabH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FABH_MYCTU | |
Accessioni | P9WNG3Primary (citable) accession number: P9WNG3 Secondary accession number(s): L0T424, O06399, P0A574 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 37 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families