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Protein

3-oxoacyl-[acyl-carrier-protein] synthase 1

Gene

kasA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.By similarity

Catalytic activityi

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei1711 Publication1
Binding sitei311Substrate1 Publication1
Binding sitei345Substrate1 Publication1

GO - Molecular functioni

  • 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: MTBBASE

GO - Biological processi

  • fatty acid elongation Source: MTBBASE
  • fatty acid elongation, saturated fatty acid Source: MTBBASE
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-6461-MONOMER.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000962.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl-ACP synthase 1
Short name:
KAS 1
Gene namesi
Name:kasA
Ordered Locus Names:Rv2245
ORF Names:MTCY427.26
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2245.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi171C → Q: Mimics structural changes caused by acyl-enzyme formation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4544.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803331 – 4163-oxoacyl-[acyl-carrier-protein] synthase 1Add BLAST416

Proteomic databases

PaxDbiP9WQD9.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2245.

Chemistry databases

BindingDBiP9WQD9.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 9Combined sources4
Beta strandi14 – 25Combined sources12
Helixi29 – 37Combined sources9
Helixi49 – 54Combined sources6
Beta strandi60 – 62Combined sources3
Helixi68 – 71Combined sources4
Helixi74 – 79Combined sources6
Helixi82 – 97Combined sources16
Helixi105 – 107Combined sources3
Beta strandi108 – 113Combined sources6
Helixi121 – 132Combined sources12
Helixi134 – 136Combined sources3
Helixi141 – 145Combined sources5
Helixi149 – 158Combined sources10
Helixi170 – 172Combined sources3
Helixi173 – 186Combined sources14
Beta strandi191 – 197Combined sources7
Helixi204 – 211Combined sources8
Turni212 – 214Combined sources3
Helixi223 – 225Combined sources3
Beta strandi242 – 250Combined sources9
Helixi251 – 256Combined sources6
Beta strandi262 – 272Combined sources11
Beta strandi277 – 279Combined sources3
Helixi285 – 298Combined sources14
Helixi302 – 304Combined sources3
Beta strandi307 – 309Combined sources3
Helixi316 – 328Combined sources13
Beta strandi334 – 337Combined sources4
Helixi340 – 343Combined sources4
Helixi347 – 349Combined sources3
Helixi350 – 364Combined sources15
Turni378 – 380Combined sources3
Beta strandi396 – 403Combined sources8
Turni404 – 406Combined sources3
Beta strandi407 – 414Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WGDX-ray2.01A1-416[»]
2WGEX-ray1.80A1-416[»]
2WGFX-ray2.15A/B/C/D/E/F/G/H1-416[»]
2WGGX-ray2.00A/B/C/D/E/F/G/H1-416[»]
5LD8X-ray2.13A/B2-416[»]
ProteinModelPortaliP9WQD9.
SMRiP9WQD9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
KOiK11609.
OMAiFEVEQYL.
PhylomeDBiP9WQD9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.

Sequencei

Sequence statusi: Complete.

P9WQD9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPSTANGG FPSVVVTAVT ATTSISPDIE STWKGLLAGE SGIHALEDEF
60 70 80 90 100
VTKWDLAVKI GGHLKDPVDS HMGRLDMRRM SYVQRMGKLL GGQLWESAGS
110 120 130 140 150
PEVDPDRFAV VVGTGLGGAE RIVESYDLMN AGGPRKVSPL AVQMIMPNGA
160 170 180 190 200
AAVIGLQLGA RAGVMTPVSA CSSGSEAIAH AWRQIVMGDA DVAVCGGVEG
210 220 230 240 250
PIEALPIAAF SMMRAMSTRN DEPERASRPF DKDRDGFVFG EAGALMLIET
260 270 280 290 300
EEHAKARGAK PLARLLGAGI TSDAFHMVAP AADGVRAGRA MTRSLELAGL
310 320 330 340 350
SPADIDHVNA HGTATPIGDA AEANAIRVAG CDQAAVYAPK SALGHSIGAV
360 370 380 390 400
GALESVLTVL TLRDGVIPPT LNYETPDPEI DLDVVAGEPR YGDYRYAVNN
410
SFGFGGHNVA LAFGRY
Length:416
Mass (Da):43,316
Last modified:April 16, 2014 - v1
Checksum:iD2187BE2F0B56C7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45025.1.
PIRiA70779.
RefSeqiNP_216761.1. NC_000962.3.
WP_003411571.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45025; CCP45025; Rv2245.
GeneIDi887269.
KEGGimtu:Rv2245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45025.1.
PIRiA70779.
RefSeqiNP_216761.1. NC_000962.3.
WP_003411571.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WGDX-ray2.01A1-416[»]
2WGEX-ray1.80A1-416[»]
2WGFX-ray2.15A/B/C/D/E/F/G/H1-416[»]
2WGGX-ray2.00A/B/C/D/E/F/G/H1-416[»]
5LD8X-ray2.13A/B2-416[»]
ProteinModelPortaliP9WQD9.
SMRiP9WQD9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2245.

Chemistry databases

BindingDBiP9WQD9.
ChEMBLiCHEMBL4544.
SwissLipidsiSLP:000000962.

Proteomic databases

PaxDbiP9WQD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45025; CCP45025; Rv2245.
GeneIDi887269.
KEGGimtu:Rv2245.

Organism-specific databases

TubercuListiRv2245.

Phylogenomic databases

eggNOGiENOG4105C0Q. Bacteria.
COG0304. LUCA.
KOiK11609.
OMAiFEVEQYL.
PhylomeDBiP9WQD9.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMTBH37RV:G185E-6461-MONOMER.

Miscellaneous databases

PROiP9WQD9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SMARTiSM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiFAB1_MYCTU
AccessioniPrimary (citable) accession number: P9WQD9
Secondary accession number(s): L0T991, P63454, Q10524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.