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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 17111 Publication
Binding sitei311 – 3111Substrate1 Publication
Binding sitei345 – 3451Substrate1 Publication

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

UniPathwayiUPA00094.

Chemistry

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi171 – 1711C → Q: Mimics structural changes caused by acyl-enzyme formation. 1 Publication

Chemistry

ChEMBLiCHEMBL4544.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4164163-oxoacyl-[acyl-carrier-protein] synthase 1PRO_0000180333Add
BLAST

Proteomic databases

PaxDbiP9WQD9.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv2245.

Chemistry

BindingDBiP9WQD9.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 94Combined sources
Beta strandi14 – 2512Combined sources
Helixi29 – 379Combined sources
Helixi49 – 546Combined sources
Beta strandi60 – 623Combined sources
Helixi68 – 714Combined sources
Helixi74 – 796Combined sources
Helixi82 – 9716Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 1136Combined sources
Helixi121 – 13212Combined sources
Helixi134 – 1363Combined sources
Helixi141 – 1455Combined sources
Helixi149 – 15810Combined sources
Helixi170 – 1723Combined sources
Helixi173 – 18614Combined sources
Beta strandi191 – 1977Combined sources
Helixi204 – 2118Combined sources
Turni212 – 2143Combined sources
Helixi223 – 2253Combined sources
Beta strandi242 – 2509Combined sources
Helixi251 – 2566Combined sources
Beta strandi262 – 27211Combined sources
Beta strandi277 – 2793Combined sources
Helixi285 – 29814Combined sources
Helixi302 – 3043Combined sources
Beta strandi307 – 3093Combined sources
Helixi316 – 32813Combined sources
Beta strandi334 – 3374Combined sources
Helixi340 – 3434Combined sources
Helixi347 – 3493Combined sources
Helixi350 – 36415Combined sources
Turni378 – 3803Combined sources
Beta strandi396 – 4038Combined sources
Turni404 – 4063Combined sources
Beta strandi407 – 4148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP9WQD9.
SMRiP9WQD9. Positions 2-416.
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
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[»]
ProteinModelPortaliP9WQD9.
SMRiP9WQD9. Positions 2-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2245.

Chemistry

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.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  3. "Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin."
    Luckner S.R., Machutta C.A., Tonge P.J., Kisker C.
    Structure 17:1004-1013(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT GLN-171 AND OF WILD-TYPE IN COMPLEX WITH SUBSTRATE ANALOG, MUTAGENESIS OF CYS-171, SUBUNIT.

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: May 11, 2016
This is version 18 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.