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Q9RT23 (FABH1_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1
EC=2.3.1.180
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III protein 1
Beta-ketoacyl-ACP synthase III 1
Short name=KAS III 1
Gene names
Name:fabH1
Ordered Locus Names:DR_1946
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP-Rule MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP-Rule MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP-Rule MF_01815

Sequence similarities

Belongs to the FabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3413413-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 HAMAP-Rule MF_01815
PRO_0000110422

Regions

Region250 – 2545ACP-binding By similarity

Sites

Active site1131 By similarity
Active site2491 By similarity
Active site2791 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RT23 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D99AC3191346EE78

FASTA34136,031
        10         20         30         40         50         60 
MKSIGITAIG MYVPERVVHN HEFESRMGIE DGWIESRSGI RERRFSAPGE FASHIGAKAV 

        70         80         90        100        110        120 
QDMLARDPDA LKDVDLVIYA TCTPDAMFPS TAALVAGQVG LTGVGAYDLS TACSGFVYAL 

       130        140        150        160        170        180 
SMARGMILGG SAKNVLVLGG EVLSKALDQD DRDTAILFGD GCGCAVVGEV PAGYGFQDFV 

       190        200        210        220        230        240 
LGADSAGGPA LYISNLADQF PDGQIMRGVP TMNGREVFKF AVRVLGDSGT QALQKSGLSN 

       250        260        270        280        290        300 
ADVDWLIPHQ ANIRIIEAAT QRFGIPMEKT VINLDRYGNT SAGTVPLALY EAVNDGRIQG 

       310        320        330        340 
GQQLLMVVFG GGLSWAACTM KWWGGRPSLH AQVAQPAEVP A

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF11498.1.
PIRB75334.
RefSeqNP_295669.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RT23.
SMRQ9RT23. Positions 5-324.
ModBaseSearch...

Protein-protein interaction databases

STRING243230.DR_1946.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11498; AAF11498; DR_1946.
GeneID1798455.
KEGGdra:DR_1946.
PATRIC21631544. VBIDeiRad64572_2166.

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHOG000246674.
KOK00648.
OMASTACSGF.
ProtClustDBPRK12879.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2315-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
HAMAPMF_01815. FabH.
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH1_DEIRA
AccessionPrimary (citable) accession number: Q9RT23
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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