Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8XLH3 (FABH_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3

EC=2.3.1.180
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III
Beta-ketoacyl-ACP synthase III
Short name=KAS III
Gene names
Name:fabH
Ordered Locus Names:CPE1068
OrganismClostridium perfringens [Complete proteome] [HAMAP]
Taxonomic identifier1502 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length324 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 MF_01815

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity. HAMAP MF_01815

Subcellular location

Cytoplasm Probable HAMAP MF_01815.

Domain

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

Sequence similarities

Belongs to the FabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3243243-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_0000110419

Regions

Region252 – 2565ACP-binding By similarity

Sites

Active site1121 By similarity
Active site2511 By similarity
Active site2811 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XLH3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 512995025494E7EA

FASTA32435,342
        10         20         30         40         50         60 
MKNAKMIGFG LYTPKNLVEN ERLQEFLETS DEWIRTRTGI ERRYISLDEN TSDLAVEASK 

        70         80         90        100        110        120 
KALSQARLSA EEIDLIIVAT VTPDNFTPST ACIVQDKLGA KNAWAFDINA ACTGFIYALK 

       130        140        150        160        170        180 
LGRSLIRSGE ANNALIIGAE TLSKALNWED RGSCVLFGDG AGATVLTSTE EDCGIKCVNV 

       190        200        210        220        230        240 
KSDGSKGDSL VIQGLPLNSP FKDGREVSEN YINMNGREIF KFATKVMEES IVEILEKENI 

       250        260        270        280        290        300 
KIEDIAAIIP HQANLRIIDY VVKRLGIPRE KFITNLQNYG NTSGASIPIA LCESIDEGNL 

       310        320 
KKGDNIIMVG FGGGLTWGAA LIKL 

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB80774.1.
RefSeqNP_561984.1. NC_003366.1.

3D structure databases

ProteinModelPortalQ8XLH3.
SMRQ8XLH3. Positions 3-323.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID989377.
GenomeReviewsGene locus CPE1068 in contig BA000016_GR.
KEGGcpe:CPE1068.
NMPDRfig|195102.1.peg.1131.
PATRIC19496082. VBICloPer59675_1138.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAKEIGAIN.
PhylomeDBQ8XLH3.
ProtClustDBPRK09352.

Enzyme and pathway databases

BioCycCPER195102:CPE1068-MONOMER.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
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 nameFABH_CLOPE
AccessionPrimary (citable) accession number: Q8XLH3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 60 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