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Reviewed, UniProtKB/Swiss-Prot Q899P3 (FABH_CLOTE)

Last modified November 3, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: CTC_00127
OrganismClostridium tetani [Complete proteome] [HAMAP]
Taxonomic identifier1513 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP MF_01815

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/acpP and fabH By similarity.

Sequence similarities

Belongs to the fabH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3343343-oxoacyl-[acyl-carrier-protein] synthase 3 HAMAP MF_01815
PRO_0000110420

Regions

Region261 – 2655ACP-binding By similarity

Sites

Active site1141 By similarity
Active site2601 By similarity
Active site2901 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q899P3-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0640A0664E3D5FDF

FASTA33436,699
        10         20         30         40         50         60 
MKNKEVRILS TGKYLPPISI SNHDLSKIID TNDNWIKTRT GIEKRRITKG ENTSDLGTKA 

        70         80         90        100        110        120 
ALDALRKGGI SPEELDLIIV ATITPDYFTP STACIIQRNI KAYNAFAFDI SAACSGFTYG 

       130        140        150        160        170        180 
ISIASQFIRN GVAKKVLVIG VETLSKLVDW KDRNTCILFG DGSGAAILTE SNEKGIMNVY 

       190        200        210        220        230        240 
LGSDGRGADL LKCKSSSLTV NSDELKELLN SKEEDLENKF IEMDGKEIFK FAVKVMIKGI 

       250        260        270        280        290        300 
EKVLKDSNLE LKDINYIIPH QANLRIIEHV AKKLGIDENK FYININHYGN TSAASIPIAL 

       310        320        330 
AEVDEKGLLK KGDNVILVGF GAGLTWAASL IKWI 

« Hide

References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed: 12552129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

Cross-references

Sequence databases

AE015927 Genomic DNA. Translation: AAO34779.1.
RefSeqNP_780842.1.

3D structure databases

HSSPHSSP built from PDB template 1HNK based on UniProtKB P24249.
ModBaseSearch...

Genome annotation databases

GeneID1059174.
GenomeReviewsGene locus CTC_00127 in contig AE015927_GR.
KEGGctc:CTC00127.
NMPDRfig|212717.1.peg.64.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ899P3.
OMAYIVPHQA.

Enzyme and pathway databases

BioCycCTET212717:CTC_00127-MON.
BRENDA2.3.1.180. 2082.

Family and domain databases

HAMAPMF_01815.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00747. fabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABH_CLOTE
AccessionPrimary (citable) accession number: Q899P3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents