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B0BBM0 (B0BBM0_CHLTB) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP MF_01815
Beta-ketoacyl-ACP synthase III HAMAP MF_01815
Gene names
Name:fabH HAMAP MF_01815 EMBL CAP06885.1
Ordered Locus Names:CTLon_0487
OrganismChlamydia trachomatis serovar L2b (strain UCH-1/proctitis) [Complete proteome] [HAMAP] EMBL CAP06885.1
Taxonomic identifier471473 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length327 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 SAAS SAAS013747

Subunit structure

Homodimer By similarity. HAMAP MF_01815 SAAS SAAS013747

Subcellular location

Cytoplasm By similarity HAMAP MF_01815 SAAS SAAS013747.

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. HAMAP MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region254 – 2585ACP-binding By similarity HAMAP MF_01815

Sites

Active site1121 By similarity HAMAP MF_01815
Active site2531 By similarity HAMAP MF_01815
Active site2831 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B0BBM0 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 6D92252184B44A38

FASTA32735,327
        10         20         30         40         50         60 
MRASIWGTGS YLPKKILTNA DLEKIVETSD EWISTRTGIK ERRIASAEEF SSFMGAKAAE 

        70         80         90        100        110        120 
KAIEAAKISK SQVDCIVFST AAPDYIFPSS AALAQAYLGI KEIPAFDCLA ACTGFLYGLS 

       130        140        150        160        170        180 
IAKAYVESGM YQCVLVIAAD KLSSFVNYQD RNTCVLFGDG GSACIVGHSR PGALEISKVN 

       190        200        210        220        230        240 
LGADGKQGDL LRLPAGGSRC PASQDTVQNH QHFITMEGKE VFKHAVRRME FAAKTCITEA 

       250        260        270        280        290        300 
GLQEKDIDWL VPHQANERII DAIAKRFAVK DSRVFKTLAK YGNTAASSVG IALDELLRTH 

       310        320 
DIHVAERLLL VAFGGGLSWG AVILQQV

« Hide

References

[1]"Chlamydia trachomatis: genome sequence analysis of lymphogranuloma venereum isolates."
Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D., Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.
Genome Res. 18:161-171(2008) [PubMed: 18032721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM884177 Genomic DNA. Translation: CAP06885.1.
RefSeqYP_001653580.1. NC_010280.2.

3D structure databases

ProteinModelPortalB0BBM0.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0BBM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5859436.
GenomeReviewsGene locus CTLon_0487 in contig AM884177_GR.
KEGGctl:CTLon_0487.
PATRIC20382595. VBIChlTra68089_0529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMADAYIRGG.
ProtClustDBPRK09352.

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 nameB0BBM0_CHLTB
AccessionPrimary (citable) accession number: B0BBM0
Entry history
Integrated into UniProtKB/TrEMBL: February 26, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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