Skip Header

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

B3QVT8 (B3QVT8_CHLT3) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 26. Feed History...

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

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
Ordered Locus Names:Ctha_0676
OrganismChloroherpeton thalassium (strain ATCC 35110 / GB-78) [Complete proteome] [HAMAP]
Taxonomic identifier517418 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chloroherpeton

Protein attributes

Sequence length328 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

Region255 – 2595ACP-binding By similarity HAMAP MF_01815

Sites

Active site1131 By similarity HAMAP MF_01815
Active site2541 By similarity HAMAP MF_01815
Active site2841 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B3QVT8 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: EDD9C4C35CBC650F

FASTA32835,679
        10         20         30         40         50         60 
MKAAITATAK YTPPDKLTNF DLEKILDTND EWIRTRTGIQ ERRILKDPDK ATAYMCAEVS 

        70         80         90        100        110        120 
KQILEKRGIS AEEIDLIIIG TVTPDTIFPA AGCLVQGMIG AKNAWAFDLS AACSGFLYSL 

       130        140        150        160        170        180 
VVGSQFIESG MHKKVLVLGA DKMSAITDFT DRNTAVLFGD GAGGVLLEPA KDGYGVLDAK 

       190        200        210        220        230        240 
LYADGANGKD HLYMLAGGSL RPPSHETVDK KMHAIRQDGR VVFKSAVTEM ANSAVEMMRR 

       250        260        270        280        290        300 
NNLSADDITY LIPHQANHRI IMATAERMNI SMDKVGINID RYGNTTAATI PLCLAELDES 

       310        320 
GKLKSGDNLI FVSFGAGYTW GGIYVKWQ

« Hide

References

[1]"Complete sequence of Chloroherpeton thalassium ATCC 35110."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35110 / GB-78.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001100 Genomic DNA. Translation: ACF13145.1.
RefSeqYP_001995592.1. NC_011026.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB3QVT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6421721.
GenomeReviewsGene locus Ctha_0676 in contig CP001100_GR.
KEGGcts:Ctha_0676.
PATRIC21429925. VBIChlTha99257_0790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAKEIGAIN.
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 nameB3QVT8_CHLT3
AccessionPrimary (citable) accession number: B3QVT8
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info