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D9TN96 (D9TN96_THETC) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 21. 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-Rule MF_01815
EC=2.3.1.180 HAMAP-Rule MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III HAMAP-Rule MF_01815
Beta-ketoacyl-ACP synthase III HAMAP-Rule MF_01815
Gene names
Name:fabH HAMAP-Rule MF_01815
Ordered Locus Names:Tthe_1496 EMBL ADL69006.1
OrganismThermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814) (Clostridium thermosaccharolyticum) [Complete proteome] [HAMAP] EMBL ADL69006.1
Taxonomic identifier580327 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Thermoanaerobacterium ›

Protein attributes

Sequence length333 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 SAAS SAAS004655

Pathway

Lipid metabolism; fatty acid biosynthesis. HAMAP-Rule MF_01815 SAAS SAAS004655

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01815 SAAS SAAS004655

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01815 SAAS SAAS004655.

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. HAMAP-Rule MF_01815

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region259 – 2635ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1181 By similarity HAMAP-Rule MF_01815
Active site2581 By similarity HAMAP-Rule MF_01815
Active site2881 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
D9TN96 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: AA072AFE3DB043BD

FASTA33335,933
        10         20         30         40         50         60 
MPQNNTFKAG ILGTGSFLPE NKLTNKDLER MVDTSDEWIV SRTGIKERRI APPSMTTSYM 

        70         80         90        100        110        120 
ATEAAKKAIE DAKITAEDID LIIVATVVPD MNFPSTACLV QANIGAINAA AFDIEVGCSG 

       130        140        150        160        170        180 
FIYGLSIAKQ FIENGTYKYV LVIAADILSK ITNWEDRNTC VLFGDGAGAA VVGQVENGYG 

       190        200        210        220        230        240 
ILDNFIGADG KGGMHLYMPA GGSRMPACEE SVKNKLHTIH MNGQEVFKFA VNVMNTATIE 

       250        260        270        280        290        300 
VLNRCGLKPE DVDIFIPHQA NIRIIDAAMK KLKLSKEKVF INLDKYGNMS AASVAVALDE 

       310        320        330 
ALKAGKIKNG DIILMVAFGA GLTWGSTVIK WLE

« Hide

References

[1]"Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM 571."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Hemme C.L., Woyke T.
Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7956 / DSM 571 / NCIB 9385 / NCA 3814.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002171 Genomic DNA. Translation: ADL69006.1.
RefSeqYP_003852090.1. NC_014410.1.

3D structure databases

ProteinModelPortalD9TN96.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL69006; ADL69006; Tthe_1496.
GeneID9707052.
KEGGttm:Tthe_1496.
PATRIC42452339. VBITheThe89703_1516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246674.
KOK00648.

Enzyme and pathway databases

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 nameD9TN96_THETC
AccessionPrimary (citable) accession number: D9TN96
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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