Skip Header

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

B0TGV7 (B0TGV7_HELMI) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 30. 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 EMBL ABZ84718.1
Ordered Locus Names:Helmi_20930
ORF Names:HM1_2162 EMBL ABZ84718.1
OrganismHeliobacterium modesticaldum (strain ATCC 51547 / Ice1) [Complete proteome] [HAMAP]
Taxonomic identifier498761 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Heliobacteriaceae › Heliobacterium

Protein attributes

Sequence length331 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 site1141 By similarity HAMAP MF_01815
Active site2531 By similarity HAMAP MF_01815
Active site2831 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
B0TGV7 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 2436177BCF45E6B0

FASTA33135,400
        10         20         30         40         50         60 
MLKKVGIWGT GAYLPERIMT NKEFESMVDT SDEWIVTRTG IRERRVAAPE EAVSDLSAIA 

        70         80         90        100        110        120 
GARALEAAGL APEEVDLVIV GSCTFDTYLP ASACLAAWKM GARRAAAFDL ETACTSFIYG 

       130        140        150        160        170        180 
CAVGAQFIAT GMYRHVLVIG AEVLSKFLDY RDRNTCVLFG DGAGAALLGP VEEGGFKAFD 

       190        200        210        220        230        240 
LGADGSGGGL ITVPAGGSRM PASAATLEER QHYVKMNGKE VYKFAVRVIG DASQRVLDRA 

       250        260        270        280        290        300 
GWRQEEIDML IPHQANLRII DSAAKKLGLS MEKVALNLDR CGNMSAASIP VALDEVVRAG 

       310        320        330 
KVKRGDRLLM VGFGSGLTWG SMAVEWNPGQ R

« Hide

References

[1]"The genome of Heliobacterium modesticaldum, a phototrophic representative of the Firmicutes containing the simplest photosynthetic apparatus."
Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M., Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.
J. Bacteriol. 190:4687-4696(2008) [PubMed: 18441057] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000930 Genomic DNA. Translation: ABZ84718.1.
RefSeqYP_001680729.1. NC_010337.2.

3D structure databases

ProteinModelPortalB0TGV7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0TGV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5910487.
GenomeReviewsGene locus Helmi_20930 in contig CP000930_GR.
KEGGhmo:HM1_2162.
PATRIC22108393. VBIHelMod36755_1957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAMAKISPE.

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 nameB0TGV7_HELMI
AccessionPrimary (citable) accession number: B0TGV7
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 30 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