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D9QPU9 (D9QPU9_ACEAZ) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. 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:Acear_1013
OrganismAcetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288) [Complete proteome] [HAMAP] EMBL ADL12540.1
Taxonomic identifier574087 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Halanaerobiales › Halobacteroidaceae › Acetohalobium ›

Protein attributes

Sequence length330 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

Region257 – 2615ACP-binding By similarity HAMAP-Rule MF_01815

Sites

Active site1171 By similarity HAMAP-Rule MF_01815
Active site2561 By similarity HAMAP-Rule MF_01815
Active site2861 By similarity HAMAP-Rule MF_01815

Sequences

Sequence LengthMass (Da)Tools
D9QPU9 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 728EB725764CFF67

FASTA33034,949
        10         20         30         40         50         60 
MSKELRRAGI TGVGSYAPDK VLTNRDLEEM VDTSDEWIKS RTGIQERRIA KEETTTSDLA 

        70         80         90        100        110        120 
YKAAEAALDD ADLAPEELDL ILVATVTPDM VFPATGCLLQ DRLNATDAAA FDLEAGCSGF 

       130        140        150        160        170        180 
VYGISVATQF VRTGAYDNVL VIGAETLSKI INWEDRNTCV LFGDGAGAAV IQPVESRGIL 

       190        200        210        220        230        240 
STVLGSDGSG GDVLQIPAGG SKQPASLETV ENNLHCIQME GNAVFKFAVR AMGKGAVEAL 

       250        260        270        280        290        300 
NEAGLEKEDV DFLIPHQANI RIIDGAAKRL NLSDDEVFVN LDKYGNTSAA SIPIALDEAV 

       310        320        330 
EAGKIHSGDR VVIVGFGAGL TWAASVIEWS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002105 Genomic DNA. Translation: ADL12540.1.
RefSeqYP_003827605.1. NC_014378.1.

3D structure databases

ProteinModelPortalD9QPU9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL12540; ADL12540; Acear_1013.
GeneID9513055.
KEGGaar:Acear_1013.
PATRIC42136231. VBIAceAra30843_1040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000246676.
KOK00648.

Enzyme and pathway databases

BioCycAARA574087:GHPK-1079-MONOMER.
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 nameD9QPU9_ACEAZ
AccessionPrimary (citable) accession number: D9QPU9
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 19 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