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Q6MLJ5 (Q6MLJ5_BDEBA) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 59. 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 CAE79862.1
Ordered Locus Names:Bd2014
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

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

Region259 – 2635ACP-binding By similarity HAMAP MF_01815

Sites

Active site1161 By similarity HAMAP MF_01815
Active site2581 By similarity HAMAP MF_01815
Active site2881 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q6MLJ5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 77229E3B5C07A777

FASTA33136,252
        10         20         30         40         50         60 
MAGMYRSRVS GIGSYLPEKI LSNKDLEKMV ETNDQWIVER TGIERRHIAS EDQATSDLCV 

        70         80         90        100        110        120 
IAAKRALEDA NLKVEDIDMI LVGTVTGDHQ MPSTACFVQA KLGAKNIMAV DLNAACSGFL 

       130        140        150        160        170        180 
YGVSIADQFI RTGMYKNILV IGAEVLSRYM NYKDRETCIL FGDGAGAWVM SRAAEGQTNV 

       190        200        210        220        230        240 
IESSHLRADG TLADLLILPA GGSKIPQSHE AIDKGLNFMT MKGRDIFKNA VRTMASCCQE 

       250        260        270        280        290        300 
ALEHNKVAPE QVDWIVPHQA NKRIIEAVAD QFKFPMERVI VYLQETGNTS AASIPLAFDW 

       310        320        330 
AVKNGKIKRG QTILLTAFGA GLTSGSILLR Y

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842651 Genomic DNA. Translation: CAE79862.1.
RefSeqNP_968869.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MLJ5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2734729.
GenomeReviewsGene locus Bd2014 in contig BX842601_GR.
KEGGbba:Bd2014.
NMPDRfig|264462.1.peg.1840.
PATRIC21078532. VBIBdeBac73187_1833.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649927.
OMAMAKISPE.
PhylomeDBQ6MLJ5.

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 nameQ6MLJ5_BDEBA
AccessionPrimary (citable) accession number: Q6MLJ5
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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