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Q6MAF5 (Q6MAF5_PARUW) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 58. 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 CAF24444.1
Ordered Locus Names:pc1720
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Parachlamydiaceae › Candidatus Protochlamydia

Protein attributes

Sequence length332 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

Region257 – 2615ACP-binding By similarity HAMAP MF_01815

Sites

Active site1161 By similarity HAMAP MF_01815
Active site2561 By similarity HAMAP MF_01815
Active site2861 By similarity HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q6MAF5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 83EE13010245C393

FASTA33236,019
        10         20         30         40         50         60 
MANQIIARIT GVGSYLPERV LSNQDLEKMV ETSDDWIVSR TGIRERRLAD AKEFPSDMGT 

        70         80         90        100        110        120 
YAAQKALKTA NLKAEQIDMI LVATMSPDYI SPSTANLIQA NLGASKAAAM DIQAACTGFL 

       130        140        150        160        170        180 
YGLSVAKAYI ESNMYRHVLV IATEKMSAFI DYKDRTTCVL FGDGAAAAVV KGEGEGLKID 

       190        200        210        220        230        240 
SLCLGADGEL ANLVLIPGGG SRKPASIETV SEGLHYFKMS GNEVFKHAVR RMSAAARECL 

       250        260        270        280        290        300 
VRAELQESDV SWLIPHQANK RIIDAIAKNF NFPDEKVYQT VHKYGNTSAS SIAIALDELI 

       310        320        330 
KEHSFENGEH FLLTAFGGGL TWGASILTKT TR

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed: 15073324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX908798 Genomic DNA. Translation: CAF24444.1.
RefSeqYP_008719.1. NC_005861.1.

3D structure databases

ProteinModelPortalQ6MAF5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6MAF5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2780157.
GenomeReviewsGene locus pc1720 in contig BX908798_GR.
KEGGpcu:pc1720.
NMPDRfig|264201.1.peg.1720.
PATRIC31998868. VBICanPro72727_1763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
HOGENOMHBG649927.
OMAMAKISPE.
PhylomeDBQ6MAF5.
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 nameQ6MAF5_PARUW
AccessionPrimary (citable) accession number: Q6MAF5
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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