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Q2SWY7 (FABZ_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ

EC=4.2.1.59
Alternative name(s):
(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase
Short name=(3R)-hydroxymyristoyl-ACP dehydrase
Beta-hydroxyacyl-ACP dehydratase
Gene names
Name:fabZ
Ordered Locus Names:BTH_I2038
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs By similarity. HAMAP-Rule MF_00406

Catalytic activity

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O. HAMAP-Rule MF_00406

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00406.

Sequence similarities

Belongs to the thioester dehydratase family. FabZ subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1601603-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ HAMAP-Rule MF_00406
PRO_0000242887

Sites

Active site591 By similarity

Secondary structure

................... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q2SWY7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5A03FC5D9F004913

FASTA16018,087
        10         20         30         40         50         60 
MRRTIMSTEK INFDIHKILT LLPHRYPILL VDRVLELEPH KSIKALKNVT VNEPFFTGHF 

        70         80         90        100        110        120 
PKRPVMPGVL IIEALAQAAA LLTFAEAEPK DPENTLYYFV GIDNARFKRV VEPGDQLILN 

       130        140        150        160 
VTFERYIRGI WKFKAVAEVD GKVAAEAELM CTVKTADAAP 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC39413.1.
RefSeqYP_442562.1. NC_007651.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H4GX-ray2.65A/B/C/D/E/F/G/H/I1-160[»]
ProteinModelPortalQ2SWY7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_I2038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC39413; ABC39413; BTH_I2038.
GeneID3848748.
KEGGbte:BTH_I2038.
PATRIC19307118. VBIBurTha36512_4848.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0764.
HOGENOMHOG000277829.
KOK02372.
OMAKERRGVA.
OrthoDBEOG6JTCGM.
ProtClustDBPRK00006.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-2039-MONOMER.

Family and domain databases

HAMAPMF_00406. FabZ.
InterProIPR013114. FabA_FabZ.
IPR010084. FabZ.
[Graphical view]
PfamPF07977. FabA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01750. fabZ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABZ_BURTA
AccessionPrimary (citable) accession number: Q2SWY7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references