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A1KRL1 (FABZ_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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:NMC0170
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length149 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 – 1491493-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ HAMAP-Rule MF_00406
PRO_0000301905

Sites

Active site531 By similarity

Secondary structure

......................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A1KRL1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: DE6BCB39FB8DACBE

FASTA14916,613
        10         20         30         40         50         60 
MDVQLPIEAK DIQKLIPHRY PFLQLDRITA FEPMKTLTAI KNVSINEPQF QGHFPDLPVM 

        70         80         90        100        110        120 
PGVLIIEAMA QACGTLAILS EGGRKENEFF FFAGIDEARF KRQVIPGDQL VFEVELLTSR 

       130        140 
RGIGKFNAVA KVDGQVAVEA IIMCAKRVV 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM09489.1.
RefSeqYP_974299.1. NC_008767.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I83X-ray2.60A/B/C/D/E/F1-149[»]
ProteinModelPortalA1KRL1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC0170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09489; CAM09489; NMC0170.
GeneID4675013.
KEGGnmc:NMC0170.
PATRIC20349847. VBINeiMen17609_0188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0764.
HOGENOMHOG000277829.
KOK02372.
OMATIEYHMR.
OrthoDBEOG6JTCGM.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-172-MONOMER.

Family and domain databases

Gene3D3.10.129.10. 1 hit.
HAMAPMF_00406. FabZ.
InterProIPR013114. FabA_FabZ.
IPR010084. FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMSSF54637. SSF54637. 1 hit.
TIGRFAMsTIGR01750. fabZ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFABZ_NEIMF
AccessionPrimary (citable) accession number: A1KRL1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 49 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