Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ

Gene

fabZ

Organism
Magnetospirillum gryphiswaldense MSR-1 v2
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.UniRule annotationSAAS annotation

Catalytic activityi

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei61UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyaseUniRule annotationSAAS annotationImported
Biological processLipid A biosynthesisUniRule annotationSAAS annotation, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMGRY1430440:MGMSRV2_RS05890-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZUniRule annotation (EC:4.2.1.59UniRule annotation)
Alternative name(s):
(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydrataseUniRule annotation
Short name:
(3R)-hydroxymyristoyl-ACP dehydraseUniRule annotation
Beta-hydroxyacyl-ACP dehydrataseUniRule annotation
Gene namesi
Name:fabZUniRule annotationImported
ORF Names:MGMSRv2__1196Imported
OrganismiMagnetospirillum gryphiswaldense MSR-1 v2Imported
Taxonomic identifieri1430440 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum
Proteomesi
  • UP000018922 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliV6F2A4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 148FabAInterPro annotationAdd BLAST125

Sequence similaritiesi

Belongs to the thioester dehydratase family. FabZ subfamily.UniRule annotationSAAS annotation

Phylogenomic databases

KOiK02372

Family and domain databases

HAMAPiMF_00406 FabZ, 1 hit
InterProiView protein in InterPro
IPR013114 FabA_FabZ
IPR010084 FabZ
IPR029069 HotDog_dom_sf
PfamiView protein in Pfam
PF07977 FabA, 1 hit
SUPFAMiSSF54637 SSF54637, 1 hit
TIGRFAMsiTIGR01750 fabZ, 1 hit

Sequencei

Sequence statusi: Complete.

V6F2A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSMVNATET AGKEVDINRI MEMIPHRYPF LMVDKVVGIV SNVSAIGIKN
60 70 80 90 100
VTINEPFFQG HFPERPVMPG VLIIEAMAQT AAVLVVDTLG PSAEGKLVYF
110 120 130 140 150
MSVDSARFRK PVGPGDQLAI HVFKERSRGN VWKFRAEAKV GDTLMAEATY

AAMIMDS
Length:157
Mass (Da):17,245
Last modified:February 19, 2014 - v1
Checksum:i61BB058EF180E971
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HG794546 Genomic DNA Translation: CDK98411.1
RefSeqiWP_024079440.1, NC_023065.1

Genome annotation databases

EnsemblBacteriaiCDK98411; CDK98411; MGMSRv2__1196
KEGGimgy:MGMSRv2__1196

Similar proteinsi

Entry informationi

Entry nameiV6F2A4_9PROT
AccessioniPrimary (citable) accession number: V6F2A4
Entry historyiIntegrated into UniProtKB/TrEMBL: February 19, 2014
Last sequence update: February 19, 2014
Last modified: June 20, 2018
This is version 28 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health