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Protein

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

Gene

fabZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.2 Publications

Catalytic activityi

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541By similarity

GO - Molecular functioni

  • 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  • 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • fatty acid biosynthetic process Source: EcoCyc
  • lipid A biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:FABZ-MONOMER.
ECOL316407:JW0175-MONOMER.
MetaCyc:FABZ-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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
17 kDa actomyosin component
Beta-hydroxyacyl-ACP dehydratase
Gene namesi
Name:fabZ
Synonyms:sefA, yaeA
Ordered Locus Names:b0180, JW0175
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11284. fabZ.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851L → P in sfhC21; suppresses an ftsH deletion mutant as well as an ftsH temperature-sensitive mutation. Probably stabilizes the enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1511513-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZPRO_0000091673Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

EPDiP0A6Q6.
PaxDbiP0A6Q6.
PRIDEiP0A6Q6.

Interactioni

Subunit structurei

Oligomer.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263243. 422 interactions.
DIPiDIP-31868N.
IntActiP0A6Q6. 33 interactions.
MINTiMINT-1218564.
STRINGi511145.b0180.

Structurei

3D structure databases

ProteinModelPortaliP0A6Q6.
SMRiP0A6Q6. Positions 8-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108YXN. Bacteria.
COG0764. LUCA.
HOGENOMiHOG000277829.
InParanoidiP0A6Q6.
KOiK02372.
OMAiEMMCARR.
OrthoDBiEOG6JTCGM.
PhylomeDBiP0A6Q6.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00406. FabZ.
InterProiIPR013114. FabA_FabZ.
IPR010084. FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01750. fabZ. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6Q6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNTHTLQI EEILELLPHR FPFLLVDRVL DFEEGRFLRA VKNVSVNEPF
60 70 80 90 100
FQGHFPGKPI FPGVLILEAM AQATGILAFK SVGKLEPGEL YYFAGIDEAR
110 120 130 140 150
FKRPVVPGDQ MIMEVTFEKT RRGLTRFKGV ALVDGKVVCE ATMMCARSRE

A
Length:151
Mass (Da):17,033
Last modified:May 10, 2005 - v1
Checksum:i91F514A7319C2FB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19334 Genomic DNA. Translation: AAC36917.1.
U00096 Genomic DNA. Translation: AAC73291.1.
AP009048 Genomic DNA. Translation: BAA77855.1.
U70214 Genomic DNA. Translation: AAB08609.1.
PIRiD64742.
RefSeqiNP_414722.1. NC_000913.3.
WP_000210739.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73291; AAC73291; b0180.
BAA77855; BAA77855; BAA77855.
GeneIDi944888.
KEGGiecj:JW0175.
eco:b0180.
PATRICi32115471. VBIEscCol129921_0187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19334 Genomic DNA. Translation: AAC36917.1.
U00096 Genomic DNA. Translation: AAC73291.1.
AP009048 Genomic DNA. Translation: BAA77855.1.
U70214 Genomic DNA. Translation: AAB08609.1.
PIRiD64742.
RefSeqiNP_414722.1. NC_000913.3.
WP_000210739.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0A6Q6.
SMRiP0A6Q6. Positions 8-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263243. 422 interactions.
DIPiDIP-31868N.
IntActiP0A6Q6. 33 interactions.
MINTiMINT-1218564.
STRINGi511145.b0180.

Proteomic databases

EPDiP0A6Q6.
PaxDbiP0A6Q6.
PRIDEiP0A6Q6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73291; AAC73291; b0180.
BAA77855; BAA77855; BAA77855.
GeneIDi944888.
KEGGiecj:JW0175.
eco:b0180.
PATRICi32115471. VBIEscCol129921_0187.

Organism-specific databases

EchoBASEiEB1261.
EcoGeneiEG11284. fabZ.

Phylogenomic databases

eggNOGiENOG4108YXN. Bacteria.
COG0764. LUCA.
HOGENOMiHOG000277829.
InParanoidiP0A6Q6.
KOiK02372.
OMAiEMMCARR.
OrthoDBiEOG6JTCGM.
PhylomeDBiP0A6Q6.

Enzyme and pathway databases

BioCyciEcoCyc:FABZ-MONOMER.
ECOL316407:JW0175-MONOMER.
MetaCyc:FABZ-MONOMER.

Miscellaneous databases

PROiP0A6Q6.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
HAMAPiMF_00406. FabZ.
InterProiIPR013114. FabA_FabZ.
IPR010084. FabZ.
IPR029069. HotDog_dom.
[Graphical view]
PfamiPF07977. FabA. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
TIGRFAMsiTIGR01750. fabZ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene."
    Coleman J., Raetz C.R.H.
    J. Bacteriol. 170:1268-1274(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Coleman J.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 140-141 AND 150-151.
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
    Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Purification and characterization of an 'actomyosin' complex from Escherichia coli W3110."
    Foster S.J.
    FEMS Microbiol. Lett. 110:295-298(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-18, SIMILARITY, POSSIBLE FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. Relation to fabA and suppression of mutations in lipid A biosynthesis."
    Mohan S., Kelly T.M., Eveland S.S., Raetz C.R.H., Anderson M.S.
    J. Biol. Chem. 269:32896-32903(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Roles of the FabA and FabZ beta-hydroxyacyl-acyl carrier protein dehydratases in Escherichia coli fatty acid biosynthesis."
    Heath R.J., Rock C.O.
    J. Biol. Chem. 271:27795-27801(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  10. "Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli."
    Ogura T., Inoue K., Tatsuta T., Suzaki T., Karata K., Young K., Su L.H., Fierke C.A., Jackman J.E., Raetz C.R., Coleman J., Tomoyasu T., Matsuzawa H.
    Mol. Microbiol. 31:833-844(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-85.
    Strain: K12 / W3110 and W2252.

Entry informationi

Entry nameiFABZ_ECOLI
AccessioniPrimary (citable) accession number: P0A6Q6
Secondary accession number(s): P21774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: April 13, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.