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Protein

Bifunctional enzyme LpxC/FabZ

Gene

lpxC/fabZ

Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
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

Catalytic activityi

UDP-3-O-((3R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H2O = UDP-3-O-((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate.
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.

Cofactori

Pathwayi: lipid IV(A) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. Bifunctional enzyme LpxC/FabZ (lpxC/fabZ)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi79Zinc; via tele nitrogenBy similarity1
Metal bindingi264Zinc; via tele nitrogenBy similarity1
Metal bindingi268ZincBy similarity1
Active sitei291Proton donorBy similarity1
Active sitei370By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase, Multifunctional enzyme
Biological processLipid A biosynthesis, Lipid biosynthesis, Lipid metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciCTEP194439:G1FZE-1701-MONOMER
UniPathwayiUPA00359; UER00478

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional enzyme LpxC/FabZ
Including the following 2 domains:
UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC:3.5.1.108)
Short name:
UDP-3-O-acyl-GlcNAc deacetylase
Alternative name(s):
UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
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 namesi
Name:lpxC/fabZ
Ordered Locus Names:CT1662
OrganismiChlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
Proteomesi
  • UP000001007 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001919741 – 467Bifunctional enzyme LpxC/FabZAdd BLAST467

Proteomic databases

PRIDEiQ8KBX0

Interactioni

Protein-protein interaction databases

STRINGi194439.CT1662

Structurei

3D structure databases

ProteinModelPortaliQ8KBX0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 306UDP-3-O-acyl-N-acetylglucosamine deacetylaseAdd BLAST306
Regioni307 – 4673-hydroxyacyl-[acyl-carrier-protein] dehydrataseAdd BLAST161

Sequence similaritiesi

In the N-terminal section; belongs to the LpxC family.Curated
In the C-terminal section; belongs to the thioester dehydratase family.Curated

Phylogenomic databases

eggNOGiENOG4105C7C Bacteria
COG0764 LUCA
COG0774 LUCA
HOGENOMiHOG000029820
KOiK16363
OMAiMVDFGTK
OrthoDBiPOG091H0292

Family and domain databases

Gene3Di3.30.1700.10, 1 hit
3.30.230.20, 1 hit
HAMAPiMF_00406 FabZ, 1 hit
MF_00388 LpxC, 1 hit
InterProiView protein in InterPro
IPR013114 FabA_FabZ
IPR010084 FabZ
IPR029069 HotDog_dom_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR004463 UDP-acyl_GlcNac_deAcase
IPR011334 UDP-acyl_GlcNac_deAcase_C
IPR015870 UDP-acyl_N-AcGlcN_deAcase_N
PANTHERiPTHR33694 PTHR33694, 2 hits
PfamiView protein in Pfam
PF07977 FabA, 1 hit
PF03331 LpxC, 1 hit
SUPFAMiSSF54211 SSF54211, 3 hits
SSF54637 SSF54637, 1 hit
TIGRFAMsiTIGR01750 fabZ, 1 hit
TIGR00325 lpxC, 1 hit

Sequencei

Sequence statusi: Complete.

Q8KBX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIHQRTLQN EISLTGIGLH TGHECTITFK PAPVNTGYIF VRTDINDCPE
60 70 80 90 100
IPALIDHVVD VLRGTTIGIG DVKVHTTEHV LAALYGLQID NCRIELSGPE
110 120 130 140 150
PPVLDGSSNP FAEALLSAGI AEQDEPKNYL VIDETIEFHN PEKSVDIVAL
160 170 180 190 200
PLDGFRMTVM VDYKNPALGS QHSGLFDLDK EFLREFSPCR TFCFLSEVEA
210 220 230 240 250
MANQGIIKGA DIDNAIVIVD KQLDETEVQT LADKVGVDAS HLVLGQNGIL
260 270 280 290 300
NNRELRFSNE PARHKLLDLL GDLALLGMPV KAQILAXRPG HASNVEFVKQ
310 320 330 340 350
LKKYADRNKL ARQYQHEKKA GVIFDINAIQ NILPHRYPFL LIDKIVEFKL
360 370 380 390 400
DEKIVSIKNV TMNEPFFQGH FPGNPIMPGV LIIEAMAQTG GIMMLNGKEN
410 420 430 440 450
IKESVVFFMG IDKARFRKPV LPGDTLVIEA VMTNMRRTVC QFDAKAYVRG
460
ELVCEASLMA TVMEKKN
Length:467
Mass (Da):51,844
Last modified:October 1, 2002 - v1
Checksum:i355120C7D2B654E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006470 Genomic DNA Translation: AAM72887.1
RefSeqiNP_662545.1, NC_002932.3
WP_010933326.1, NC_002932.3

Genome annotation databases

EnsemblBacteriaiAAM72887; AAM72887; CT1662
GeneIDi1006145
KEGGicte:CT1662
PATRICifig|194439.7.peg.1500

Similar proteinsi

Entry informationi

Entry nameiLPXZ_CHLTE
AccessioniPrimary (citable) accession number: Q8KBX0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: October 1, 2002
Last modified: March 28, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health