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Protein

Acyl transferase

Gene

luxD

Organism
Vibrio harveyi (Beneckea harveyi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acyl transferase is part of the fatty acid reductase system required for aldehyde biosynthesis; it produces fatty acids for the luminescent reaction.

Pathwayi: fatty acid reduction for biolumincescence

This protein is involved in the pathway fatty acid reduction for biolumincescence, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid reduction for biolumincescence and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei114Charge relay system1
Active sitei211Charge relay system1
Active sitei241Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Luminescence

Enzyme and pathway databases

UniPathwayiUPA00569.

Protein family/group databases

ESTHERivibha-1luxd. Thioesterase_acyl-transferase.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl transferase (EC:2.3.1.-)
Short name:
ACT
Alternative name(s):
C14ACP-TE
Myristoyl-ACP-specific thioesterase
Gene namesi
Name:luxD
OrganismiVibrio harveyi (Beneckea harveyi)
Taxonomic identifieri669 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002201951 – 305Acyl transferaseAdd BLAST305

Interactioni

Protein-protein interaction databases

STRINGi338187.VIBHAR_06243.

Structurei

Secondary structure

1305
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 14Combined sources7
Turni15 – 17Combined sources3
Beta strandi18 – 25Combined sources8
Beta strandi37 – 41Combined sources5
Helixi46 – 51Combined sources6
Helixi52 – 59Combined sources8
Turni60 – 62Combined sources3
Beta strandi65 – 68Combined sources4
Helixi86 – 102Combined sources17
Beta strandi108 – 113Combined sources6
Helixi116 – 123Combined sources8
Turni124 – 126Combined sources3
Beta strandi130 – 136Combined sources7
Helixi141 – 149Combined sources9
Helixi153 – 155Combined sources3
Helixi158 – 160Combined sources3
Beta strandi163 – 167Combined sources5
Beta strandi170 – 173Combined sources4
Helixi174 – 183Combined sources10
Helixi189 – 196Combined sources8
Beta strandi203 – 208Combined sources6
Helixi216 – 223Combined sources8
Beta strandi231 – 236Combined sources6
Helixi247 – 265Combined sources19
Helixi280 – 296Combined sources17
Helixi297 – 299Combined sources3
Beta strandi302 – 304Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1THTX-ray2.10A/B1-305[»]
ProteinModelPortaliP05521.
SMRiP05521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05521.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxD family.Curated

Phylogenomic databases

eggNOGiENOG4108XDE. Bacteria.
ENOG4111MFF. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_00774. LuxD. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003157. LuxD.
[Graphical view]
PfamiPF02273. Acyl_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF009416. LuxD. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

P05521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNQCKTIAH VLRVNNGQEL HVWETPPKEN VPFKNNTILI ASGFARRMDH
60 70 80 90 100
FAGLAEYLSE NGFHVFRYDS LHHVGLSSGS IDEFTMTTGK NSLCTVYHWL
110 120 130 140 150
QTKGTQNIGL IAASLSARVA YEVISDLELS FLITAVGVVN LRDTLEKALG
160 170 180 190 200
FDYLSLPIDE LPNDLDFEGH KLGSEVFVRD CFEHHWDTLD STLDKVANTS
210 220 230 240 250
VPLIAFTANN DDWVKQEEVY DMLAHIRTGH CKLYSLLGSS HDLGENLVVL
260 270 280 290 300
RNFYQSVTKA AIAMDGGSLE IDVDFIEPDF EQLTIATVNE RRLKAEIESR

TPEMA
Length:305
Mass (Da):34,207
Last modified:August 1, 1990 - v2
Checksum:i316B694A0E864AD9
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti75G → E in mutant M17. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03950 Genomic DNA. Translation: AAA27535.1.
M10961 Genomic DNA. Translation: AAA88684.1.
PIRiA28947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03950 Genomic DNA. Translation: AAA27535.1.
M10961 Genomic DNA. Translation: AAA88684.1.
PIRiA28947.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1THTX-ray2.10A/B1-305[»]
ProteinModelPortaliP05521.
SMRiP05521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338187.VIBHAR_06243.

Protein family/group databases

ESTHERivibha-1luxd. Thioesterase_acyl-transferase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108XDE. Bacteria.
ENOG4111MFF. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00569.

Miscellaneous databases

EvolutionaryTraceiP05521.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_00774. LuxD. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR003157. LuxD.
[Graphical view]
PfamiPF02273. Acyl_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF009416. LuxD. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLUXD_VIBHA
AccessioniPrimary (citable) accession number: P05521
Secondary accession number(s): P11002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.