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Protein

(R)-specific enoyl-CoA hydratase

Gene

phaJ

Organism
Aeromonas caviae (Aeromonas punctata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.2 Publications

Catalytic activityi

(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=29 µM for crotonyl-CoA1 Publication
  2. KM=36 µM for 2-pentenoyl-CoA1 Publication
  3. KM=34 µM for 2-hexenoyl-CoA1 Publication
  4. KM=50 µM for 2-octenoyl-CoA1 Publication
  1. Vmax=6200 µmol/min/mg enzyme with crotonyl-CoA as substrate1 Publication
  2. Vmax=2800 µmol/min/mg enzyme with 2-pentenoyl-CoA as substrate1 Publication
  3. Vmax=1800 µmol/min/mg enzyme with 2-hexenoyl-CoA as substrate1 Publication
  4. Vmax=2.5 µmol/min/mg enzyme with 2-octenoyl-CoA as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei55(3R)-3-hydroxyacyl-CoA; via amide nitrogenBy similarity1
Binding sitei84(3R)-3-hydroxyacyl-CoA; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
(R)-specific enoyl-CoA hydratase (EC:4.2.1.1191 Publication)
Gene namesi
Name:phaJ
OrganismiAeromonas caviae (Aeromonas punctata)
Taxonomic identifieri648 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi32D → A: Almost no activity. 1 Publication1
Mutagenesisi37H → A or N: Almost no activity. 1 Publication1
Mutagenesisi63S → A: 100-fold lower Vmax. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004136822 – 134(R)-specific enoyl-CoA hydrataseAdd BLAST133

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1134
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 17Combined sources7
Helixi20 – 30Combined sources11
Helixi35 – 38Combined sources4
Helixi40 – 43Combined sources4
Helixi55 – 68Combined sources14
Beta strandi76 – 84Combined sources9
Beta strandi93 – 103Combined sources11
Beta strandi105 – 117Combined sources13
Beta strandi123 – 132Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IQ6X-ray1.50A/B1-134[»]
ProteinModelPortaliO32472.
SMRiO32472.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO32472.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 119MaoC-likeAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 37(3R)-3-hydroxyacyl-CoA bindingBy similarity6

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Phylogenomic databases

KOiK19659.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR003965. Fatty_acid_synthase.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR01483. FASYNTHASE.
SUPFAMiSSF54637. SSF54637. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O32472-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAQSLEVGQ KARLSKRFGA AEVAAFAALS EDFNPLHLDP AFAATTAFER
60 70 80 90 100
PIVHGMLLAS LFSGLLGQQL PGKGSIYLGQ SLSFKLPVFV GDEVTAEVEV
110 120 130
TALREDKPIA TLTTRIFTQG GALAVTGEAV VKLP
Length:134
Mass (Da):14,086
Last modified:January 1, 1998 - v1
Checksum:iECB87170A10A2C9F
GO

Mass spectrometryi

Molecular mass is 13963 Da from positions 2 - 134. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88825 Genomic DNA. Translation: BAA21816.1.

Genome annotation databases

KEGGiag:BAA21816.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88825 Genomic DNA. Translation: BAA21816.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IQ6X-ray1.50A/B1-134[»]
ProteinModelPortaliO32472.
SMRiO32472.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAA21816.

Phylogenomic databases

KOiK19659.

Miscellaneous databases

EvolutionaryTraceiO32472.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR003965. Fatty_acid_synthase.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PRINTSiPR01483. FASYNTHASE.
SUPFAMiSSF54637. SSF54637. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHAJ_AERCA
AccessioniPrimary (citable) accession number: O32472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 55 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.