Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q3SZH7 (LKHA4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leukotriene A-4 hydrolase
Short name=LTA-4 hydrolase
EC=3.3.2.6
Alternative name(s):
Leukotriene A(4) hydrolase
Gene names
Name:LTA4H
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity By similarity.

Catalytic activity

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by bestatin. Subject to suicide inhibition by leukotriene A4 By similarity.

Pathway

Lipid metabolism; leukotriene B4 biosynthesis.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 611610Leukotriene A-4 hydrolase
PRO_0000244880

Regions

Region135 – 1373Substrate binding By similarity
Region267 – 2726Substrate binding By similarity
Region564 – 5663Substrate binding By similarity

Sites

Active site2971Proton acceptor By similarity
Active site3841Proton donor By similarity
Metal binding2961Zinc; catalytic By similarity
Metal binding3001Zinc; catalytic By similarity
Metal binding3191Zinc; catalytic By similarity
Site3761Essential for epoxide hydrolase activity, but not for aminopeptidase activity By similarity
Site3791Covalently modified during suicide inhibition by leukotrienes By similarity

Amino acid modifications

Modified residue731N6-acetyllysine By similarity
Modified residue3371N6-acetyllysine By similarity
Modified residue4141N6-acetyllysine By similarity
Modified residue5731N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SZH7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E0FB709BE629ED7D

FASTA61169,306
        10         20         30         40         50         60 
MPEVVDTCSL ASPASVCQTK HLHLRCSIDF TRRVLSGTAA LTIQSQEDNL RSLILDTKDL 

        70         80         90        100        110        120 
TIEKVVINGQ EVKYTLGERQ SYKGSPIEIS LPIALCKNQE IVIEISFETS PKSSALQWLT 

       130        140        150        160        170        180 
PEQTSGKEHP YLFSQCQAIH CRAILPCQDT PSVKLTYSAE VSVPKELVAL MSAIRDGEAP 

       190        200        210        220        230        240 
DPEDPNRKIY RFSQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES 

       250        260        270        280        290        300 
MLKIAEDLGG PYIWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH 

       310        320        330        340        350        360 
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL QNSIKTFGET 

       370        380        390        400        410        420 
HPFTKLVVDL TNTDPDVAYS SVPYEKGFAL LFYLEQLLGG PEVFLGFLKA YVEKFSYKSI 

       430        440        450        460        470        480 
TTDNWKDFLY SHFKDKVDIL NQVDWNTWLY SPGLPPVKPN YDMTLTNACI SLSQRWITAK 

       490        500        510        520        530        540 
DDDLNSFSSA DLKDFSSHQV NEFLAQMLQN APLPLGHIKR MQEVYNFNAI NNSEIRFRWL 

       550        560        570        580        590        600 
RLCIQSKWEE AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAIRTYK EHKASMHPVT 

       610 
AMLVGKDLKV D

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC102852 mRNA. Translation: AAI02853.1.
IPIIPI00718490.
RefSeqNP_001029452.1. NM_001034280.1.
UniGeneBt.48395.

3D structure databases

ProteinModelPortalQ3SZH7.
SMRQ3SZH7. Positions 2-611.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SZH7.

Protein family/group databases

MEROPSM01.004.

Proteomic databases

PRIDEQ3SZH7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000021833; ENSBTAP00000021833; ENSBTAG00000016415.
GeneID507130.
KEGGbta:507130.

Organism-specific databases

CTD4048.

Phylogenomic databases

eggNOGmaNOG07497.
GeneTreeENSGT00530000063003.
HOVERGENHBG001274.
InParanoidQ3SZH7.
OrthoDBEOG40GCQC.
PhylomeDBQ3SZH7.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
KOK01254.
PANTHERPTHR11533. Peptidase_M1. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
SUPFAMSSF48371. ARM-type_fold. 1 hit.
TIGRFAMsTIGR02411. Leuko_A4_hydro. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLKHA4_BOVIN
AccessionPrimary (citable) accession number: Q3SZH7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents