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A7THG7 (LKHA4_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 homolog
Short name=LTA-4 hydrolase
EC=3.3.2.6
Alternative name(s):
Leukotriene A(4) hydrolase
Gene names
ORF Names:Kpol_1039p41
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Vanderwaltozyma ›

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA4 to form LTB4 (in vitro) 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.

Pathway

Lipid metabolism; leukotriene B4 biosynthesis.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656Leukotriene A-4 hydrolase homolog
PRO_0000324941

Regions

Region173 – 1753Substrate binding By similarity
Region302 – 3076Substrate binding By similarity

Sites

Active site3321Proton acceptor By similarity
Active site4201Proton donor By similarity
Metal binding3311Zinc; catalytic By similarity
Metal binding3351Zinc; catalytic By similarity
Metal binding3541Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A7THG7 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 5768A5A9E11A4AFF

FASTA65674,538
        10         20         30         40         50         60 
MLSQFTRSLS CFVKPTPPKL NKLTRTMTVL PKILQDARPK VSPELDYSTY SNYQNFKINH 

        70         80         90        100        110        120 
TDLNLNISFD DSIVNGFVTF NLNKIDKSCN EIRLDTSFLT VDSVEIDDAK VDFQLKDRLE 

       130        140        150        160        170        180 
PLGSQLIINP PTATSLNNEF NLKLGFSTTK DCTALQWLNG EQTSSGKPYV FSQLEAIHAR 

       190        200        210        220        230        240 
ALFPCFDTPS VKSTFNAAIT STLPVVFSGI EQSVVDNGNG TKTYNFKQSV PIPAYLIGIA 

       250        260        270        280        290        300 
SGDLVSGEIG PRSKVYTEPF RLKDCEWEFS GDVEKFIQAA EKIIFPYEWG TYDILVNVNS 

       310        320        330        340        350        360 
YPYGGMESPN MTFATPTLIA YDKSNIDVIA HELAHSWSGN LVTNCSWNHF WLNEGWTVYL 

       370        380        390        400        410        420 
ERRIVAAIHG EATRHFSALI GWNDLANSIS AMKNPDRFST LIQNLNDGTD PDEAFSSVPY 

       430        440        450        460        470        480 
EKGFNLLFHL ETILGGPKEF DPFIKHYFTK FSKKSLDSYQ FFDTLFEFFA DKREILDAVD 

       490        500        510        520        530        540 
WETWLYKPGM PPKPKFITTL ADNVYSLAEK WATEIKNGNT TEDDLKQAFT AADIKDFNSN 

       550        560        570        580        590        600 
QIVLFLDTLV QNKEIQWNNH HTAAKTLLKI YEDSIVKSRN AEVVFRTYRF EITAQLKESY 

       610        620        630        640        650 
PQLAEWLATV GRMKFVRPGY RLLNSVDRPL ALATFEKLQN IYHPICKALV KQDLEA

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References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DS480391 Genomic DNA. Translation: EDO18291.1.
RefSeqXP_001646149.1. XM_001646099.1.

3D structure databases

ProteinModelPortalA7THG7.
ModBaseSearch...

Protein-protein interaction databases

STRING436907.A7THG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5546571.
KEGGvpo:Kpol_1039p41.

Phylogenomic databases

eggNOGCOG0308.
KOK01254.
OrthoDBEOG49KJZX.

Enzyme and pathway databases

UniPathwayUPA00878.

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]
PANTHERPTHR11533. PTHR11533. 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_VANPO
AccessionPrimary (citable) accession number: A7THG7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 2, 2007
Last modified: May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

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