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Q0CFY9 (LKHA4_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:ATEG_06861
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length617 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 caution

The sequence EAU32245.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAU32245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 617617Leukotriene A-4 hydrolase homolog
PRO_0000324922

Regions

Region139 – 1413Substrate binding By similarity
Region271 – 2766Substrate binding By similarity

Sites

Active site3011Proton acceptor By similarity
Active site3881Proton donor By similarity
Metal binding3001Zinc; catalytic By similarity
Metal binding3041Zinc; catalytic By similarity
Metal binding3231Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CFY9 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: F0BC113CF9551639

FASTA61769,701
        10         20         30         40         50         60 
MATTINPPRD PNTLSNYNNW LSTHITANFD ILFDQKKLVG NVIHKLKSIT NAESTDIVLD 

        70         80         90        100        110        120 
TSHVDVTDVK VDGKPSVWEL LPPVKPYGTA LKIKLDQGVK MDEIVHVDIS VKTTEKCTAL 

       130        140        150        160        170        180 
QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKST IDFNITSPLP VIASGLLVRD 

       190        200        210        220        230        240 
ASGAPQTGGK NLYQFHQKVP IPSYLFALAS GDISEAAIGP RSVVATSPDK LRECQWELEA 

       250        260        270        280        290        300 
DTENFINAIE KIVYPYVWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENVDVIAH 

       310        320        330        340        350        360 
ELAHSWSGNL VTNASWEHFW LNEGWTVYLE RRILAAVHGE AYRHFSAIIG WKALSDSVDH 

       370        380        390        400        410        420 
FGHDHEFTRL ITDLKGKDPD DAFSSIPYEK GFNFLFHLEN LVGKQKFDQF IPHYFTKFKG 

       430        440        450        460        470        480 
KSLDSYEFKA TILDFFKSDA EASKLLNELD WDTWFYAPGL PPKPKFDTSL VDVVYDLAKK 

       490        500        510        520        530        540 
WQSIPESSFK PQPSDIKDLT GNQIVVFLEQ VLLFERPLAP ELSKLMGEVY GLAKSANIEV 

       550        560        570        580        590        600 
ANLYFRVGLN AGDESVFEPT ADLLGKIGRM KFVRPLYRNL QKVNRPLAIE TFEKNKDFYH 

       610 
PICRAMVEKD LFGKKDA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476603 Genomic DNA. Translation: EAU32245.1. Sequence problems.
RefSeqXP_001209547.1. XM_001209547.1.

3D structure databases

ProteinModelPortalQ0CFY9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4319230.

Phylogenomic databases

GeneTreeEFGT00050000003006.
OrthoDBEOG49KJZX.

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. 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_ASPTN
AccessionPrimary (citable) accession number: Q0CFY9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 16, 2011
This is version 44 of the entry and version 2 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