Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q1DVD1 (LKHA4_COCIM)

Last modified November 3, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Leukotriene A-4 hydrolase
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase
Gene names
ORF Names: CIMG_05732
OrganismCoccidioides immitis (Valley fever fungus) [Complete proteome]
Taxonomic identifier5501 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesmitosporic OnygenalesCoccidioides

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Hydrolyzes an epoxide moiety of LTA4 to form LTB4. The enzyme also has some peptidase 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.

Pathway

Lipid metabolism; leukotriene B4 biosynthesis.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Leukotriene A-4 hydrolase
PRO_0000324927

Sites

Active site3011 By similarity
Active site3921Proton donor By similarity
Metal binding3001Zinc; catalytic By similarity
Metal binding3041Zinc; catalytic By similarity
Metal binding3231Zinc; catalytic By similarity
Site2041Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1DVD1-1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 91D14256BB6736F7

FASTA62170,941
        10         20         30         40         50         60 
MATPANPLRD PNTLSNYNKF RTVHTSVNFE IRFDQKRLVG NVIHRLKSLT NAESKEVILD 

        70         80         90        100        110        120 
SSYLEVKSVK VNGEAAEWQL LPRFEPYGSP LKISLEQAIP LDELIEVDIS VNTTEKCTAL 

       130        140        150        160        170        180 
QWLNPEQTSN GKHPYMFSQC QAIHARAIFP CQDTPDVKAT FDFNLSSPLP VIASGVPVKQ 

       190        200        210        220        230        240 
DASPPQSSGS IYYRFEQKVP IPSYLFAIAS GDIAQAQIGP RSHVAVSPDR LDECKWELEG 

       250        260        270        280        290        300 
DTERFLQTIG NIIFPYVWGE YNVLILPPSF PYGGMENPVY TFATPSIISK DRQNVDVIAH 

       310        320        330        340        350        360 
EISHSWSGNL VTNCSWEHFW LNEGWTTYLE RRVCLHCVFI CHGEPYRHFS AIIGWKHLVD 

       370        380        390        400        410        420 
SVERHGDTHE FTKLVVDLKG KDPDDAFSSV PYEKGFTFIF HLENLIGKDK FDKFIPHYFT 

       430        440        450        460        470        480 
RFRGKSLDSY EFKSCILDFF ASDEESHVLL NKLDWDSWFY KPGLPPKPSF DTSLVDVVYE 

       490        500        510        520        530        540 
LANKWKYISQ SSFSPKASDM DGLVANQIVV FLEQVLLFDN PLTPEQSRFM GQVYNFAQSQ 

       550        560        570        580        590        600 
NIEVSYLYLQ VGLKAGDDSI VEPTIKLLGE IGRMKFVRPL YRTLEKFNRD IAVDTFEKHK 

       610        620 
NFYHPICRGL LEKDLFGDKG A 

« Hide

References

[1]"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives."
Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. expand/collapse author list , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.
Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RS.

Cross-references

Sequence databases

CH476728 Genomic DNA. Translation: EAS30253.1. Different initiation.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.3.2.6. 97654.

Family and domain databases

InterProIPR012777. Leuk_A4_hydro_aminopept.
IPR006025. Pept_M_Zn_BS.
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.
TIGRFAMsTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLKHA4_COCIM
AccessionPrimary (citable) accession number: Q1DVD1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 3, 2009
This is version 24 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents