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Q6FTM0 (LKHA4_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. 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
Ordered Locus Names:CAGL0G01430g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length652 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 – 652652Leukotriene A-4 hydrolase homolog
PRO_0000324925

Regions

Region165 – 1673Substrate binding By similarity
Region293 – 2986Substrate binding By similarity

Sites

Active site3231Proton acceptor By similarity
Active site4111Proton donor By similarity
Metal binding3221Zinc; catalytic By similarity
Metal binding3261Zinc; catalytic By similarity
Metal binding3451Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6FTM0 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 4AD4BB847DEF880B

FASTA65274,823
        10         20         30         40         50         60 
MINRLIQRIV PFSRPLSTVK KTMLTPFLES KRPQQSPEYD YSTLSNYKSF QIKHTTLNFL 

        70         80         90        100        110        120 
LSFEKSTVSG DVVFDLTTLK EAVKHIDLDT SYLDVNEVLV DDKPVEFKIE ERKQPLGSKL 

       130        140        150        160        170        180 
VIAAELEAER QFKLRVKFST TKDCTALQWL TPQQTSGDKP YMFSQLEAIH ARALFPCFDT 

       190        200        210        220        230        240 
PSYKSTFTAN IESTLPVVFS GIATGSTPNG ESTVYHFKQD IPIPAYLVGI ASGDLVSASI 

       250        260        270        280        290        300 
GPRSKVYTEP HRLDDCVWEF SNDVEKFIKT AENLIFDYEW GTYDILVNVD SYPYGGMESP 

       310        320        330        340        350        360 
NMTFATPTLI AHDKTNIDVI AHELAHSWSG NLVTNCSWNH FWLNEGWTVY IERRIVGALH 

       370        380        390        400        410        420 
GEPTRHFSAL IGWSDLENSI NSMRNPEKFS TLVQNLNDGT DPDDAFSTVP YEKGFNLLFH 

       430        440        450        460        470        480 
LETVLGGPQE FDPFIRHYFK KFARQSLDTF QFLDTLFEFF ENKREILENV DWETWLFKPG 

       490        500        510        520        530        540 
MPPKPQFITT MADNVFSLVN KWIVKAQELK TTEEFSKEFS ESDLSEFNSN QVVLFLEELV 

       550        560        570        580        590        600 
AQNCVPVESK IEWSKYSVAS ESLLSIYKKQ VTESQNAEVV FKNYKFQTTA RIQPSYQQLA 

       610        620        630        640        650 
NWLGTVGRMK FVRPGYRLLN AVDRDLAIAT FEKLKDTYHP ICKQLVKQDL EL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380953 Genomic DNA. Translation: CAG59351.1.
RefSeqXP_446424.1. XM_446424.1.

3D structure databases

HSSPHSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortalQ6FTM0.
ModBaseSearch...

Protein family/group databases

MEROPSM01.034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2888012.
KEGGcgr:CAGL0G01430g.

Phylogenomic databases

HOGENOMHOG000293296.
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_CANGA
AccessionPrimary (citable) accession number: Q6FTM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 19, 2004
Last modified: May 1, 2013
This is version 67 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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