Leukotriene A-4 hydrolase homolog - Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast)

Preferred order of sections

Names and origin

Protein names

Recommended 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:

DEHA2B14960g

Organism

Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]

Taxonomic identifier

284592 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB epoxide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB leukotriene-A4 hydrolase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 641

641

Leukotriene A-4 hydrolase homolog

PRO_0000324928

Regions

Region

145 – 147

3

Substrate binding By similarity

Region

270 – 275

6

Substrate binding By similarity

Sites

Active site

300

1

Proton acceptor By similarity

Active site

401

1

Proton donor By similarity

Metal binding

299

1

Zinc; catalytic By similarity

Metal binding

303

1

Zinc; catalytic By similarity

Metal binding

322

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6BW21 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 2D9E4A4206AD9C6F
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FASTA

641

73,104

        10         20         30         40         50         60 
MTLEYINKKR PSVSPELDPC SNSNYKDFQV SNTELDISVS FDKKIVSGQV TYKLTAKTPN 

        70         80         90        100        110        120 
TTSIVLDTSY LKIIKIRING LPSDNYELVK RKEPFGSPLK ISLPTTINKE FELNIEFSTT 

       130        140        150        160        170        180 
DKCTALQFIE KEATDGQTAP YLFSQCQAIH ARSLFPCFDT PGIKSPYNMK VKSPYACLMS 

       190        200        210        220        230        240 
GRPKETNEEG VYCFHQPIPI PSYLVALASG DLASAPIGPR STVYSERVGL SDCQWEFEKD 

       250        260        270        280        290        300 
MENFIQVAEG LIFKYEWLKF DALILPSSFP YGGMENPNIT FATPTLISKD RSQVKVMAHE 

       310        320        330        340        350        360 
LAHSWSGNLV TNCSWEHFWL NEGWTVYLER RIIGGIAAAE AKSLGEKEAA QYGEKRRHFS 

       370        380        390        400        410        420 
AIVGWNSLVD SVKTLDPKYT SLVWNLKEGS DPDDAFSRIP YEKGFNFLFY IEQQVGGIKE 

       430        440        450        460        470        480 
FDPFIPYYFK KFRYESLDTY QFIDVLYEFF EPRGKAAKLD AIDWKGWIFG EGLPPNIPQF 

       490        500        510        520        530        540 
DPSLADECYR LVDKWVDFAK SNSTDISGFN ESRDIGNFEP DQHKLFLESL TEKFGAYSVS 

       550        560        570        580        590        600 
EQIIRKLPSI YPFYAASTNG EIKSSWNELL IRFGNYNTTD QIVQDFAMWL GTVGRMKFVR 

       610        620        630        640 
PGYKLLQAYV SKEFAISTFT KFESSYHPIC KTMVKKDLSL I

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References

[1]

"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.

Souciet J.-L.
Nature 430:35-44(2004) [PubMed: 15229592] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382134 Genomic DNA. Translation: CAG85609.2.
RefSeq	XP_457598.2. XM_457598.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2913567.
GenomeReviews	Gene locus DEHA2B14960g in contig CR382134_GR.
KEGG	dha:DEHA2B14960g.
Phylogenomic databases
HOGENOM	HBG444814.
OMA	STIHATA.
OrthoDB	EOG49KJZX.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR012777. Leukotriene_A4_hydrolase. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
KO	K01254.
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
TIGRFAMs	TIGR02411. Leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_DEBHA

Accession

Primary (citable) accession number: Q6BW21

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	December 16, 2008
Last modified:	November 16, 2011
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal 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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents