Leukotriene A-4 hydrolase homolog - Yarrowia lipolytica (strain CLIB 122 / E 150) (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:

YALI0F00396g

Organism

Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)

Taxonomic identifier

284591 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	647 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 Reference 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 – 647

647

Leukotriene A-4 hydrolase homolog

PRO_0000324942

Regions

Region

169 – 171

3

Substrate binding By similarity

Region

295 – 300

6

Substrate binding By similarity

Sites

Active site

325

1

Proton acceptor By similarity

Active site

418

1

Proton donor By similarity

Metal binding

324

1

Zinc; catalytic By similarity

Metal binding

328

1

Zinc; catalytic By similarity

Metal binding

347

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6C3E5 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 5171D59AE03DA696
Show »

FASTA

647

72,895

        10         20         30         40         50         60 
MFSLRALSGV VTRSLVRAPH RRTMSHAARL LPHRVPQKKG PERDPSTLSN YEHFKPTNTT 

        70         80         90        100        110        120 
VCLKVDWTDQ KLAGSVTYDL TVENSPKNLV LDTSYLDIQE VQVNGHKADF SIGERHNIFG 

       130        140        150        160        170        180 
SPLTITLPPN SGDKLQVKIA YSTTPSCTAL QWLTPEQTAG KKAPYFFSQC QAIHARSVMP 

       190        200        210        220        230        240 
AFDTPSVKST FDIEIESDHP VVASGLPIKS SNDTGKFVFR QKVPIPAYLF ALAGGDLDSA 

       250        260        270        280        290        300 
PIGPRSDVYS EPCDLHKCQY EFEADTEKFI NAAENIVFPY EWEKYDVLVL PPSFPYGGME 

       310        320        330        340        350        360 
NPNITFATPT LVSGDRQNVD VIAHELAHSW SGNLVTNCSW EHFWLNEGWT VYLERRIVGA 

       370        380        390        400        410        420 
LEGEQQRHFS AIIGWNALEE SVKLMSRDPV QESYTQLVVD LKPNGGADPD DAFSSVPYEK 

       430        440        450        460        470        480 
GSTFLFFLET EIGQAKFDPF VKHYFKHFRY KSLDTYQFID CLFDFYANDK EVTDKLNAID 

       490        500        510        520        530        540 
WEKTLFAPGL PNKPKFDTTL ADECYSLASR WKDASDASAF SAKDIASFNS SQMVVFLITL 

       550        560        570        580        590        600 
SEYEGKDGFS WANKKELISN MGDIYSLANS SNPEVIAKWY SIAILAKVES EYPKLADWLA 

       610        620        630        640 
TVGRMKFVRP GYRALNSVDP KLAKETFEKN KDFYHPICRD MVSKDLQ

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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: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR382132 Genomic DNA. Translation: CAG77619.1.
RefSeq	XP_504817.1. XM_504817.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q6C3E5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6C3E5.
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2908541.
GenomeReviews	Gene locus YALI0F00396g in contig CR382132_GR.
KEGG	yli:YALI0F00396g.
Phylogenomic databases
eggNOG	fuNOG04031.
HOGENOM	HBG444814.
OMA	QEVKYTL.
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_YARLI

Accession

Primary (citable) accession number: Q6C3E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	August 16, 2004
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 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

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents