Leukotriene A-4 hydrolase homolog 2 - Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Leukotriene A-4 hydrolase homolog 2
Short name=LTA-4 hydrolase 2
EC=3.3.2.6

Alternative name(s):
Leukotriene A(4) hydrolase

Gene names

ORF Names:

PGUG_02354

Organism

Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

294746 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	631 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 – 631

631

Leukotriene A-4 hydrolase homolog 2

PRO_0000324937

Regions

Region

140 – 142

3

Substrate binding By similarity

Region

265 – 270

6

Substrate binding By similarity

Sites

Active site

295

1

Proton acceptor By similarity

Active site

395

1

Proton donor By similarity

Metal binding

294

1

Zinc; catalytic By similarity

Metal binding

298

1

Zinc; catalytic By similarity

Metal binding

317

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5DGF3 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 689055C32D166BC7
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FASTA

631

72,546

        10         20         30         40         50         60 
MNVNELRSRA ASQEQDPCTL SNYRGFEVVQ SSLDLNVSFE KKNVSGTVTY ELKNLKSTTE 

        70         80         90        100        110        120 
VVLDTSFLDI EQAFVDEKAV DFKLEARKEP FGSPLVIKLA NVVEKLKISI KFATTENCSA 

       130        140        150        160        170        180 
LQFIDKEATD SKVCDYLFSQ CQAIHARSLF PCFDTPAVKS PYSFHVKSPS YTLMSGRPVE 

       190        200        210        220        230        240 
CSEENTYRFE QPIPIPSYLV AIASGNLAGA PIGPRSTVYT EPPNLKACQW EFEKDMENFL 

       250        260        270        280        290        300 
VVAEDLIYKY EWLKYDALIL PSSFPYGGME NPNITFATPT LISKDRSQVK VMAHELAHSW 

       310        320        330        340        350        360 
SGNLVTNCTW EHFWLNEGWT VYLERRILGG VASYEAKQRG EKDYVDAGEK VRHFAAILGW 

       370        380        390        400        410        420 
NDLVDTVKTI PSQYTRLVWD LKTVTPDDAF SKIPYEKGFS FLFYLETVLG GTDEFDPFMK 

       430        440        450        460        470        480 
HYFKKYRYKS LDSYQFIDTL YEFFEPKGKK DVLDSVDWNT WLYGEGVPPF TPKYDTRLAD 

       490        500        510        520        530        540 
ECYHLRDKWA AYEQNKGQFS ASDIEHFEVN QHLLFLGTLT ELFSNKKPAP EVYEELRKVY 

       550        560        570        580        590        600 
HQYSEASNCE IIASWNDLLL KSENFKPSDK IVQNFATWLG TVGRMKFARP GYKLLKDYVD 

       610        620        630 
KDLAIATFRK FESRYHPICK AMVRKDLGLD S

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References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes."
Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J.

Cuomo C.A.
Nature 459:657-662(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH408157 Genomic DNA. Translation: EDK38256.2.
RefSeq	XP_001484625.1. XM_001484575.1.
3D structure databases
ProteinModelPortal	A5DGF3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5126859.
KEGG	pgu:PGUG_02354.
Phylogenomic databases
eggNOG	COG0308.
KO	K01254.
OrthoDB	EOG49KJZX.
Enzyme and pathway databases
UniPathway	UPA00878.
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]
PANTHER	PTHR11533. PTHR11533. 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

LKA42_PICGU

Accession

Primary (citable) accession number: A5DGF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 45 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents