Leukotriene A-4 hydrolase homolog - Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (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

ORF Names:

LELG_00410

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	648 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.
Sequence caution	The sequence EDK42232.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 648

648

Leukotriene A-4 hydrolase homolog

PRO_0000324931

Regions

Region

143 – 145

3

Substrate binding By similarity

Region

269 – 274

6

Substrate binding By similarity

Sites

Active site

299

1

Proton acceptor By similarity

Active site

408

1

Proton donor By similarity

Metal binding

298

1

Zinc; catalytic By similarity

Metal binding

302

1

Zinc; catalytic By similarity

Metal binding

321

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5DSS4 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: C3C91E3173D14493
Show »

FASTA

648

75,111

        10         20         30         40         50         60 
MEELKAYRPK TSPELDPSTL SNYTCFTVKL TTLHFDIDFE KKIVSGKVKY DLLNKSETDH 

        70         80         90        100        110        120 
VDLDTSYLDI TKVSIQNESC DNQYKLHSRK EPLGSKLHIL IPASTPKNFQ LEIEFSTTSK 

       130        140        150        160        170        180 
CTALQFLDKE ATDGKNHPYL FCQCQAIHAR SLFPSFDTPG IKSPYKFSAK SPLKTLLSGL 

       190        200        210        220        230        240 
LIKEDNENNT VYFEQPVPIP SYLVSIALGD IARTSIGPRS DVMTEPVNLA KCKWEFERDM 

       250        260        270        280        290        300 
ENFIQVAEKL IFEYEWQKFD SLVLPASFPY GGMEIPNLCQ LTPTLICGDR SLVNVVAHEL 

       310        320        330        340        350        360 
AHSWSGNLVT NCSWEHFWLN EGWTVYLERR ILEALAVIEA KQQGKGDKEA HYYGEQVRQF 

       370        380        390        400        410        420 
NAIIGWTDLE NDLKSMGDNV DKYSILVQDL KGKKNPDDPD DAFSTVPYEK GFNLLYLIEK 

       430        440        450        460        470        480 
IVGKEKFDLF IPAYFREFRF KSLDTFQFID YLFDFFKEDA VKLDQIEWKK WLYEPGMPPI 

       490        500        510        520        530        540 
DPKFDTTLAQ ACYDLAKKCY QYALSEDDEN EFTQFKLVAN EINDFSPSQN IVFLDTLIAY 

       550        560        570        580        590        600 
EKVAGFSWKQ HKKTLNRMAT LYHDQYTETL NAEIKFRWFY LQATGEVLDF EVAMGEFLGT 

       610        620        630        640 
IGRMKFVRPG YALLNKVNRE LAVRYFQRFE NRYHPICKAM VRKDLQLD

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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: 19465905] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981524 Genomic DNA. Translation: EDK42232.1. Sequence problems.
RefSeq	XP_001527890.1. XM_001527840.1.
3D structure databases
ProteinModelPortal	A5DSS4.
ModBase	Search...
Protein-protein interaction databases
STRING	A5DSS4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5235941.
KEGG	lel:LELG_00410.
Phylogenomic databases
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_LODEL

Accession

Primary (citable) accession number: A5DSS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	November 16, 2011
This is version 39 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

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents