Leukotriene A-4 hydrolase homolog - Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (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:	ADL233W
ORF Names:	AGOS_ADL233W

Organism

Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]

Taxonomic identifier

284811 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium ›

Protein attributes

Sequence length	623 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 protein catabolic process Inferred from electronic annotation. Source: EnsemblFungi 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 – 623

623

Leukotriene A-4 hydrolase homolog

PRO_0000324917

Regions

Region

140 – 142

3

Substrate binding By similarity

Region

266 – 271

6

Substrate binding By similarity

Sites

Active site

296

1

Proton acceptor By similarity

Active site

382

1

Proton donor By similarity

Metal binding

295

1

Zinc; catalytic By similarity

Metal binding

299

1

Zinc; catalytic By similarity

Metal binding

318

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q75B10 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: F390F56063A931C1
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FASTA

623

69,174

        10         20         30         40         50         60 
MKLPAVLEER RAAATDRSTL SNYEDFAVRH TNLELEVAFD ERQIRAEVCY DLEQTGKGVA 

        70         80         90        100        110        120 
EVHLDTSYVQ LECILVDGKR VPWELRERQE PLGSQLVITP EGGLPARFQL TCRSVTTARS 

       130        140        150        160        170        180 
TAVQWLGGAQ TAGKPYVYTQ LESVHARSLV PCFDTPACKS PFTVRVRSPL RAVVAGQEQP 

       190        200        210        220        230        240 
GSGKDGVYVF EQPVPIPIYL LGLAAGDIAC APLGPRSNVY CEPALLEAAA GEFGGEIERF 

       250        260        270        280        290        300 
LDAAEELLPR YIWGNYNLLV CPSSYPYGGM EVAGTSFISP SVIAYDRSNN DLIVHEMAHS 

       310        320        330        340        350        360 
WSGNLITNAN WGHFWLNEGW TVYLERRITG ALHGEDTRQF SSLLGMAELE VAIRASNGAS 

       370        380        390        400        410        420 
FALVEDVSES VNPDNVVSLA AYEKGSALLL HLERELGGTA AFDPFIKHYF GKFGGQSLTT 

       430        440        450        460        470        480 
WQFLDILFDF FADKREKLER IDWKTWLFAP GMPPKLTYST SLADDVYDLA EQWLEKAVQL 

       490        500        510        520        530        540 
RLPEEFAAEF SGSVLAAFTT AQQILFLNTI IQGGVSPDNT FDWTQHPVAA AALLSVYADT 

       550        560        570        580        590        600 
LGKSRNQEII YRRYNFQLTA GMEDAYPEIT TWLGSTGRMK HVRPIYRRLA SIDKALAAST 

       610        620 
FQEHREKYHP ICRAAIQADL GLS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]	Dietrich F.S., Voegeli S., Philippsen P. Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 430 AND 448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016817 Genomic DNA. Translation: AAS51687.2.
RefSeq	NP_983863.2. NM_209216.2.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q75B10.
ModBase	Search...
Protein-protein interaction databases
STRING	33169.AGOS_ADL233W.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4619998.
KEGG	ago:AGOS_ADL233W.
Phylogenomic databases
eggNOG	COG0308.
HOGENOM	HOG000293296.
KO	K01254.
OMA	PCSAANI.
OrthoDB	EOG49KJZX.
Enzyme and pathway databases
UniPathway	UPA00878.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. 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.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_ASHGO

Accession

Primary (citable) accession number: Q75B10

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	January 9, 2013
Last modified:	May 1, 2013
This is version 71 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents