Leukotriene A-4 hydrolase homolog - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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:

AO090011000940

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length	615 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 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 – 615

615

Leukotriene A-4 hydrolase homolog

PRO_0000324921

Regions

Region

139 – 141

3

Substrate binding By similarity

Region

271 – 276

6

Substrate binding By similarity

Sites

Active site

301

1

Proton acceptor By similarity

Active site

386

1

Proton donor By similarity

Metal binding

300

1

Zinc; catalytic By similarity

Metal binding

304

1

Zinc; catalytic By similarity

Metal binding

323

1

Zinc; catalytic By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2TZ99 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: B2669E5A98060C85
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FASTA

615

69,817

        10         20         30         40         50         60 
MATVIHSPRD PNTLSNYNNW VSTHITATFD ILFEQKKLVG NVVHKLKSIT DARSTEIILD 

        70         80         90        100        110        120 
TNHVDIGDVK VDGQASHWEL LPPLEPYGAA LKINLDQGVG LNEMVEVEIS VKTTEKCTAL 

       130        140        150        160        170        180 
QWLTPAQTSN RKHPYMFSQC QAIHARSIFP CQDTPDVKST IDFNITSPLP VVASGLPVRG 

       190        200        210        220        230        240 
IIEKAQPGSK TLYQFHQKLP IPSYLFALAS GDISEAAIGP RSVVATSPDK LSECQWELKA 

       250        260        270        280        290        300 
DTENFIHAIE KIVYPYAWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENVDVIAH 

       310        320        330        340        350        360 
ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRVSLHGEAY RHFSAIIGWK SLADSVEHFG 

       370        380        390        400        410        420 
HDHPFTKLVT DLKGKDPDDA FSSIPYEKGF NFLFHLENLL AKDKFDRFIP HYFTKFKGKS 

       430        440        450        460        470        480 
LDSYEFKATM LEFFQHDLEA SNLLKNVDWD AWFYAPGLPP KPQFDTSLVD VVYELSSKWK 

       490        500        510        520        530        540 
SLPDSSFQPR TSDIEGLTAN QIVVLLEQIL LFERPLTPEL SRVLGEVYSL AKSENIEVSN 

       550        560        570        580        590        600 
LYFQVGLRAG DDTVYKPTAE LLGKIGRMKF VRPLYRNLQK VNRPLAIETF EKNKDFYHPI 

       610 
CRAMVEKDLF GKREE

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References

[1]

"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.

Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007171 Genomic DNA. Translation: BAE65366.1.
3D structure databases
ProteinModelPortal	Q2TZ99.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00005524.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00005625; CADAORAP00005524; CADAORAG00005625.
Phylogenomic databases
eggNOG	COG0308.
HOGENOM	HOG000293296.
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

LKHA4_ASPOR

Accession

Primary (citable) accession number: Q2TZ99

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 56 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

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents