Leukotriene A-4 hydrolase homolog - Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)

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:

ACLA_079530

Organism

Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]

Taxonomic identifier

344612 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	618 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 – 618

618

Leukotriene A-4 hydrolase homolog

PRO_0000324918

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

389

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

A1CSI2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 145E2B2F39F1304B
Show »

FASTA

618

70,370

        10         20         30         40         50         60 
MATVINPPRD PNTLSNYNNW VSIHITANFD ILFDQKKLAG NVVHRFRSTT RGESRDIILD 

        70         80         90        100        110        120 
TNHLDIGGVK VNGQPSSWEF LPRLEPYGTP LKIKLDQAVE LDETIEVDIS VTTTEKCTAL 

       130        140        150        160        170        180 
QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKCT LDFNITSPLP VIASGLPVRK 

       190        200        210        220        230        240 
QPETSKSEGK SLYQFHQKVP IPSYLFALAS GDISEASIGP RSVVATSPDK LRECQWELEA 

       250        260        270        280        290        300 
DTEKFINAIE KIVYPYVWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENIDVIAH 

       310        320        330        340        350        360 
ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRVSDASVHG EPYRHFSAII GWKALTDSMD 

       370        380        390        400        410        420 
HFGHDHDFTK LITNLKGKDP DDAFSSIPYE KGFNFLYYLE TLVGKSKFDD FIPHYFNKFK 

       430        440        450        460        470        480 
GKSLDSYEFK ATILDFFQAD SEAAKALNEV DWDKWFYAPG LPPKPDFDTS LVDVVYDLAK 

       490        500        510        520        530        540 
KWLSLPGSSF KPQPNDIRGL SANQIVVFLE QVLVSEHQLT PELSRLMGEV YGLARSNNIE 

       550        560        570        580        590        600 
VANLYCQVGM KAGDESVLEP TIELLGKIGR MKFVRPLYRN LQKFNRQRAI ETFQEYKDFY 

       610 
HPICRAMVEK DLFGKKEE

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References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus."
Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.

Nierman W.C.
PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027060 Genomic DNA. Translation: EAW06269.1.
RefSeq	XP_001267695.1. XM_001267694.1.
3D structure databases
ProteinModelPortal	A1CSI2.
ModBase	Search...
Protein-protein interaction databases
STRING	A1CSI2.
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADACLAT00008253; CADACLAP00008062; CADACLAG00008253.
GeneID	4700012.
KEGG	act:ACLA_079530.
Phylogenomic databases
GeneTree	EFGT00050000003006.
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_ASPCL

Accession

Primary (citable) accession number: A1CSI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 41 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