Leukotriene A-4 hydrolase homolog - Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181)

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:

NFIA_083260

Organism

Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]

Taxonomic identifier

331117 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya

Protein attributes

Sequence length	617 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 – 617

617

Leukotriene A-4 hydrolase homolog

PRO_0000324933

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

388

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

A1DG68 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 1365EBF978DA3519
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FASTA

617

69,941

        10         20         30         40         50         60 
MPTVVNPPRD PNTLSNYNNW VSTHITANFD ILFDQRKLAG SVIHQFRSTT HGESNHIILD 

        70         80         90        100        110        120 
TNHLDIGSVK VNGQPSEWEY LPRLEPYGTP LKIKLDQGVK LNEMIEVDIS VKTTEKCTAL 

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

       190        200        210        220        230        240 
SSEAPKSDGK TLYKFHQKVP IPSYLFALAS GDISEAPIGP RSVVATSPDK LGECQWELEA 

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

       310        320        330        340        350        360 
ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRIVAAVHGE PYRHFSAIIG WKALTDSVEH 

       370        380        390        400        410        420 
FGPEHDFTKL ITNLKGMDPD DAFSSIPYEK GFNFLFHLEN LVGKSKFDLF IPHYFNKYKG 

       430        440        450        460        470        480 
KSLDSYEFKS TILDFFKDDS EASTALNELD WDSWFYAPGL PPKPDFDTSL VDVVYDLAKK 

       490        500        510        520        530        540 
WLSLPNSSFK PQPEDIRGLT ANQVVVFLEQ ILVSERQLTP ELSKLMGEIY GLAASQNIEV 

       550        560        570        580        590        600 
ANLYFQVGLQ AGDASVLEPT ADLLGKIGRM KFVRPLYRKL AKFDRKRAVE TFEKHRDFYH 

       610 
PICRAMVEKD LFGKKDE

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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 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027696 Genomic DNA. Translation: EAW18375.1.
RefSeq	XP_001260272.1. XM_001260271.1.
3D structure databases
ProteinModelPortal	A1DG68.
ModBase	Search...
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADNFIAT00007676; CADNFIAP00007509; CADNFIAG00007676.
GeneID	4586829.
KEGG	nfi:NFIA_083260.
Phylogenomic databases
GeneTree	EFGT00050000003006.
OrthoDB	EOG49KJZX.
PhylomeDB	A1DG68.
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_NEOFI

Accession

Primary (citable) accession number: A1DG68

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 family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents