A2QKF8 (LKHA4_ASPNC) Reviewed, UniProtKB/Swiss-Prot

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:

An05g00070

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

Taxonomic identifier

425011 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus › Aspergillus niger

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.
Sequence caution	The sequence CAK44827.1 differs from that shown. Reason: Erroneous initiation.

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 – 618	618	Leukotriene A-4 hydrolase homolog		PRO_0000324920
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)
	A2QKF8 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 7AD5021B3129A1FC	FASTA	618	69,842
	10 20 30 40 50 60 MAISIHPPRD PNTLSNYNNW ICTHITANFD ILFDQKKLVG NVIHKLKSTT NGESQEIILD 70 80 90 100 110 120 SNHVAIGDVK IDGRPSEWEL LPPLEPYGSA LKIKLDQGVN LNETIDVEIS VQTTEKCTAL 130 140 150 160 170 180 QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKST IDFNISSPLP VIASGLPVRD 190 200 210 220 230 240 ALGASKSEGK SLYQFHQRVP IPSYLFALAS GDISEAAIGP RSVVATSPDK VQECQWELEA 250 260 270 280 290 300 DTEKFIGAIE KIVYPYAWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENIDVIAH 310 320 330 340 350 360 ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRILAAVHGE AYRHFSAIIG WKALTDSVEH 370 380 390 400 410 420 FGHDHEFTKL ITDLKGKDPD DAFSSIPYEK GFNFLFHLET LVGKQKFDRF IPHYFTVFKG 430 440 450 460 470 480 KSLDSYEFKA TLLDFFGTDA EASKLLNDLD WDTWFYAPGL PPKPQFDTSL VDVVYELAQK 490 500 510 520 530 540 WKSLSETSSF KPQLSDIESL SANQIVVFLE QMLLLERPLT PELSKLMGEV YGLSKSENIE 550 560 570 580 590 600 VANLYFQLGL KAGDENVVDP ATELLGRIGR MKFVRPLFRS LQRVNREVAV ATFEKYKDFY 610 HPICRAMVEK DLFGKRDV

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88." Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M. , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H. Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270101 Genomic DNA. Translation: CAK44827.1. Different initiation.
3D structure databases
ProteinModelPortal	A2QKF8.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00004659.
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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_ASPNC

Accession

Primary (citable) accession number: A2QKF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	May 1, 2013
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program