Reviewed, UniProtKB/Swiss-Prot Q0CFY9 (LKHA4_ASPTN)

Names and origin

Protein names

Recommended name:
    Leukotriene A-4 hydrolase
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase

Gene names

ORF Names:

ATEG_06861

Organism

Aspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]

Taxonomic identifier

341663 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	617 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Hydrolyzes an epoxide moiety of LTA4 to form LTB4. The enzyme also has some peptidase activity 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 EAU32245.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAU32245.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	leukotriene-A4 hydrolase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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		PRO_0000324922
Sites
	Active site	301	1	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
	Site	204	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0CFY9-1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: F0BC113CF9551639	FASTA	617	69,701
	10 20 30 40 50 60 MATTINPPRD PNTLSNYNNW LSTHITANFD ILFDQKKLVG NVIHKLKSIT NAESTDIVLD 70 80 90 100 110 120 TSHVDVTDVK VDGKPSVWEL LPPVKPYGTA LKIKLDQGVK MDEIVHVDIS VKTTEKCTAL 130 140 150 160 170 180 QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKST IDFNITSPLP VIASGLLVRD 190 200 210 220 230 240 ASGAPQTGGK NLYQFHQKVP IPSYLFALAS GDISEAAIGP RSVVATSPDK LRECQWELEA 250 260 270 280 290 300 DTENFINAIE KIVYPYVWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENVDVIAH 310 320 330 340 350 360 ELAHSWSGNL VTNASWEHFW LNEGWTVYLE RRILAAVHGE AYRHFSAIIG WKALSDSVDH 370 380 390 400 410 420 FGHDHEFTRL ITDLKGKDPD DAFSSIPYEK GFNFLFHLEN LVGKQKFDQF IPHYFTKFKG 430 440 450 460 470 480 KSLDSYEFKA TILDFFKSDA EASKLLNELD WDTWFYAPGL PPKPKFDTSL VDVVYDLAKK 490 500 510 520 530 540 WQSIPESSFK PQPSDIKDLT GNQIVVFLEQ VLLFERPLAP ELSKLMGEVY GLAKSANIEV 550 560 570 580 590 600 ANLYFRVGLN AGDESVFEPT ADLLGKIGRM KFVRPLYRNL QKVNRPLAIE TFEKNKDFYH 610 PICRAMVEKD LFGKKDA

References

[1]

"Annotation of the Aspergillus terreus NIH2624 genome." Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. , Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., Nierman W.C., Milne T., Madden K. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH476603 Genomic DNA. Translation: EAU32245.1. Sequence problems.
RefSeq	XP_001209547.1.
3D structure databases
SMR	Q0CFY9. Positions 7-611.
ModBase	Search...
Genome annotation databases
GeneID	4319230.
Phylogenomic databases
OrthoDB	EOG92RFQK.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR012777. Leuk_A4_hydro_aminopept. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
TIGRFAMs	TIGR02411. leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_ASPTN

Accession

Primary (citable) accession number: Q0CFY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	February 9, 2010
This is version 28 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)