Reviewed, UniProtKB/Swiss-Prot Q7S785 (LKHA4_NEUCR)

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:

NCU06732

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.

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 – 614	614	Leukotriene A-4 hydrolase		PRO_0000324934
Sites
	Active site	295	1	By similarity
	Active site	383	1	Proton donor By similarity
	Metal binding	294	1	Zinc; catalytic By similarity
	Metal binding	298	1	Zinc; catalytic By similarity
	Metal binding	317	1	Zinc; catalytic By similarity
	Site	198	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7S785-1 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 21B9E4B81C1B4C31	FASTA	614	69,001
	10 20 30 40 50 60 MAPVRDPNTL SNYDAWRTRH TTANLKIDFT AKCLRGSVIL ELESQTDKAS KEIVLDSSYV 70 80 90 100 110 120 TVNSIKLNSA PSLWETKART EPNGSPVHIA VPEGAAKGEV VKVEIELATT DKCTALQWLT 130 140 150 160 170 180 PAQTSDKAAP FMFSQCQAIH ARSLFPCQDT PDVKSTYDFN ITSPYVVVAS GVPVPDETKD 190 200 210 220 230 240 LGEEKLYKFQ QKVPIPSYLF ALSSGEIASA PVGKRSCVCT GPNELKASQW ELEGDMDKFL 250 260 270 280 290 300 EAAEKIVFPY RWGEYNVLVL PPSFPYGGME NPIFTFATPT IISGDKQNID VIAHELAHSW 310 320 330 340 350 360 SGNLVTSCSW EHFWLNEGWT MYLERRILAS IHGGDAHFDF SAIRGWKALE EAIKEYGEDH 370 380 390 400 410 420 EFTKLCISHK GIDPDDAFST VPYEKGFHFV WSLDRLVGRE NFDKFIPYYF GKWSNKSLDS 430 440 450 460 470 480 YEFKDTFLEF FSAPEYSDLK DKIASIDWEG RFHSTGLPPK PEFDTSLADV CYELAEKWKS 490 500 510 520 530 540 KDFTPSPSDV ASWTGNQVLV FLNAVQDFEE PLTVEQSQAL GKAYGLSESK NAELKAAYYH 550 560 570 580 590 600 IAMRSKDASA YQGVADLLGE VGRMKFVRPL FRGLNKVDRE LALKTFEKNR EFYHPICRQM 610 VEKDLGVSEA ANSS

References

[1]

"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABX02000031 Genomic DNA. Translation: EAA31424.1.
RefSeq	XP_960660.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7S785.
Genome annotation databases
GeneID	3876807.
KEGG	ncr:NCU06732.
NMPDR	fig|5141.1.peg.4951.
Enzyme and pathway databases
BRENDA	3.3.2.6. 266.
Family and domain databases
InterPro	IPR012777. Leuk_A4_hydro_aminopept. IPR006025. Pept_M_Zn_BS. 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_NEUCR

Accession

Primary (citable) accession number: Q7S785

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	December 15, 2003
Last modified:	September 1, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)