Reviewed, UniProtKB/Swiss-Prot O94544 (LKHA4_SCHPO)

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:

SPCC1322.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
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 – 612	612	Leukotriene A-4 hydrolase		PRO_0000095128
Sites
	Active site	295	1	By similarity
	Active site	382	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)
	O94544-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 19D3DFFC5CE2A341	FASTA	612	69,522
	10 20 30 40 50 60 MKLRLDPSTQ SNYHDVSISK LDWHARIDFD QELLHGKVSF VIQSARVSQA LSHIILDTSY 70 80 90 100 110 120 LEIKNVTIND IPTPFRVDKR RGFLGSALHI VPADEIPSSK SCILTILYST TKDCTALQFL 130 140 150 160 170 180 KPEQTIGGKF PYVFSECQAI HARSFIPCQD TPSVKVPCTF KIRSKLPVIA SGIPCGTANF 190 200 210 220 230 240 CNGSLEYLFE QKNPIPSYLF CILSGDLAST NIGPRSSVYT EPGNLLACKY EFEHDMENFM 250 260 270 280 290 300 EAAEQLTLPY CWTRYDFVIL PPSFPYGGME NPNATFATPT LIAGDRSNVN VIAHELAHSW 310 320 330 340 350 360 SGNLVTNESW QCFWLNEGMT VFLERKILGR LYGEPTRQFE AIIGWGELEE SVKLLGEDSE 370 380 390 400 410 420 YTKLIQNLEG RDPDDAFSTV PYEKGSNFLY EIERVIGGPS VFEPFLPFYF RKFAKSTVNE 430 440 450 460 470 480 VKFKHALYEY FSPLGLASKL DSIDWDTWYH APGMPPVKPH FDTTLADPCY KLAESWTNSA 490 500 510 520 530 540 KNSDDPSKFS SKDIENWSAG QKSLFLDVVY EAVSFPHNYI KRMGDVYSFA ESKNAELSFR 550 560 570 580 590 600 FFKLALKSKY KPLYNTIAER VGSVGRMKFV RPIFRLLNEA DRAFAIETFE KYKHFYHKIC 610 ASQVEKDLGL SE

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA22858.1.
PIR	T40936.
RefSeq	NP_588133.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ModBase	Search...
Protein-protein interaction databases
STRING	O94544.
Genome annotation databases
GeneID	2538917.
KEGG	spo:SPCC1322.05c.
NMPDR	fig|4896.1.peg.471.
Organism-specific databases
GeneDB_Spombe	SPCC1322.05c.
Phylogenomic databases
OMA	FTNRIVE.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000075-MON.
BRENDA	3.3.2.6. 653.
Gene expression databases
ArrayExpress	O94544.
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_SCHPO

Accession

Primary (citable) accession number: O94544

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)