Reviewed, UniProtKB/Swiss-Prot A5DSS4 (LKHA4_LODEL)

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:

LELG_00410

Organism

Lodderomyces elongisporus (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

36914 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Lodderomyces

Protein attributes

Sequence length	648 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.
Sequence caution	The sequence EDK42232.1 differs from that shown. Reason: Erroneous gene model prediction.

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 – 648	648	Leukotriene A-4 hydrolase		PRO_0000324931
Sites
	Active site	299	1	By similarity
	Active site	408	1	Proton donor By similarity
	Metal binding	298	1	Zinc; catalytic By similarity
	Metal binding	302	1	Zinc; catalytic By similarity
	Metal binding	321	1	Zinc; catalytic By similarity
	Site	202	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DSS4-1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: C3C91E3173D14493	FASTA	648	75,111
	10 20 30 40 50 60 MEELKAYRPK TSPELDPSTL SNYTCFTVKL TTLHFDIDFE KKIVSGKVKY DLLNKSETDH 70 80 90 100 110 120 VDLDTSYLDI TKVSIQNESC DNQYKLHSRK EPLGSKLHIL IPASTPKNFQ LEIEFSTTSK 130 140 150 160 170 180 CTALQFLDKE ATDGKNHPYL FCQCQAIHAR SLFPSFDTPG IKSPYKFSAK SPLKTLLSGL 190 200 210 220 230 240 LIKEDNENNT VYFEQPVPIP SYLVSIALGD IARTSIGPRS DVMTEPVNLA KCKWEFERDM 250 260 270 280 290 300 ENFIQVAEKL IFEYEWQKFD SLVLPASFPY GGMEIPNLCQ LTPTLICGDR SLVNVVAHEL 310 320 330 340 350 360 AHSWSGNLVT NCSWEHFWLN EGWTVYLERR ILEALAVIEA KQQGKGDKEA HYYGEQVRQF 370 380 390 400 410 420 NAIIGWTDLE NDLKSMGDNV DKYSILVQDL KGKKNPDDPD DAFSTVPYEK GFNLLYLIEK 430 440 450 460 470 480 IVGKEKFDLF IPAYFREFRF KSLDTFQFID YLFDFFKEDA VKLDQIEWKK WLYEPGMPPI 490 500 510 520 530 540 DPKFDTTLAQ ACYDLAKKCY QYALSEDDEN EFTQFKLVAN EINDFSPSQN IVFLDTLIAY 550 560 570 580 590 600 EKVAGFSWKQ HKKTLNRMAT LYHDQYTETL NAEIKFRWFY LQATGEVLDF EVAMGEFLGT 610 620 630 640 IGRMKFVRPG YALLNKVNRE LAVRYFQRFE NRYHPICKAM VRKDLQLD

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH981524 Genomic DNA. Translation: EDK42232.1. Sequence problems.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.3.2.6. 3705.
Family and domain databases
InterPro	IPR012777. Leuk_A4_hydro_aminopept. IPR006025. Pept_M_Zn_BS. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 2 hits. [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_LODEL

Accession

Primary (citable) accession number: A5DSS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	October 13, 2009
This is version 21 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)