Reviewed, UniProtKB/Swiss-Prot A5DME6 (LKA41_PICGU)

Names and origin

Protein names

Recommended name:
    Leukotriene A-4 hydrolase 1
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase

Gene names

ORF Names:

PGUG_04447

Organism

Pichia guilliermondii (Yeast) (Candida guilliermondii) [Complete proteome]

Taxonomic identifier

4929 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	615 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 – 615	615	Leukotriene A-4 hydrolase 1		PRO_0000324936
Sites
	Active site	291	1	By similarity
	Active site	380	1	Proton donor By similarity
	Metal binding	290	1	Zinc; catalytic By similarity
	Metal binding	294	1	Zinc; catalytic By similarity
	Metal binding	313	1	Zinc; catalytic By similarity
	Site	194	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A5DME6-1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: B41C65A30CC891C7	FASTA	615	70,392
	10 20 30 40 50 60 MLRRPKVSPE LDPSTLSNYG DFIVHKTQLD LAVDFDKNRV SSCVSLNVTN RTNTHQVVLD 70 80 90 100 110 120 SSYLVIHSAS INGISTPFDV AERQTLGSKV TIKIPPEMKI SELTITIESE TTYECTALQF 130 140 150 160 170 180 LPAEATDGGV GPYLFSQCQA IHARSLFPCF DTPAVKCPYE MSVTSPYPSV MSGRPLGVSG 190 200 210 220 230 240 NMYRFSQPVP IPSYLVAVAS GDIKSAPIGP RSSVYCEPLK LEVCQHEFQA DMEHFLQAAE 250 260 270 280 290 300 SLVFKYEWER YDALVLPSSF PYGGMENPNI TFVTPTLISG DRENVDVIAH ELAHSWSGNL 310 320 330 340 350 360 VTNCSWEHFW LNEGWTVYLE RRILGKLHGN ATRDFSAIIG WTDLENSIAA MGPSAERWSM 370 380 390 400 410 420 LVHNLKDGSD PDDAFSTVPY EKGSTLLYHI ETLIGQEKFD KFIPHYFHTF RYKSLDTYQF 430 440 450 460 470 480 IDCLYSFFAD FKSVLDTIDW ESWLYKPGMP PVKPDFDTSM VDQCYQLADK WYHHSLKNKF 490 500 510 520 530 540 HKFSSEDIKS FTANQSVVFL DTLIAFDKLD FKWKHHLDAL NTMASVYQEY SKSTNAEVLF 550 560 570 580 590 600 RWYVLQVTGH NQEYYSRLGE WLGTVGRMKF VRPGYVLLNK VDRSMALHYF EKFHNRYHAI 610 CKSMVRRDWD LIKTK

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 6260 / CBS 566 / IFO 10279 / JCM 1539 / NRRL Y-324.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH408159 Genomic DNA. Translation: EDK40349.2.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.3.2.6. 3704.
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

LKA41_PICGU

Accession

Primary (citable) accession number: A5DME6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	February 10, 2009
Last modified:	September 22, 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)