Reviewed, UniProtKB/Swiss-Prot Q6FTM0 (LKHA4_CANGA)

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

Ordered Locus Names:

CAGL0G01430g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	652 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 – 652	652	Leukotriene A-4 hydrolase		PRO_0000324925
Sites
	Active site	323	1	By similarity
	Active site	411	1	Proton donor By similarity
	Metal binding	322	1	Zinc; catalytic By similarity
	Metal binding	326	1	Zinc; catalytic By similarity
	Metal binding	345	1	Zinc; catalytic By similarity
	Site	226	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FTM0-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 4AD4BB847DEF880B	FASTA	652	74,823
	10 20 30 40 50 60 MINRLIQRIV PFSRPLSTVK KTMLTPFLES KRPQQSPEYD YSTLSNYKSF QIKHTTLNFL 70 80 90 100 110 120 LSFEKSTVSG DVVFDLTTLK EAVKHIDLDT SYLDVNEVLV DDKPVEFKIE ERKQPLGSKL 130 140 150 160 170 180 VIAAELEAER QFKLRVKFST TKDCTALQWL TPQQTSGDKP YMFSQLEAIH ARALFPCFDT 190 200 210 220 230 240 PSYKSTFTAN IESTLPVVFS GIATGSTPNG ESTVYHFKQD IPIPAYLVGI ASGDLVSASI 250 260 270 280 290 300 GPRSKVYTEP HRLDDCVWEF SNDVEKFIKT AENLIFDYEW GTYDILVNVD SYPYGGMESP 310 320 330 340 350 360 NMTFATPTLI AHDKTNIDVI AHELAHSWSG NLVTNCSWNH FWLNEGWTVY IERRIVGALH 370 380 390 400 410 420 GEPTRHFSAL IGWSDLENSI NSMRNPEKFS TLVQNLNDGT DPDDAFSTVP YEKGFNLLFH 430 440 450 460 470 480 LETVLGGPQE FDPFIRHYFK KFARQSLDTF QFLDTLFEFF ENKREILENV DWETWLFKPG 490 500 510 520 530 540 MPPKPQFITT MADNVFSLVN KWIVKAQELK TTEEFSKEFS ESDLSEFNSN QVVLFLEELV 550 560 570 580 590 600 AQNCVPVESK IEWSKYSVAS ESLLSIYKKQ VTESQNAEVV FKNYKFQTTA RIQPSYQQLA 610 620 630 640 650 NWLGTVGRMK FVRPGYRLLN AVDRDLAIAT FEKLKDTYHP ICKQLVKQDL EL

References

[1]

"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR380953 Genomic DNA. Translation: CAG59351.1.
RefSeq	XP_446424.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FTM0.
Genome annotation databases
GeneID	2888012.
GenomeReviews	Gene locus CAGL0G01430g in contig CR380953_GR.
KEGG	cgr:CAGL0G01430g.
Phylogenomic databases
HOGENOM	Q6FTM0.
OMA	SERCAVW.
Enzyme and pathway databases
BRENDA	3.3.2.6. 189220.
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_CANGA

Accession

Primary (citable) accession number: Q6FTM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)