A6ZS33 (LKHA4_YEAS7) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leukotriene A-4 hydrolase homolog
Short name=LTA-4 hydrolase
EC=3.3.2.6

Alternative name(s):
Leukotriene A(4) hydrolase

Gene names

ORF Names:

SCY_4744

Organism

Saccharomyces cerevisiae (strain YJM789) (Baker's yeast) [Complete proteome]

Taxonomic identifier

307796 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA4 to form LTB4 (in vitro) 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.
Enzyme regulation	Inhibited 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The amiminopeptidase activity is stimulated by LTA4 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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB epoxide hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB leukotriene-A4 hydrolase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 671	671	Leukotriene A-4 hydrolase homolog		PRO_0000324943
Regions
	Region	184 – 186	3	Substrate binding By similarity
	Region	311 – 316	6	Substrate binding By similarity
Sites
	Active site	341	1	Proton acceptor By similarity
	Active site	429	1	Proton donor By similarity
	Metal binding	340	1	Zinc; catalytic By similarity
	Metal binding	344	1	Zinc; catalytic By similarity
	Metal binding	363	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	51	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6ZS33 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 454E40F030BF28FA	FASTA	671	77,353
	10 20 30 40 50 60 MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP SRSPEYDQST 70 80 90 100 110 120 LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK NKSDELHLDT SYLDVQEVHI 130 140 150 160 170 180 DGSKADFQIE QRKEPLGSRL VINNASCNDN FTLNIQFRTT DKCTALQWLN SKQTKGGKPY 190 200 210 220 230 240 VFSQLEAIHA RSLFPCFDTP SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP 250 260 270 280 290 300 IPAYLIGIAS GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT 310 320 330 340 350 360 YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL VTNCSWNHFW 370 380 390 400 410 420 LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS MKDPERFSTL VQNLNDNTDP 430 440 450 460 470 480 DDAFSTVPYE KGFNLLFHLE TILGGKAEFD PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE 490 500 510 520 530 540 KKEILDSVDW ETWLYKPGMP PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI 550 560 570 580 590 600 DIKDFNSNQL VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF 610 620 630 640 650 660 KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF DKFKDTYHPI 670 CKALVKQDLG L

References

[1]

"Genome sequencing and comparative analysis of Saccharomyces cerevisiae strain YJM789." Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X., Jia P., Luedi P., Oefner P.J., David L. , Dietrich F.S., Li Y., Davis R.W., Steinmetz L.M. Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007) [PubMed: 17652520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: YJM789.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFW02000067 Genomic DNA. Translation: EDN62765.1.
3D structure databases
ProteinModelPortal	A6ZS33.
SMR	A6ZS33. Positions 40-671.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR012777. Leukotriene_A4_hydrolase. 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.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
TIGRFAMs	TIGR02411. Leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_YEAS7

Accession

Primary (citable) accession number: A6ZS33

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	September 11, 2007
Last modified:	November 16, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program