Q75B10 (LKHA4_ASHGO) 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

Ordered Locus Names:	ADL233W
ORF Names:	AGOS_ADL233W

Organism

Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

284811 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	623 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.
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
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 – 623	623	Leukotriene A-4 hydrolase homolog		PRO_0000324917
Regions
	Region	140 – 142	3	Substrate binding By similarity
	Region	266 – 271	6	Substrate binding By similarity
Sites
	Active site	296	1	Proton acceptor By similarity
	Active site	382	1	Proton donor By similarity
	Metal binding	295	1	Zinc; catalytic By similarity
	Metal binding	299	1	Zinc; catalytic By similarity
	Metal binding	318	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q75B10 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D053DEFDF36DAB39	FASTA	623	69,156
	10 20 30 40 50 60 MKLPAVLEER RAAATDRSTL SNYEDFAVRH TNLELEVAFD ERQIRAEVCY DLEQTGKGVA 70 80 90 100 110 120 EVHLDTSYVQ LECILVDGKR VPWELRERQE PLGSQLVITP EGGLPARFQL TCRSVTTARS 130 140 150 160 170 180 TAVQWLGGAQ TAGKPYVYTQ LESVHARSLV PCFDTPACKS PFTVRVRSPL RAVVAGQEQP 190 200 210 220 230 240 GSGKDGVYVF EQPVPIPIYL LGLAAGDIAC APLGPRSNVY CEPALLEAAA GEFGGEIERF 250 260 270 280 290 300 LDAAEELLPR YIWGNYNLLV CPSSYPYGGM EVAGTSFISP SVIAYDRSNN DLIVHEMAHS 310 320 330 340 350 360 WSGNLITNAN WGHFWLNEGW TVYLERRITG ALHGEDTRQF SSLLGMAELE VAIRASNGAS 370 380 390 400 410 420 FALVEDVSES VNPDNVVSLA AYEKGSALLL HLERELGGTA AFDPFIKHYF GKFGGQSLTT 430 440 450 460 470 480 WQFLDILFDY FADKREKLER IDWKTWLLAP GMPPKLTYST SLADDVYDLA EQWLEKAVQL 490 500 510 520 530 540 RLPEEFAAEF SGSVLAAFTT AQQILFLNTI IQGGVSPDNT FDWTQHPVAA AALLSVYADT 550 560 570 580 590 600 LGKSRNQEII YRRYNFQLTA GMEDAYPEIT TWLGSTGRMK HVRPIYRRLA SIDKALAAST 610 620 FQEHREKYHP ICRAAIQADL GLS

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016817 Genomic DNA. Translation: AAS51687.1.
RefSeq	NP_983863.2. NM_209216.2.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q75B10.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75B10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4619998.
GenomeReviews	Gene locus ADL233W in contig AE016817_GR.
KEGG	ago:AGOS_ADL233W.
NMPDR	fig|33169.1.peg.1508.
Organism-specific databases
AGD	ADL233W.
Phylogenomic databases
eggNOG	fuNOG04031.
HOGENOM	HBG444814.
OMA	FTNRIVE.
OrthoDB	EOG49KJZX.
PhylomeDB	Q75B10.
Family and domain databases
InterPro	IPR016024. ARM-type_fold. IPR001930. Peptidase_M1. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
KO	K01254.
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.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_ASHGO

Accession

Primary (citable) accession number: Q75B10

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program