P52922 (LKHA4_DICDI) 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

Name:	lkhA
ORF Names:	DDB_G0269148

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	606 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference 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
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 – 606	606	Leukotriene A-4 hydrolase homolog		PRO_0000095127
Regions
	Region	132 – 134	3	Substrate binding By similarity
	Region	261 – 266	6	Substrate binding By similarity
Sites
	Active site	291	1	Proton acceptor 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
Experimental info
	Sequence conflict	291 – 292	2	EI → HE in AAA70101. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P52922 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: C851065439B1C115	FASTA	606	68,469
	10 20 30 40 50 60 MDPSSLSNPQ ECKVTSLNLV LSVNFEKSQL QGYVEVASQI VKEGTESLIL DTNQLEISHC 70 80 90 100 110 120 NDVTSNPINF KLSEEHKVFG KALIISIPEG LRSVGKEFIV RVYYNTTVDS NALQWLTKDQ 130 140 150 160 170 180 TAGKLHPYLF SQCQAIHARS LVPCQDSPSN KVKYQAEITV PKPLTALMSA LSTGKTESTD 190 200 210 220 230 240 SSVFTFTQEI PIPTYLIAIV VGDLESRVIG PRSKVWSEPS MVAAAEYEFA NTEKFIAVGE 250 260 270 280 290 300 DLLTPYVWGR YDILLLPPSF PYGGMENPLL TFVTPTLLAG DRSLEGVVAH EIAHSWCGNL 310 320 330 340 350 360 VTNKYWSEFF LNEGFTVFVE RKILGRLYGE EMFDFEAMNG LKHLHDDVDL FTHKHQEELT 370 380 390 400 410 420 ALIPNLNGID PDDAFSSVPY EKGFNLLCYL QSLVGVADFE AWLKSYISKF SYQSIVATQM 430 440 450 460 470 480 KDYFIEYFTE KGKSEQISVV NWNDWFNKPG MPIEQVVFVS PAAKVAKDLA EITWIKDQGV 490 500 510 520 530 540 NATKDDIKSF KTQQIILFLD TLIHSTSEKP LSVDVLEKMD SLYGFTDVVN SEYKFRWQTL 550 560 570 580 590 600 CLHSGLKRIE PKVVEFLISQ GRMKFVRPLY RELNKVNPEL AKSTFNKYKS QYHIIASKMV AKDLGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Primary sequence and developmental regulation of Dictyostelium discoideum cDNA encoding homolog of the human leukotriene A4 hydrolase." Jho E., Kopachik W. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 291-606. Strain: AX3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000005 Genomic DNA. Translation: EAL71924.1. U27538 mRNA. Translation: AAA70101.1.
RefSeq	XP_646766.1. XM_641674.1.
3D structure databases
ProteinModelPortal	P52922.
ModBase	Search...
Protein-protein interaction databases
STRING	P52922.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0191291; DDB0191291; DDB_G0269148.
GeneID	8617739.
GenomeReviews	Gene locus lkhA in contig CM000150_GR.
KEGG	ddi:DDB_G0269148.
Organism-specific databases
dictyBase	DDB_G0269148. lkhA.
Phylogenomic databases
eggNOG	KOG1047.
GeneTree	EPrGT00050000002222.
HOGENOM	HBG444814.
OMA	SNLYTKI.
PhylomeDB	P52922.
ProtClustDB	CLSZ2431464.
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_DICDI

Accession

Primary (citable) accession number: P52922
Secondary accession number(s): Q55BR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	December 4, 2007
Last modified:	November 16, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)