Q0U653 (LKHA4_PHANO) 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:

SNOG_12761

Organism

Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Septoria nodorum)

Taxonomic identifier

321614 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Phaeosphaeriaceae › Phaeosphaeria

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 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 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_0000324935
Regions
	Region	136 – 138	3	Substrate binding By similarity
	Region	273 – 278	6	Substrate binding By similarity
Sites
	Active site	303	1	Proton acceptor By similarity
	Active site	390	1	Proton donor By similarity
	Metal binding	302	1	Zinc; catalytic By similarity
	Metal binding	306	1	Zinc; catalytic By similarity
	Metal binding	325	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0U653 [UniParc]. Last modified February 5, 2008. Version 2. Checksum: 0012E38B949B27F8	FASTA	623	70,890
	10 20 30 40 50 60 METRTPRDPN TLSNYHNYVT RHTSLDFEIE FERKRLVGSV VLRMESLTDA EVDVVLDSSF 70 80 90 100 110 120 LDVSAIKVDR QSAEFSIGER IEPYGSPLTI KLPAAVPKGK TVEIELTVAT TEKCTALQWM 130 140 150 160 170 180 EPAQTSNKKH PYMFSQCQAN HARSVFPCQD TPDVKSTFSF ALRSPLPVLA SGLPTGASKY 190 200 210 220 230 240 QPAKKDGASG TLKYTFEQPV AITSYLMAVA SGDLACASIG PRSTVWSGPE ELLECQQELE 250 260 270 280 290 300 GEIEPFMKAI ESIVKPTYQW TQYNVLILPP SFPYGGMENP VWTYATPSII SGDKQNIDVI 310 320 330 340 350 360 AHELSHSWSG NLVSAASWEH FWLNEGWTTY LERRIQGVLH GESHRHFSAI IGWKALEESI 370 380 390 400 410 420 ERYGADHDFT KLVIDLKGKD PDDAFSSIPY EKGFHALYQF ELLLGKDKWD NFIPHYFETF 430 440 450 460 470 480 KFKSIDSYDF KACLIDFFAK DTEANKKLAE FDWDKLFYAP GYPPKPDFDQ TMVKSCYKLA 490 500 510 520 530 540 DKWQYLITNN SSSDFKPHHS DVADWVSNQS VVFLEKVQSF AEKFSAEQIH LLGHTYGYDK 550 560 570 580 590 600 TQNIEVLSRY LSAGLMAKAP ETYQPSAELL GRIGRMKFVR PMYRLLEKAD RKLAVETFEK 610 620 NKDFYHPICR SMVEKDLFGD EKK

References

[1]

"Dothideomycete-plant interactions illuminated by genome sequencing and EST analysis of the wheat pathogen Stagonospora nodorum." Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L., Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E., Torriani S.F.F., McDonald B.A., Oliver R.P. Plant Cell 19:3347-3368(2007) [PubMed: 18024570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SN15 / ATCC MYA-4574 / FGSC 10173.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH445347 Genomic DNA. Translation: EAT80059.2.
RefSeq	XP_001802980.1. XM_001802928.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SNOT_12761; SNOT_12761; SNOG_12761.
GeneID	5979891.
KEGG	pno:SNOG_12761.
Phylogenomic databases
OrthoDB	EOG49KJZX.
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_PHANO

Accession

Primary (citable) accession number: Q0U653

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	February 5, 2008
Last modified:	December 14, 2011
This is version 43 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program