Q5B0W8 (LKHA4_EMENI) 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:

AN5812

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	618 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.
Sequence caution	The sequence EAA58321.1 differs from that shown. Reason: Erroneous initiation.

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 – 618	618	Leukotriene A-4 hydrolase homolog		PRO_0000324929
Regions
	Region	140 – 142	3	Substrate binding By similarity
	Region	272 – 277	6	Substrate binding By similarity
Sites
	Active site	302	1	Proton acceptor By similarity
	Active site	389	1	Proton donor By similarity
	Metal binding	301	1	Zinc; catalytic By similarity
	Metal binding	305	1	Zinc; catalytic By similarity
	Metal binding	324	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5B0W8 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: AEEB8A7BB540D9C9	FASTA	618	70,100
	10 20 30 40 50 60 MATLMNPVRD PNTLSNYNNW LCTHTTANFE IFFEEKKLVG NVVHKLRSIT NAETDEIILD 70 80 90 100 110 120 SHHVDIRNVQ VAGLPVKAWE LLPPLGPYGT ALKIKLENPV GLNEIIDVDI AVQTTKECTA 130 140 150 160 170 180 LQWLTPAQTS NKKHPYMFSQ CQAIHARSIF PCQDTPDVKC TFDFNITSPL PVIASGLPVR 190 200 210 220 230 240 STSTVPQSGV KTLHRFHQKV PIPSYLFALA SGDIAEAAIG PRSVVATSPD KLEECKWELE 250 260 270 280 290 300 ADTERFIKTI EEIIYPYAWG EYNVLILPPS FPYGGMENPV FTFATPSIIS KDRENVDVIA 310 320 330 340 350 360 HELAHSWSGN LVTSASWEHF WLNEGWTVYL ERRILASLHG EKYRHFSAII GWKALRDSVE 370 380 390 400 410 420 HYSHDHEFTK LVPNLKGEDP DDAFSTIPYE KGFNFLFHLE NLVGKEKFDR FIPHYFTTFK 430 440 450 460 470 480 GKSLDSYDFK ATLLDFFKSD AEASRLLQEL DWDSWFYKPG LPPKPEFDTS LADVVYELAG 490 500 510 520 530 540 KWRSLPESPF QPQPSDIQGL TANQIVVFLE QILLFERPLT AELSKLMGEV YGLTGSENIE 550 560 570 580 590 600 VANLYLQVGL KAADKSVIGP TTDLLGRIGR MKFVRPLYRA LQKVDRQVAI DTFEKHKDFY 610 HPICRGMVEK DLFGKKDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AACD01000100 Genomic DNA. Translation: EAA58321.1. Different initiation. BN001301 Genomic DNA. Translation: CBF70797.1.
RefSeq	XP_663416.1. XM_658324.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q5B0W8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5B0W8.
Protein family/group databases
MEROPS	M01.034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00007234; CADANIAP00007234; CADANIAG00007234.
GeneID	2871086.
KEGG	ani:AN5812.2.
Phylogenomic databases
OMA	FTNRIVE.
OrthoDB	EOG49KJZX.
PhylomeDB	Q5B0W8.
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]
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.
TIGRFAMs	TIGR02411. Leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_EMENI

Accession

Primary (citable) accession number: Q5B0W8
Secondary accession number(s): C8V091

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	January 25, 2012
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program