Q4X265 (LKHA4_ASPFU) 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:

AFUA_2G07520

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	614 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 – 614	614	Leukotriene A-4 hydrolase homolog		PRO_0000324919
Regions
	Region	139 – 141	3	Substrate binding By similarity
	Region	271 – 276	6	Substrate binding By similarity
Sites
	Active site	301	1	Proton acceptor By similarity
	Active site	385	1	Proton donor By similarity
	Metal binding	300	1	Zinc; catalytic By similarity
	Metal binding	304	1	Zinc; catalytic By similarity
	Metal binding	323	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4X265 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: 9380C62C0E262319	FASTA	614	69,722
	10 20 30 40 50 60 MTTVVNLPRD PNTLSNYNNW VSTHITANFD ILFDQRKLAG NVIHRFRSTT DGESNHIILD 70 80 90 100 110 120 TNHLDIGSVK VNGQPSEWEY LPRLEPYGTP LKIKLDQGVK LNETIEVDIS VQTTEKCTAL 130 140 150 160 170 180 QWLTPAQTSN KKHPYMFSQC QAIHARSIFP CQDTPDVKCT LDFNITSPLP VIASGLPVRG 190 200 210 220 230 240 SSEAPKSDGK TLYKFHQKVP IPSYLFALAS GDISEAPIGP RSVVATSPDK LGECQWELEA 250 260 270 280 290 300 DTEKFINAIE KIVYPYVWGE YNVLILPPSF PYGGMENPIF TFATPSIISK DRENIDVIAH 310 320 330 340 350 360 ELAHSWSGNL VTNASWEHFW LNEGWTTYLE RRLRHGEPYR HFSAIIGWKA LTDSVEHFGP 370 380 390 400 410 420 EHDFTKLITN LKGMDPDDAF SSIPYEKGFN FLFHLENLVG KSKFDRFIPH YFNKYKGKSL 430 440 450 460 470 480 DSYEFKSTIL DFFKDDSDAS TALNELDWDS WFYAPGLPPK PDFDTSLVDV VYDLAKKWLS 490 500 510 520 530 540 LPKSSFKPQP EDIRGLTANQ VVVFLEQILV SERQLTPELS KLMGEIYGLA ASQNIEVANL 550 560 570 580 590 600 YFQVGLQAGD ASVVEPTADL LGKIGRMKFV RPLYRKLAKF DRKRALDTFE KHKGFYHPIC 610 RAMVEKDLFG KKDE

References

[1]

"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000001 Genomic DNA. Translation: EAL93050.1.
RefSeq	XP_755088.1. XM_749995.1.
3D structure databases
HSSP	HSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortal	Q4X265.
ModBase	Search...
Protein-protein interaction databases
STRING	Q4X265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00004451; CADAFUAP00004451; CADAFUAG00004451.
GeneID	3513337.
KEGG	afm:AFUA_2G07520.
Phylogenomic databases
eggNOG	fuNOG04031.
GeneTree	EFGT00050000003006.
HOGENOM	HBG444814.
OMA	QEVKYTL.
OrthoDB	EOG49KJZX.
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_ASPFU

Accession

Primary (citable) accession number: Q4X265

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	July 5, 2005
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program