Reviewed, UniProtKB/Swiss-Prot A6RCT2 (LKHA4_AJECN)

Names and origin

Protein names

Recommended name:
    Leukotriene A-4 hydrolase
    EC=3.3.2.6
Alternative name(s):
    Leukotriene A(4) hydrolase
      Short name=LTA-4 hydrolase

Gene names

ORF Names:

HCAG_07440

Organism

Ajellomyces capsulata (strain NAm1 / WU24) (Darling's disease fungus) (Histoplasma capsulatum)

Taxonomic identifier

339724 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Ajellomyces

Protein attributes

Sequence length	623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Hydrolyzes an epoxide moiety of LTA4 to form LTB4. The enzyme also has some peptidase activity 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 EDN10979.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Leukotriene biosynthesis
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	leukotriene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	leukotriene-A4 hydrolase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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		PRO_0000324916
Sites
	Active site	307	1	By similarity
	Active site	394	1	Proton donor By similarity
	Metal binding	306	1	Zinc; catalytic By similarity
	Metal binding	310	1	Zinc; catalytic By similarity
	Metal binding	329	1	Zinc; catalytic By similarity
	Site	210	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6RCT2-1 [UniParc]. Last modified March 18, 2008. Version 2. Checksum: 00C7317297839194	FASTA	623	70,379
	10 20 30 40 50 60 MRRCTKNSRS TNPPRDPNTL SNYNAFRTTH TTVNFDILFE KQKLTGNVMH KLISLTNLEA 70 80 90 100 110 120 REVILDSSFL NIHDVKVDGK QSKFELLPRQ EPYGSALKIP LAEGVALSKT LDIDITVETT 130 140 150 160 170 180 EKCTALQWLT PAQTSTQKHP YMFTQCQAIH ARSIFPCQDT PDVKAVIDFN ISSPLPVIAS 190 200 210 220 230 240 GVPVNDVSSS SSKSKNKVYK FHQKVPIPTY LFAMASGEIA EAPIGPRSRV AASPDKLEEC 250 260 270 280 290 300 KWELEADTEK FMQAIDKIIF PYIWGEYNVL ILPPSFPYGG MENPIFTFAT PSVISKDRQN 310 320 330 340 350 360 VDVIAHELAH SWSGNLVTNA SWEHFWLNEG WTTYLERRIL AAVHGEPYRH FSAIIGWKAL 370 380 390 400 410 420 TESVERYGKD HEFTKLVVDL KGKDPDDAFS SVPYEKGFNF LFYLENLIGK DKFDKFIPHY 430 440 450 460 470 480 FTKYKEASLD SYEFKSSILS FFSSDSEAHA LLTSFDWDKW FYSPGLPPKP DFDTSLVDIV 490 500 510 520 530 540 YALAQKWRTA SESGFSPSAV DVNGLVANQL VVFLEQVLVF EKPLSAEQSK LMGDKYGLAK 550 560 570 580 590 600 SENAEVLNMY FQVGLKAGDK SVIEPTAAFL SSIGRMKYVR PLYRALDKLD RNIAIEVFEK 610 620 NKSFYHPICR GLVQKDLFGN KGS

References

[1]

"Comparative genomic analyses of the human fungal pathogens Coccidioides and their relatives." Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N. , Orbach M.J., Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W. Genome Res. 19:1722-1731(2009) [PubMed: 19717792] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CH476662 Genomic DNA. Translation: EDN10979.1. Sequence problems.
RefSeq	XP_001538018.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5444402.
Family and domain databases
InterPro	IPR012777. Leuk_A4_hydro_aminopept. IPR006025. Pept_M_Zn_BS. IPR015211. Peptidase_M1_C. IPR014782. Peptidase_M1_N. [Graphical view]
Pfam	PF09127. Leuk-A4-hydro_C. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
TIGRFAMs	TIGR02411. leuko_A4_hydro. 1 hit.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LKHA4_AJECN

Accession

Primary (citable) accession number: A6RCT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 18, 2008
Last modified:	November 3, 2009
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)