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Q5B0W8 (LKHA4_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Leukotriene A-4 hydrolase homolog
PRO_0000324929

Regions

Region140 – 1423Substrate binding By similarity
Region272 – 2776Substrate binding By similarity

Sites

Active site3021Proton acceptor By similarity
Active site3891Proton donor By similarity
Metal binding3011Zinc; catalytic By similarity
Metal binding3051Zinc; catalytic By similarity
Metal binding3241Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5B0W8 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: AEEB8A7BB540D9C9

FASTA61870,100
        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

« Hide

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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.
RefSeqXP_663416.1. XM_658324.1.

3D structure databases

HSSPHSSP built from PDB template 1HS6 based on UniProtKB P09960.
ProteinModelPortalQ5B0W8.
ModBaseSearch...

Protein-protein interaction databases

STRING162425.CADANIAP00007234.

Protein family/group databases

MEROPSM01.034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00007234; CADANIAP00007234; CADANIAG00007234.
GeneID2871086.
KEGGani:AN5812.2.

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000293296.
KOK01254.
OMAFTNRIVE.
OrthoDBEOG49KJZX.

Enzyme and pathway databases

UniPathwayUPA00878.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
SUPFAMSSF48371. ARM-type_fold. 1 hit.
TIGRFAMsTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLKHA4_EMENI
AccessionPrimary (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: May 1, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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