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Protein

Leukotriene A-4 hydrolase homolog

Gene

LAP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).5 Publications

Catalytic activityi

(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.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited 3-(4-benzyloxyphenyl)-2-(R)-amino-1-propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The aminopeptidase activity is stimulated by LTA4.2 Publications

Kineticsi

  1. KM=1.5 mM for Leu-p-nitroanilide3 Publications
  2. KM=1.8 mM for Met-p-nitroanilide3 Publications
  3. KM=2.0 mM for Ala-p-nitroanilide3 Publications
  1. Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate3 Publications
  2. Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate3 Publications
  3. Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate3 Publications

pH dependencei

Optimum pH is about 7.3.3 Publications

Pathwayi: leukotriene B4 biosynthesis

This protein is involved in the pathway leukotriene B4 biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway leukotriene B4 biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi340Zinc; catalytic1
Active sitei341Proton acceptor1
Metal bindingi344Zinc; catalytic1
Metal bindingi363Zinc; catalytic1
Active sitei429Proton donor1

GO - Molecular functioni

  • aminopeptidase activity Source: SGD
  • epoxide hydrolase activity Source: SGD
  • leukotriene-A4 hydrolase activity Source: UniProtKB-EC
  • metalloaminopeptidase activity Source: GO_Central
  • peptide binding Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular lipid metabolic process Source: SGD
  • peptide catabolic process Source: UniProtKB
  • protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Leukotriene biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YNL045W-MONOMER.
ReactomeiR-SCE-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-SCE-6798695. Neutrophil degranulation.
SABIO-RKQ10740.
UniPathwayiUPA00878.

Protein family/group databases

MEROPSiM01.034.

Names & Taxonomyi

Protein namesi
Recommended name:
Leukotriene A-4 hydrolase homolog (EC:3.3.2.6)
Short name:
LTA-4 hydrolase
Alternative name(s):
Leucine aminopeptidase 2
Leukotriene A(4) hydrolase
Gene namesi
Name:LAP2
Ordered Locus Names:YNL045W
ORF Names:N2535
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL045W.
SGDiS000004990. LAP2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi244Y → F: Reduces strongly the substrate affinity. 1 Publication1
Mutagenesisi316E → A, Q or D: Abolishes the aminopeptidase activity. 1 Publication1
Mutagenesisi340H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication1
Mutagenesisi341E → Q: Abolishes aminopeptidase activity. No effect on the epoxide hydrolase activity. 1 Publication1
Mutagenesisi344H → Q: Abolishes the epoxide hydrolase and aminopeptidase activities. 1 Publication1
Mutagenesisi363E → Q: Abolishes the epoxide hydrolase activity. 1 Publication1
Mutagenesisi424F → Y: Increases the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication1
Mutagenesisi429Y → F: Abolishes the aminopeptidase activity and decreases the epoxide hydrolase activity. 1 Publication1
Mutagenesisi627R → K or A: Abolishes the aminopeptidase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000951291 – 671Leukotriene A-4 hydrolase homologAdd BLAST671

Proteomic databases

MaxQBiQ10740.
PRIDEiQ10740.

PTM databases

iPTMnetiQ10740.

Interactioni

Protein-protein interaction databases

BioGridi35779. 27 interactors.
DIPiDIP-4371N.
IntActiQ10740. 6 interactors.
MINTiMINT-542331.

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 48Combined sources6
Beta strandi51 – 54Combined sources4
Helixi64 – 66Combined sources3
Beta strandi67 – 79Combined sources13
Turni80 – 83Combined sources4
Beta strandi84 – 95Combined sources12
Beta strandi99 – 101Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi111 – 120Combined sources10
Beta strandi127 – 129Combined sources3
Turni134 – 136Combined sources3
Beta strandi140 – 143Combined sources4
Beta strandi147 – 159Combined sources13
Beta strandi164 – 169Combined sources6
Turni171 – 173Combined sources3
Beta strandi175 – 178Combined sources4
Beta strandi180 – 183Combined sources4
Turni186 – 189Combined sources4
Helixi190 – 192Combined sources3
Beta strandi204 – 211Combined sources8
Beta strandi216 – 222Combined sources7
Beta strandi232 – 241Combined sources10
Helixi243 – 245Combined sources3
Beta strandi248 – 252Combined sources5
Beta strandi254 – 259Combined sources6
Beta strandi262 – 266Combined sources5
Helixi268 – 278Combined sources11
Turni279 – 281Combined sources3
Helixi282 – 292Combined sources11
Beta strandi297 – 299Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi312 – 315Combined sources4
Beta strandi321 – 323Combined sources3
Helixi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Helixi336 – 344Combined sources9
Turni348 – 350Combined sources3
Beta strandi351 – 355Combined sources5
Helixi356 – 359Combined sources4
Helixi360 – 378Combined sources19
Helixi380 – 399Combined sources20
Beta strandi401 – 403Combined sources3
Helixi404 – 407Combined sources4
Beta strandi409 – 411Combined sources3
Beta strandi416 – 418Combined sources3
Helixi420 – 423Combined sources4
Helixi427 – 442Combined sources16
Helixi446 – 459Combined sources14
Turni460 – 462Combined sources3
Beta strandi463 – 465Combined sources3
Helixi467 – 477Combined sources11
Helixi479 – 481Combined sources3
Helixi482 – 486Combined sources5
Helixi490 – 495Combined sources6
Helixi508 – 523Combined sources16
Turni524 – 526Combined sources3
Helixi530 – 536Combined sources7
Helixi539 – 542Combined sources4
Helixi547 – 558Combined sources12
Beta strandi562 – 565Combined sources4
Helixi572 – 574Combined sources3
Helixi576 – 585Combined sources10
Helixi587 – 591Combined sources5
Helixi596 – 608Combined sources13
Helixi612 – 614Combined sources3
Helixi615 – 621Combined sources7
Turni622 – 624Combined sources3
Helixi628 – 639Combined sources12
Helixi643 – 653Combined sources11
Helixi654 – 656Combined sources3
Helixi659 – 668Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XPYX-ray2.73A40-671[»]
2XPZX-ray2.30A40-671[»]
2XQ0X-ray1.96A40-669[»]
ProteinModelPortaliQ10740.
SMRiQ10740.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10740.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 186Substrate binding3
Regioni311 – 316Substrate binding6

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
InParanoidiQ10740.
KOiK01254.
OMAiSNASWEH.
OrthoDBiEOG092C0ZZE.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP
60 70 80 90 100
SRSPEYDQST LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK
110 120 130 140 150
NKSDELHLDT SYLDVQEVHI DGSKADFQIE QRKEPLGSRL VINNASCNDN
160 170 180 190 200
FTLNIQFRTT DKCTALQWLN SKQTKGGKPY VFSQLEAIHA RSLFPCFDTP
210 220 230 240 250
SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP IPAYLIGIAS
260 270 280 290 300
GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT
310 320 330 340 350
YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL
360 370 380 390 400
VTNCSWNHFW LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS
410 420 430 440 450
MKDPERFSTL VQNLNDNTDP DDAFSTVPYE KGFNLLFHLE TILGGKAEFD
460 470 480 490 500
PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE KKEILDSVDW ETWLYKPGMP
510 520 530 540 550
PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI DIKDFNSNQL
560 570 580 590 600
VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF
610 620 630 640 650
KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF
660 670
DKFKDTYHPI CKALVKQDLG L
Length:671
Mass (Da):77,353
Last modified:October 1, 1996 - v1
Checksum:i454E40F030BF28FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94547 Genomic DNA. Translation: CAA64237.1.
Z71321 Genomic DNA. Translation: CAA95912.1.
BK006947 Genomic DNA. Translation: DAA10500.1.
PIRiS61099.
RefSeqiNP_014353.1. NM_001182884.1.

Genome annotation databases

EnsemblFungiiYNL045W; YNL045W; YNL045W.
GeneIDi855682.
KEGGisce:YNL045W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94547 Genomic DNA. Translation: CAA64237.1.
Z71321 Genomic DNA. Translation: CAA95912.1.
BK006947 Genomic DNA. Translation: DAA10500.1.
PIRiS61099.
RefSeqiNP_014353.1. NM_001182884.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XPYX-ray2.73A40-671[»]
2XPZX-ray2.30A40-671[»]
2XQ0X-ray1.96A40-669[»]
ProteinModelPortaliQ10740.
SMRiQ10740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35779. 27 interactors.
DIPiDIP-4371N.
IntActiQ10740. 6 interactors.
MINTiMINT-542331.

Protein family/group databases

MEROPSiM01.034.

PTM databases

iPTMnetiQ10740.

Proteomic databases

MaxQBiQ10740.
PRIDEiQ10740.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL045W; YNL045W; YNL045W.
GeneIDi855682.
KEGGisce:YNL045W.

Organism-specific databases

EuPathDBiFungiDB:YNL045W.
SGDiS000004990. LAP2.

Phylogenomic databases

GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
InParanoidiQ10740.
KOiK01254.
OMAiSNASWEH.
OrthoDBiEOG092C0ZZE.

Enzyme and pathway databases

UniPathwayiUPA00878.
BioCyciYEAST:YNL045W-MONOMER.
ReactomeiR-SCE-2142691. Synthesis of Leukotrienes (LT) and Eoxins (EX).
R-SCE-6798695. Neutrophil degranulation.
SABIO-RKQ10740.

Miscellaneous databases

EvolutionaryTraceiQ10740.
PROiQ10740.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR012777. Leukotriene_A4_hydrolase.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
TIGRFAMsiTIGR02411. leuko_A4_hydro. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLKHA4_YEAST
AccessioniPrimary (citable) accession number: Q10740
Secondary accession number(s): D6W1D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5590 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  6. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.