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Q6TUJ5

- Q6TUJ5_LEIME

UniProt

Q6TUJ5 - Q6TUJ5_LEIME

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Protein

Arginase

Gene

ARG

Organism
Leishmania mexicana
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Note: Binds 2 manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Manganese 1; via pros nitrogenImported
Metal bindingi137 – 1371Manganese 1Imported
Metal bindingi137 – 1371Manganese 2Imported
Metal bindingi139 – 1391Manganese 2; via pros nitrogenImported
Metal bindingi141 – 1411Manganese 1Imported
Metal bindingi243 – 2431Manganese 1Imported
Metal bindingi243 – 2431Manganese 2Imported
Metal bindingi245 – 2451Manganese 2Imported

GO - Molecular functioni

  1. arginase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Arginine metabolismUniRule annotation

Keywords - Ligandi

ManganeseUniRule annotationImported, Metal-bindingUniRule annotationImported

Names & Taxonomyi

Protein namesi
Recommended name:
ArginaseUniRule annotation (EC:3.5.3.1UniRule annotation)
Gene namesi
Name:ARGImported
OrganismiLeishmania mexicanaImported
Taxonomic identifieri5665 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ITYX-ray1.80A13-329[»]
4IU0X-ray1.77A13-329[»]
4IU1X-ray1.95A13-329[»]
4IU4X-ray1.80A13-329[»]
4IU5X-ray1.95A13-329[»]
ProteinModelPortaliQ6TUJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family.UniRule annotation

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6TUJ5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEHVQQYKFY KEKKMSIVLA PFSGGQPHSG VELGPDYLLK QGLQQDMEKL
60 70 80 90 100
GWDTRLERVF DGKVVEARKA SDNGDRIGRV KRPRLTAECT EKIYKCVRRV
110 120 130 140 150
AEQGRFPLTI GGDHSIALGT VAGVLSVHPD AGVIWVDAHA DINTMSGTVS
160 170 180 190 200
GNLHGCPLSI LLGLDRENIP ECFSWVPQVL KPNKIAYIGL RAVDDEEKKI
210 220 230 240 250
LHDLNIAAFS MHHVDRYGID KVVSMAIEAV SPKGTEPVMV SYDVDTIDPL
260 270 280 290 300
YVPATGTPVR GGLSFREALF LCERIAECGR LVALDVVECN PLLAATESHV
310 320
NDTISVGCAI ARCMMGETLL YTPHTSSKL
Length:329
Mass (Da):36,082
Last modified:July 5, 2004 - v1
Checksum:i98A2BCA12455AF0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY386701 Genomic DNA. Translation: AAR06176.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY386701 Genomic DNA. Translation: AAR06176.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ITY X-ray 1.80 A 13-329 [» ]
4IU0 X-ray 1.77 A 13-329 [» ]
4IU1 X-ray 1.95 A 13-329 [» ]
4IU4 X-ray 1.80 A 13-329 [» ]
4IU5 X-ray 1.95 A 13-329 [» ]
ProteinModelPortali Q6TUJ5.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Arginase plays a pivotal role in polyamine precursor metabolism in Leishmania. Characterization of gene deletion mutants."
    Roberts S.C., Tancer M.J., Polinsky M.R., Gibson K.M., Heby O., Ullman B.
    J. Biol. Chem. 279:23668-23678(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Crystal structure of arginase from Leishmania mexicana and implications for the inhibition of polyamine biosynthesis in parasitic infections."
    D'Antonio E.L., Ullman B., Roberts S.C., Dixit U.G., Wilson M.E., Hai Y., Christianson D.W.
    Arch. Biochem. Biophys. 535:163-176(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 13-329 IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ6TUJ5_LEIME
AccessioniPrimary (citable) accession number: Q6TUJ5
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3