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Protein

Arginase

Gene

CAR1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.1 Publication

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi113 – 1131Manganese 1By similarity
Metal bindingi136 – 1361Manganese 1By similarity
Metal bindingi136 – 1361Manganese 2By similarity
Metal bindingi138 – 1381Manganese 2By similarity
Metal bindingi140 – 1401Manganese 1By similarity
Binding sitei193 – 1931SubstrateBy similarity
Metal bindingi242 – 2421Manganese 1By similarity
Metal bindingi242 – 2421Manganese 2By similarity
Metal bindingi244 – 2441Manganese 2By similarity

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

Hydrolase

Keywords - Biological processi

Arginine metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase1 Publication (EC:3.5.3.11 Publication)
Gene namesi
Name:CAR11 Publication
Ordered Locus Names:KLLA0F00704g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Chromosome F

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319ArginasePRO_0000432230Add
BLAST

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi28985.Q6CLS8.

Structurei

3D structure databases

ProteinModelPortaliQ6CLS8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 1425Substrate bindingBy similarity
Regioni149 – 1513Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000204319.
InParanoidiQ6CLS8.
KOiK01476.
OMAiDYGDLPF.
OrthoDBiEOG7X0VT2.

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]
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6CLS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSDPRFDFF QQKKLGIVLA PFSGGQPKSG VENGPKYLMK QGLRSDIESL
60 70 80 90 100
GWETTLEEPL KGRDFESGKN DETDVYGIMK RPNLVGEATK LIYESVKKVS
110 120 130 140 150
NEGRLAVTLG GDHSIAIGTV AGVLDKYPNA GLLWIDAHAD INTCSTTESG
160 170 180 190 200
NIHGCPVSFL MGLDAKNTPP SLKWVPKCLD PKKIAYIGLR DVDAAERKIL
210 220 230 240 250
KDNGIASYSM YHVDRYGLNK VIEMALEKVA PNGDEPIMVS YDVDAIDPLY
260 270 280 290 300
VPATGTPVRG GLTLREGLFL VERIAETGRL VALDVVECNP ELASHDGHVV
310
DTITTGCSIA RCALGETLL
Length:319
Mass (Da):34,535
Last modified:August 15, 2004 - v1
Checksum:i021AEE6C115B656E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382126 Genomic DNA. Translation: CAG97818.1.
RefSeqiXP_455111.1. XM_455111.1.

Genome annotation databases

GeneIDi2895828.
KEGGikla:KLLA0F00704g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR382126 Genomic DNA. Translation: CAG97818.1.
RefSeqiXP_455111.1. XM_455111.1.

3D structure databases

ProteinModelPortaliQ6CLS8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.Q6CLS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2895828.
KEGGikla:KLLA0F00704g.

Phylogenomic databases

HOGENOMiHOG000204319.
InParanoidiQ6CLS8.
KOiK01476.
OMAiDYGDLPF.
OrthoDBiEOG7X0VT2.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.

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]
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
  2. "An alternative, arginase-independent pathway for arginine metabolism in Kluyveromyces lactis involves guanidinobutyrase as a key enzyme."
    Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R., van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V., Wahl S.A., Pronk J.T., Daran J.M.
    Mol. Microbiol. 93:369-389(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiARGI_KLULA
AccessioniPrimary (citable) accession number: Q6CLS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2015
Last sequence update: August 15, 2004
Last modified: March 31, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.