CAR1

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: urea cycle

This protein is involved in step 1 of the subpathway that synthesizes L-ornithine and urea from L-arginine.1 Publication
Proteins known to be involved in this subpathway in this organism are:

Arginase (CAR1)

This subpathway is part of the pathway urea cycle, which is itself part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine and urea from L-arginine, the pathway urea cycle and in Nitrogen metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	113	Manganese 1By similarity	1
Metal bindingⁱ	136	Manganese 1By similarity	1
Metal bindingⁱ	136	Manganese 2By similarity	1
Metal bindingⁱ	138	Manganese 2By similarity	1
Metal bindingⁱ	140	Manganese 1By similarity	1
Binding siteⁱ	193	SubstrateBy similarity	1
Metal bindingⁱ	242	Manganese 1By similarity	1
Metal bindingⁱ	242	Manganese 2By similarity	1
Metal bindingⁱ	244	Manganese 2By similarity	1
Binding siteⁱ	256	SubstrateBy similarity	1
Binding siteⁱ	287	SubstrateBy similarity	1

GO - Molecular functionⁱ

arginase activity Source: UniProtKB-EC
manganese ion binding Source: EnsemblFungi
ornithine carbamoyltransferase inhibitor activity Source: EnsemblFungi
zinc ion binding Source: EnsemblFungi

Complete GO annotation...

GO - Biological processⁱ

arginine catabolic process to ornithine Source: EnsemblFungi
urea cycle Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Arginine metabolism
Ligand	Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayⁱ	UPA00158; UER00270.

UniPathwayⁱ

UPA00158; UER00270.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Arginase1 Publication (EC:3.5.3.11 Publication)
Gene namesⁱ	Name:CAR11 Publication Ordered Locus Names:KLLA0F00704g
Organismⁱ	Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifierⁱ	284590 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis
Proteomesⁱ	UP000000598 Componentⁱ: Chromosome F

Subcellular locationⁱ

GO (Gene Ontology) annotation

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000432230	1 – 319	ArginaseAdd BLAST		319

Interactionⁱ

Subunit structureⁱ

Homotrimer.By similarity

Protein-protein interaction databases

STRINGⁱ	284590.XP_455111.1.

STRINGⁱ

284590.XP_455111.1.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q6CLS8.
SMRⁱ	Q6CLS8.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	138 – 142	Substrate bindingBy similarity		5
Regionⁱ	149 – 151	Substrate bindingBy similarity		3

Sequence similaritiesⁱ

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG2965. Eukaryota. COG0010. LUCA.
HOGENOMⁱ	HOG000204319.
InParanoidⁱ	Q6CLS8.
KEGG Orthology (KO) More...KOⁱ	K01476.
OMAⁱ	SAVARHC.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C3GMN.

Family and domain databases

InterProⁱ	View protein in InterPro IPR014033. Arginase. IPR006035. Ureohydrolase. IPR020855. Ureohydrolase_Mn_BS.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00491. Arginase. 1 hit.
PRINTSⁱ	PR00116. ARGINASE.
TIGRFAMsⁱ	TIGR01229. rocF_arginase. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q6CLS8-1 [UniParc]FASTA Add 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 16, 2004 - v1

Checksum:ⁱ021AEE6C115B656E

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CR382126 Genomic DNA. Translation: CAG97818.1.
NCBI Reference Sequences More...RefSeqⁱ	XP_455111.1. XM_455111.1.

Genome annotation databases

EnsemblFungiⁱ	CAG97818; CAG97818; KLLA0_F00704g.
GeneIDⁱ	2895828.
KEGGⁱ	kla:KLLA0F00704g.

Similar proteinsⁱ

50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q6CLS8	I2JZ33 A0A1G4KMR5 A0A1E3NJ04 A0A0A8LAL4 W0TCC3 A0A1E4RJE9 Q6FP31 A0A0W0E873 C5MIY7 H8X923 +45	Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) Brettanomyces bruxellensis AWRI1499 Lachancea nothofagi CBS 11611 Pichia membranifaciens NRRL Y-2026 Kluyveromyces dobzhanskii CBS 2104 Kluyveromyces marxianus DMKU3-1042 Hyphopichia burtonii NRRL Y-1933 Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) Candida glabrata (Yeast) (Torulopsis glabrata) Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast) And more	319	UniRef50_Q6CLS8	Cluster: Arginase	56

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CR382126 Genomic DNA. Translation: CAG97818.1.
NCBI Reference Sequences More...RefSeqⁱ	XP_455111.1. XM_455111.1.

3D structure databases

ProteinModelPortalⁱ	Q6CLS8.
SMRⁱ	Q6CLS8.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	284590.XP_455111.1.

STRINGⁱ

284590.XP_455111.1.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	CAG97818; CAG97818; KLLA0_F00704g.
GeneIDⁱ	2895828.
KEGGⁱ	kla:KLLA0F00704g.

Phylogenomic databases

eggNOGⁱ	KOG2965. Eukaryota. COG0010. LUCA.
HOGENOMⁱ	HOG000204319.
InParanoidⁱ	Q6CLS8.
KEGG Orthology (KO) More...KOⁱ	K01476.
OMAⁱ	SAVARHC.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C3GMN.

Enzyme and pathway databases

UniPathwayⁱ	UPA00158; UER00270.

UniPathwayⁱ

UPA00158; UER00270.

Family and domain databases

InterProⁱ	View protein in InterPro IPR014033. Arginase. IPR006035. Ureohydrolase. IPR020855. Ureohydrolase_Mn_BS.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00491. Arginase. 1 hit.
PRINTSⁱ	PR00116. ARGINASE.
TIGRFAMsⁱ	TIGR01229. rocF_arginase. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ARGI_KLULA
Accessionⁱ	Q6CLS8Primary (citable) accession number: Q6CLS8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 4, 2015
	Last sequence update:	August 16, 2004
	Last modified:	September 27, 2017
	This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q6CLS8 (ARGI_KLULA)

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Arginase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: urea cycle

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: urea cycle

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ