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)	Length	Description
Metal bindingⁱ	113 – 113	1	Manganese 1By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	136 – 136	1	Manganese 1By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	136 – 136	1	Manganese 2By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	138 – 138	1	Manganese 2By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	140 – 140	1	Manganese 1By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Binding siteⁱ	193 – 193	1	SubstrateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	242 – 242	1	Manganese 1By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	242 – 242	1	Manganese 2By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Metal bindingⁱ	244 – 244	1	Manganese 2By similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Binding siteⁱ	256 – 256	1	SubstrateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P53608 (ARGI_BACCD)
Binding siteⁱ	287 – 287	1	SubstrateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P53608 (ARGI_BACCD)

GO - Molecular functionⁱ

arginase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW

GO - Biological processⁱ

arginine metabolic process Source: UniProtKB-KW
urea cycle Source: UniProtKB-UniPathway

Complete GO annotation...

Enzyme and pathway databases

UniPathwayⁱ	UPA00158; UER00270.

UniPathwayⁱ

UPA00158; UER00270.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Arginase1 Publication Manual assertion based on opinion inⁱ Ref.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(2014) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PATHWAY. (EC:3.5.3.11 Publication Manual assertion based on experiment inⁱ Ref.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(2014) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PATHWAY. )
Gene namesⁱ	Name:CAR11 Publication Manual assertion based on opinion inⁱ Ref.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(2014) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, PATHWAY. 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

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 319	319	Arginase		PRO_0000432230	Add BLAST

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.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	138 – 142	5	Substrate bindingBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)
Regionⁱ	149 – 151	3	Substrate bindingBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:P05089 (ARGI1_HUMAN)

Sequence similaritiesⁱ

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG2965. Eukaryota. COG0010. LUCA.
HOGENOMⁱ	HOG000204319.
InParanoidⁱ	Q6CLS8.
KOⁱ	K01476.
OMAⁱ	EQECDVK.
OrthoDBⁱ	EOG092C3GMN.

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]
PRINTSⁱ	PR00116. ARGINASE.
TIGRFAMsⁱ	TIGR01229. rocF_arginase. 1 hit.
PROSITEⁱ	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]

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.
RefSeqⁱ	XP_455111.1. XM_455111.1.

Genome annotation databases

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

Cross-referencesⁱ

Sequence databases

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

3D structure databases

ProteinModelPortalⁱ	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.
KOⁱ	K01476.
OMAⁱ	EQECDVK.
OrthoDBⁱ	EOG092C3GMN.

Enzyme and pathway databases

UniPathwayⁱ	UPA00158; UER00270.

UniPathwayⁱ

UPA00158; UER00270.

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]
PRINTSⁱ	PR00116. ARGINASE.
TIGRFAMsⁱ	TIGR01229. rocF_arginase. 1 hit.
PROSITEⁱ	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

ARGI_KLULA

Accessionⁱ

Primary (citable) accession number: Q6CLS8

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	March 4, 2015
Last sequence update:	August 16, 2004
Last modified:	September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q6CLS8 (ARGI_KLULA)

UniProt

Q6CLS8 - ARGI_KLULA

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Arginase

Select a section on the left to see content.

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

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/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><p><a href='../manual/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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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

Molecule processing

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

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

Region

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>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><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/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>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

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

Documents

Functionⁱ

Pathwayⁱ: urea cycle

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ