ID A0A1D8PP00_CANAL Unreviewed; 317 AA.
AC A0A1D8PP00;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|RuleBase:RU361159};
DE EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
GN Name=CAR1 {ECO:0000313|CGD:CAL0000174553,
GN ECO:0000313|EMBL:AOW29856.1};
GN OrderedLocusNames=CAALFM_C504490CA {ECO:0000313|EMBL:AOW29856.1},
GN orf19.11416 {ECO:0000313|CGD:CAL0000174553};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW29856.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW29856.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW29856.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW29856.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000227,
CC ECO:0000256|RuleBase:RU361159};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361159};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|RuleBase:RU361159};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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DR EMBL; CP017627; AOW29856.1; -; Genomic_DNA.
DR RefSeq; XP_721843.1; XM_716750.2.
DR AlphaFoldDB; A0A1D8PP00; -.
DR SMR; A0A1D8PP00; -.
DR STRING; 237561.A0A1D8PP00; -.
DR EnsemblFungi; C5_04490C_A-T; C5_04490C_A-T-p1; C5_04490C_A.
DR GeneID; 3636503; -.
DR KEGG; cal:CAALFM_C504490CA; -.
DR CGD; CAL0000174553; CAR1.
DR VEuPathDB; FungiDB:C5_04490C_A; -.
DR eggNOG; KOG2965; Eukaryota.
DR InParanoid; A0A1D8PP00; -.
DR OMA; YKEFRYA; -.
DR OrthoDB; 161483at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0004053; F:arginase activity; IMP:CGD.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IMP:CGD.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR NCBIfam; TIGR01229; rocF_arginase; 1.
DR PANTHER; PTHR43782; ARGINASE; 1.
DR PANTHER; PTHR43782:SF3; ARGINASE; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Arginine metabolism {ECO:0000256|ARBA:ARBA00022503,
KW ECO:0000256|RuleBase:RU361159};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Manganese {ECO:0000256|RuleBase:RU361159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361159};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559}.
SQ SEQUENCE 317 AA; 34329 MW; 787507A7270BC30A CRC64;
MSSIQYKYHP DKKASIITAP FSGGQPKGGV ELGPDYILKA GFQKQIESLG WTTDLKEPLE
GTDYEKMKTN DKDDFGVKNS KIVSESCQKI HDAVKGSLAE GKLPITIGGD HSIGTATVSA
SLVHDPSTCV VWVDAHADIN TPKTTDSGNL HGCPLSFIMG IDRDSYPPEF SWVPQVLKSN
KLVYIGLRDV DDGEKEILRK HNIAAFSMYH VDKYGIGKVV EMALDKVNPN RDCPVHLSYD
VDAIDPSFVP ATGTRVEGGL SLREGLFIAE EIAQSGLLQS LDIVETNPML AETEEHVLDT
VSAACAIGRC ALGQTLL
//
