ID   ARGI_KLULA              Reviewed;         319 AA.
AC   Q6CLS8;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-SEP-2026, entry version 126.
DE   RecName: Full=Arginase {ECO:0000303|PubMed:24912400};
DE            EC=3.5.3.1 {ECO:0000269|PubMed:24912400};
GN   Name=CAR1 {ECO:0000303|PubMed:24912400};
GN   OrderedLocusNames=KLLA0F00704g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=24912400; DOI=10.1111/mmi.12666;
RA   Romagnoli G., Verhoeven M.D., Mans R., Fleury Rey Y., Bel-Rhlid R.,
RA   van den Broek M., Seifar R.M., Ten Pierick A., Thompson M., Muller V.,
RA   Wahl S.A., Pronk J.T., Daran J.M.;
RT   "An alternative, arginase-independent pathway for arginine metabolism in
RT   Kluyveromyces lactis involves guanidinobutyrase as a key enzyme.";
RL   Mol. Microbiol. 93:369-389(2014).
CC   -!- FUNCTION: Catalyzes the hydrolysis of L-arginine into urea and L-
CC       ornithine. {ECO:0000250|UniProtKB:P39138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine + H2O = urea + L-ornithine; 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:0000269|PubMed:24912400};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00742};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742};
CC   -!- ACTIVITY REGULATION: Allosterically activated by L-arginine.
CC       {ECO:0000250|UniProtKB:P53608}.
CC   -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC       arginine: step 1/1. {ECO:0000305|PubMed:24912400}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P00812}.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742}.
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DR   EMBL; CR382126; CAG97818.1; -; Genomic_DNA.
DR   RefSeq; XP_455111.1; XM_455111.1.
DR   AlphaFoldDB; Q6CLS8; -.
DR   SMR; Q6CLS8; -.
DR   FunCoup; Q6CLS8; 1417.
DR   STRING; 284590.Q6CLS8; -.
DR   PaxDb; 284590-Q6CLS8; -.
DR   GeneID; 2895828; -.
DR   KEGG; kla:KLLA0_F00704g; -.
DR   eggNOG; KOG2965; Eukaryota.
DR   HOGENOM; CLU_039478_6_1_1; -.
DR   InParanoid; Q6CLS8; -.
DR   OMA; YKEFRYA; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004053; F:arginase activity; EXP:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter.
DR   GO; GO:0006525; P:arginine metabolic process; IEA:InterPro.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd09989; Arginase; 1.
DR   FunFam; 3.40.800.10:FF:000009; 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   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   1: Evidence at protein level;
KW   Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..319
FT                   /note="Arginase"
FT                   /id="PRO_0000432230"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         136
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         136
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         138
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         138
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         140
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         140
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         142
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         149
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         153
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         154
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         193
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         196
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         214
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         242
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         244
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         244
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P05089"
FT   BINDING         256
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         272
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         287
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         316
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
SQ   SEQUENCE   319 AA;  34535 MW;  021AEE6C115B656E CRC64;
     MSSDPRFDFF QQKKLGIVLA PFSGGQPKSG VENGPKYLMK QGLRSDIESL GWETTLEEPL
     KGRDFESGKN DETDVYGIMK RPNLVGEATK LIYESVKKVS NEGRLAVTLG GDHSIAIGTV
     AGVLDKYPNA GLLWIDAHAD INTCSTTESG NIHGCPVSFL MGLDAKNTPP SLKWVPKCLD
     PKKIAYIGLR DVDAAERKIL KDNGIASYSM YHVDRYGLNK VIEMALEKVA PNGDEPIMVS
     YDVDAIDPLY VPATGTPVRG GLTLREGLFL VERIAETGRL VALDVVECNP ELASHDGHVV
     DTITTGCSIA RCALGETLL
//