ARGI_KLULA
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 03-AUG-2022, entry version 110.
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}; 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 / 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 -!- 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:0000269|PubMed:24912400};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
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 STRING; 28985.XP_455111.1; -.
DR EnsemblFungi; CAG97818; CAG97818; KLLA0_F00704g.
DR GeneID; 2895828; -.
DR KEGG; kla:KLLA0_F00704g; -.
DR eggNOG; KOG2965; Eukaryota.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q6CLS8; -.
DR OMA; IATCFGQ; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:1903269; C:ornithine carbamoyltransferase inhibitor complex; IEA:EnsemblFungi.
DR GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:EnsemblFungi.
DR GO; GO:0090369; F:ornithine carbamoyltransferase inhibitor activity; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:EnsemblFungi.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:EnsemblFungi.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd09989; Arginase; 1.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01229; rocF_arginase; 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..142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
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="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 287
FT /ligand="substrate"
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
