OTC_YEAST
ID OTC_YEAST Reviewed; 338 AA.
AC P05150; D6VW96;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ornithine carbamoyltransferase;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
GN Name=ARG3; OrderedLocusNames=YJL088W; ORFNames=J0924;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3038540; DOI=10.1111/j.1432-1033.1987.tb13525.x;
RA Huygen R., Crabeel M., Glansdorff N.;
RT "Nucleotide sequence of the ARG3 gene of the yeast Saccharomyces cerevisiae
RT encoding ornithine carbamoyltransferase. Comparison with other
RT carbamoyltransferases.";
RL Eur. J. Biochem. 166:371-377(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=3915770; DOI=10.1128/mcb.5.11.3139-3148.1985;
RA Crabeel M., Huygen R., Verschueren K., Messenguy F., Tinel K., Cunin R.,
RA Glansdorff N.;
RT "General amino acid control and specific arginine repression in
RT Saccharomyces cerevisiae: physical study of the bifunctional regulatory
RT region of the ARG3 gene.";
RL Mol. Cell. Biol. 5:3139-3148(1985).
RN [6]
RP MUTAGENESIS OF THR-68; GLY-181; ASP-182; ASN-184; ASN-185; GLU-256;
RP LYS-263; CYS-289 AND LEU-290, INTERACTION WITH CAR1, AND ACTIVITY
RP REGULATION.
RX PubMed=12679340; DOI=10.1074/jbc.m300383200;
RA El Alami M., Dubois E., Oudjama Y., Tricot C., Wouters J., Stalon V.,
RA Messenguy F.;
RT "Yeast epiarginase regulation, an enzyme-enzyme activity control:
RT identification of residues of ornithine carbamoyltransferase and arginase
RT responsible for enzyme catalytic and regulatory activities.";
RL J. Biol. Chem. 278:21550-21558(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3;
CC -!- ACTIVITY REGULATION: Forms a stable complex with CAR1 in the presence
CC of ornithine and arginine. In this complex CAR1 retains activity, but
CC ARG3 activity is inhibited. {ECO:0000269|PubMed:12679340}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC -!- SUBUNIT: Interacts with CAR1. {ECO:0000269|PubMed:12679340}.
CC -!- INTERACTION:
CC P05150; P00812: CAR1; NbExp=4; IntAct=EBI-12712, EBI-2856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 1140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M11946; AAA34432.1; -; Genomic_DNA.
DR EMBL; X83502; CAA58480.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49363; CAA89381.1; ALT_INIT; Genomic_DNA.
DR EMBL; M28301; AAA34433.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08712.1; -; Genomic_DNA.
DR PIR; S56020; OWBY.
DR RefSeq; NP_012447.1; NM_001181521.1.
DR AlphaFoldDB; P05150; -.
DR SMR; P05150; -.
DR BioGRID; 33669; 27.
DR ComplexPortal; CPX-1707; Ornithine carbamoyltransferase arginase complex.
DR DIP; DIP-8093N; -.
DR IntAct; P05150; 60.
DR MINT; P05150; -.
DR STRING; 4932.YJL088W; -.
DR iPTMnet; P05150; -.
DR MaxQB; P05150; -.
DR PaxDb; P05150; -.
DR PRIDE; P05150; -.
DR EnsemblFungi; YJL088W_mRNA; YJL088W; YJL088W.
DR GeneID; 853357; -.
DR KEGG; sce:YJL088W; -.
DR SGD; S000003624; ARG3.
DR VEuPathDB; FungiDB:YJL088W; -.
DR eggNOG; KOG1504; Eukaryota.
DR GeneTree; ENSGT00510000047417; -.
DR HOGENOM; CLU_043846_3_0_1; -.
DR InParanoid; P05150; -.
DR OMA; DGNNVCN; -.
DR BioCyc; MetaCyc:YJL088W-MON; -.
DR BioCyc; YEAST:YJL088W-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR Reactome; R-SCE-70635; Urea cycle.
DR SABIO-RK; P05150; -.
DR UniPathway; UPA00068; UER00112.
DR PRO; PR:P05150; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P05150; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:1903269; C:ornithine carbamoyltransferase inhibitor complex; IPI:ComplexPortal.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:SGD.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:SGD.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..338
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000113082"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 67..70
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 118
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 145
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 148
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 185
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 249
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 253
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 254
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 289..290
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 316
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 68
FT /note="T->G: Reduces activity by 95%. Reduces affinity for
FT ornithine 2-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 181
FT /note="G->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 182
FT /note="D->N: Reduces activity by 33%. Reduces affinity for
FT ornithine 30-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 184
FT /note="N->Q: Reduces activity by 50%. Reduces affinity for
FT ornithine 20-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 185
FT /note="N->Q: No effect on activity. Reduces affinity for
FT ornithine 200-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 256
FT /note="E->Q: Reduces activity by 50%."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 263
FT /note="K->A: Reduces activity by 70%. Reduces affinity for
FT ornithine 18-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 289
FT /note="C->S: Reduces activity by 90%. Reduces affinity for
FT ornithine 6-fold."
FT /evidence="ECO:0000269|PubMed:12679340"
FT MUTAGEN 290
FT /note="L->S: Reduces activity by 86%."
FT /evidence="ECO:0000269|PubMed:12679340"
SQ SEQUENCE 338 AA; 37845 MW; 6EBB6598FA93C59E CRC64;
MSTTASTPSS LRHLISIKDL SDEEFRILVQ RAQHFKNVFK ANKTNDFQSN HLKLLGRTIA
LIFTKRSTRT RISTEGAATF FGAQPMFLGK EDIQLGVNES FYDTTKVVSS MVSCIFARVN
KHEDILAFCK DSSVPIINSL CDKFHPLQAI CDLLTIIENF NISLDEVNKG INSKLKMAWI
GDANNVINDM CIACLKFGIS VSISTPPGIE MDSDIVDEAK KVAERNGATF ELTHDSLKAS
TNANILVTDT FVSMGEEFAK QAKLKQFKGF QINQELVSVA DPNYKFMHCL PRHQEEVSDD
VFYGEHSIVF EEAENRLYAA MSAIDIFVNN KGNFKDLK
