PYR1_SCHPO
ID PYR1_SCHPO Reviewed; 2244 AA.
AC Q09794;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 181.
DE RecName: Full=Protein ura1;
DE Includes:
DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE EC=6.3.5.5 {ECO:0000305|PubMed:8590465};
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2 {ECO:0000269|PubMed:8590465};
GN Name=ura1; ORFNames=SPAC22G7.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-2244, FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND DOMAIN.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8590465; DOI=10.1007/bf00315780;
RA Lollier M., Jaquet L., Nedeva T., Lacroute F., Potier S., Souciet J.-L.;
RT "As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled
RT on a multifunctional protein including a dihydroorotase-like cryptic domain
RT in Schizosaccharomyces pombe.";
RL Curr. Genet. 28:138-149(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1119; SER-1881 AND SER-1885,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: This protein is a 'fusion' protein encoding three enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
CC {ECO:0000250, ECO:0000269|PubMed:8590465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000305|PubMed:8590465};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2; Evidence={ECO:0000269|PubMed:8590465};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000305|PubMed:8590465}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000305|PubMed:8590465}.
CC -!- DOMAIN: The DHOase domain is defective. {ECO:0000269|PubMed:8590465}.
CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC (carbamoyl phosphate synthase) form together the glutamine-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5).
CC -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two pathway-
CC specific (arginine and pyrimidine) genes under separate control.
CC -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily. {ECO:0000305}.
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DR EMBL; X81841; CAA57433.1; -; mRNA.
DR EMBL; CU329670; CAA91130.1; -; Genomic_DNA.
DR PIR; S65074; S65074.
DR PIR; T11616; T11616.
DR RefSeq; NP_593055.1; NM_001018453.2.
DR AlphaFoldDB; Q09794; -.
DR SMR; Q09794; -.
DR BioGRID; 278044; 25.
DR DIP; DIP-59121N; -.
DR IntAct; Q09794; 1.
DR STRING; 4896.SPAC22G7.06c.1; -.
DR MEROPS; C26.956; -.
DR iPTMnet; Q09794; -.
DR MaxQB; Q09794; -.
DR PaxDb; Q09794; -.
DR PRIDE; Q09794; -.
DR EnsemblFungi; SPAC22G7.06c.1; SPAC22G7.06c.1:pep; SPAC22G7.06c.
DR GeneID; 2541544; -.
DR KEGG; spo:SPAC22G7.06c; -.
DR PomBase; SPAC22G7.06c; ura1.
DR VEuPathDB; FungiDB:SPAC22G7.06c; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_0_1; -.
DR InParanoid; Q09794; -.
DR OMA; IPCTSML; -.
DR PhylomeDB; Q09794; -.
DR Reactome; R-SPO-500753; Pyrimidine biosynthesis.
DR Reactome; R-SPO-70635; Urea cycle.
DR UniPathway; UPA00070; UER00115.
DR UniPathway; UPA00070; UER00116.
DR PRO; PR:Q09794; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IMP:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IGI:PomBase.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IGI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IGI:PomBase.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IGI:PomBase.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1370; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Multifunctional enzyme; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..2244
FT /note="Protein ura1"
FT /id="PRO_0000199510"
FT DOMAIN 264..449
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 598..790
FT /note="ATP-grasp 1"
FT DOMAIN 1133..1324
FT /note="ATP-grasp 2"
FT DOMAIN 1390..1552
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..437
FT /note="GATase (Glutamine amidotransferase)"
FT /evidence="ECO:0000250"
FT REGION 16..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..477
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 478..1514
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT /evidence="ECO:0000250"
FT REGION 1515..1524
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 1525..1853
FT /note="Defective DHOase domain"
FT /evidence="ECO:0000250"
FT REGION 1854..1935
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 1936..2244
FT /note="ATCase (Aspartate transcarbamylase)"
FT /evidence="ECO:0000250"
FT ACT_SITE 338
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 422
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 424
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1881
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1885
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 336..338
FT /note="GIC -> RYF (in Ref. 1; CAA57433)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035..1039
FT /note="CAVRA -> LQFAQ (in Ref. 1; CAA57433)"
FT /evidence="ECO:0000305"
FT CONFLICT 1409..1410
FT /note="EL -> DV (in Ref. 1; CAA57433)"
FT /evidence="ECO:0000305"
FT CONFLICT 1975
FT /note="G -> E (in Ref. 1; CAA57433)"
FT /evidence="ECO:0000305"
FT CONFLICT 2002
FT /note="G -> E (in Ref. 1; CAA57433)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2244 AA; 248309 MW; 5700D153B50CD3E9 CRC64;
MSGLLPSLSS SFPLVQSEAL GMPRTHGPKP SENDPKEPTC SPSPAFYSVN GEMKDYKLMA
LELEDKSVLQ GYSFGADHSV SGELVFQTGM VGYPESLTDP SYRGQILVFT FPTVGNYGVP
DRRILDEISG LPKYFESNQI HVAAIIISSY SQNYSHFLAH SSLGEWLKEQ GIPGIFGIDT
RALTKKIRDQ GSMLGRLLIQ KDESPINPSS ITGLGKDWST AFEDIPWKNP NTENLTSQVS
IKEPKLYEPH PTTAIKKADG KIIRILVIDV GMKYNQIRCF LNRGVELLVV PWDYDFTKET
YDGLFISNGP GDPSLMDLVV DRVKRVLESK TVPVFGICFG HQIMARAAGA STTKMKFGNR
GHNIPCTCMI SGRCYITSQN HGYAVDASSL SNGWKELFVN ANDGSNEGIY NTEYPFFSVQ
FHPESTPGPR DTEFLFDVFI DVVKRSADAK SLQPFKLPGG TIEENRSRHP LVDAKRVLIL
GSGGLSIGQA GEFDYSGSQA IKALREEGIY TILINPNIAT IQTSKGLADK VYFLPVNADF
VRKVIKQERP DSIYVTFGGQ TALNVGIELK DEFEQLGVKV LGTPIDTIIT TEDRELFARA
MDEINEKCAK SASASSIEEA IKVSKDISFP VIVRAAYALG GLGSGFADNE AELIDLCTLA
FATSPQVLIE RSMKGWKEIE YEVVRDAFDN CITVCNMENF DPLGIHTGDS IVVAPSQTLT
DEDYNMLRTT AVNVIRHLGV VGECNIQYAL NPFTKEYCII EVNARLSRSS ALASKATGYP
LAFTAAKLGL NIPLNEVKNS VTKVTCACFE PSLDYVVVKI PRWDLKKFTR VSTQLSSAMK
SVGEVMSIGR TFEEAIQKAI RAIDYSNTGF NVKDALMSID TELQTPSDQR LFAIANAMAS
GYSVDRIWEL TRIDKWFLEK LMGLIRTSQL ISKHDISSLP ISLLKTAKQL GFADVQIAAF
MNSTELAVRR IRTEAGIRPF VKQIDTVAAE FPAFTNYLYT TYNAVEHDIH FNDKGVMVLG
SGVYRIGSSV EFDWCAVRAV RTLRDRGVKT IMVNYNPETV STDYDEADRL YFENIGLETV
LDIYEQESSS GIIIAMGGQT ANNIALPLHR ENVKILGTSP EMIDGAENRF KFSRMLDDIG
VDQPKWKELT SFDEADKFCD TVGYPVLVRP SYVLSGAAMN TVYSQSDLHS YLQQAVAINK
DHPVVISKYI ENAKEIELDA VAREGKMVMH VISEHVENAG VHSGDATLVL PPQDLAPTTI
ERIVDAAAKI GEALNITGPY NIQFIAKDNE IKVIECNVRA SRSFPFVSKV IGVDMISMAT
DVIMGNPIQP YPDVDLPRDY VAVKVPQFSF SRLSGADPVL GVEMASTGEV ACFGHNKFEA
YLKAMISTGF RLPKKNILIS IGSYKEKAEL LPYVKKLYEN NYNIFATAGT SDYFMESGVP
CKYLADLPAE EANNEYSLSA HLANNMIDMY INLPSNNRYR RPANYISSGY KSRRLAIDYS
VPLVTNVKCA KLMIEAICRN LDFSLSTVDF QSSFQTANLP GLINISAFLP EFTSEAVSDY
TKECIASGFT MARFLPFSTS STLADKDSLS AVKKLALDHA HCDYNFSVIA SSTNEVTISE
LTSESGCLFF HFEKDDSGID HVTAVASHFN VWPDTQTVMT DAKSTTLASL LLLASLHNRR
IHITNVSSKD DLNLIVLAKQ RSLPVTFDVS VYSLFLNQND YPGATFLPTA DDQVEIWNKL
SYIDCFSIGS IPSRLAKFVG NTAFTGFGVR EAIPLLLTAV NEGRLTLKDV VDRFYSNPKA
IFRLHDQDDS GVQLEVDRSV SWSSKDWTPF NGKKLYGSIQ SVQFDGHDVF FDGELNFEHT
YGRDYSSASL ADKSKATRKV SALMSPGLPH AAPSLAEAFG QAPENKAHPD ISLNMTPNFK
PSHELVQLIN SSPFYRKHII SVHQVTRSDL HVLFAIAHQM RIIVERQGVI DLCYGKLLCT
MFFEPSTRTS SSFDAAMQRL GGKVVAVTAS ASSVNKGESL ADTIRTLGCY GDAIVLRHPS
IESARIAANF SPVPIINGGN GSKEHPTQAF LDLYTIREEL GSVNGLTITF IGDLKYGRTV
HSLARLLAFW HVELHLVSPE QLALPDDVKD DIRANGLNFI EHRELTKEVV AQSDVLYCTR
VQKERFASVD EYEKLKDSFI VDNSVLASAK SHCIVMHPLP RNREISEEVD FDQRRAAYFR
QMRYGLYIRM ALLACVMGAT EVAN
