GenomeNet

Database: UniProt
Entry: Q09794
LinkDB: Q09794
Original site: Q09794 
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   13-FEB-2019, entry version 166.
DE   RecName: Full=Protein ura1;
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE              EC=6.3.5.5;
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase;
DE              EC=2.1.3.2;
GN   Name=ura1; ORFNames=SPAC22G7.06c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-2244.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8590465; DOI=10.1007/BF00315780;
RA   Lollier M., Jaquet L., Nedeva T., Lacroute F., Potier S.,
RA   Souciet J.-L.;
RT   "As in Saccharomyces cerevisiae, aspartate transcarbamoylase is
RT   assembled on a multifunctional protein including a dihydroorotase-like
RT   cryptic domain 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RP   SER-1885, 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
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       and ATCase). {ECO:0000250}.
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   -!- 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;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- DOMAIN: The DHOase domain is defective.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) form together the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5).
CC   -!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two
CC       pathway-specific (arginine and pyrimidine) genes under separate
CC       control.
CC   -!- SIMILARITY: In the central section; belongs to the metallo-
CC       dependent hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000305}.
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   ProteinModelPortal; Q09794; -.
DR   SMR; Q09794; -.
DR   BioGrid; 278044; 22.
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   EuPathDB; FungiDB:SPAC22G7.06c; -.
DR   PomBase; SPAC22G7.06c; ura1.
DR   HOGENOM; HOG000234584; -.
DR   InParanoid; Q09794; -.
DR   KO; K11541; -.
DR   OMA; FTNANDH; -.
DR   PhylomeDB; Q09794; -.
DR   Reactome; R-SPO-500753; Pyrimidine biosynthesis.
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; PR00101; ATCASE.
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; Complete proteome; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Pyrimidine biosynthesis;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN         1   2244       Protein ura1.
FT                                /FTId=PRO_0000199510.
FT   DOMAIN      264    449       Glutamine amidotransferase type-1.
FT   DOMAIN      598    790       ATP-grasp 1.
FT   DOMAIN     1133   1324       ATP-grasp 2.
FT   DOMAIN     1390   1552       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   REGION        1    437       GATase (Glutamine amidotransferase).
FT                                {ECO:0000250}.
FT   REGION      438    477       Linker. {ECO:0000250}.
FT   REGION      478   1514       CPSase (Carbamoyl-phosphate synthase).
FT                                {ECO:0000250}.
FT   REGION     1515   1524       Linker. {ECO:0000250}.
FT   REGION     1525   1853       Defective DHOase domain. {ECO:0000250}.
FT   REGION     1854   1935       Linker. {ECO:0000250}.
FT   REGION     1936   2244       ATCase (Aspartate transcarbamylase).
FT                                {ECO:0000250}.
FT   ACT_SITE    338    338       For GATase activity. {ECO:0000250}.
FT   ACT_SITE    422    422       For GATase activity. {ECO:0000250}.
FT   ACT_SITE    424    424       For GATase activity. {ECO:0000250}.
FT   MOD_RES    1119   1119       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES    1881   1881       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES    1885   1885       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   CONFLICT    336    338       GIC -> RYF (in Ref. 1; CAA57433).
FT                                {ECO:0000305}.
FT   CONFLICT   1035   1039       CAVRA -> LQFAQ (in Ref. 1; CAA57433).
FT                                {ECO:0000305}.
FT   CONFLICT   1409   1410       EL -> DV (in Ref. 1; CAA57433).
FT                                {ECO:0000305}.
FT   CONFLICT   1975   1975       G -> E (in Ref. 1; CAA57433).
FT                                {ECO:0000305}.
FT   CONFLICT   2002   2002       G -> E (in Ref. 1; CAA57433).
FT                                {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
//
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