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P08955

- PYR1_MESAU

UniProt

P08955 - PYR1_MESAU

Protein

CAD protein

Gene

CAD

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).

    Catalytic activityi

    2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
    Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
    (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

    Cofactori

    Binds 3 zinc ions per subunit (for dihydroorotase activity).By similarity

    Enzyme regulationi

    Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei252 – 2521For GATase activityBy similarity
    Active sitei336 – 3361For GATase activityBy similarity
    Active sitei338 – 3381For GATase activityBy similarity
    Metal bindingi1471 – 14711Zinc 1; via tele nitrogenBy similarity
    Metal bindingi1471 – 14711Zinc 2; via pros nitrogenBy similarity
    Metal bindingi1473 – 14731Zinc 1; via tele nitrogenBy similarity
    Binding sitei1475 – 14751N-carbamoyl-L-aspartateBy similarity
    Binding sitei1505 – 15051N-carbamoyl-L-aspartateBy similarity
    Metal bindingi1556 – 15561Zinc 1; via carbamate groupBy similarity
    Metal bindingi1556 – 15561Zinc 3; via carbamate groupBy similarity
    Metal bindingi1590 – 15901Zinc 3; via pros nitrogenBy similarity
    Metal bindingi1613 – 16131Zinc 2By similarity
    Metal bindingi1614 – 16141Zinc 3; via tele nitrogenBy similarity
    Metal bindingi1637 – 16371Zinc 2By similarity
    Binding sitei1661 – 16611N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity
    Metal bindingi1686 – 16861Zinc 1By similarity
    Binding sitei1686 – 16861N-carbamoyl-L-aspartateBy similarity
    Binding sitei1690 – 16901N-carbamoyl-L-aspartateBy similarity

    GO - Molecular functioni

    1. aspartate binding Source: BHF-UCL
    2. aspartate carbamoyltransferase activity Source: BHF-UCL
    3. ATP binding Source: BHF-UCL
    4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: BHF-UCL
    5. dihydroorotase activity Source: BHF-UCL
    6. protein kinase activity Source: BHF-UCL
    7. UTP binding Source: MGI
    8. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: BHF-UCL
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    3. carbamoyl phosphate biosynthetic process Source: InterPro
    4. glutamine catabolic process Source: InterPro
    5. glutamine metabolic process Source: BHF-UCL
    6. peptidyl-threonine phosphorylation Source: BHF-UCL
    7. protein autophosphorylation Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Ligase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.2.3. 3239.
    SABIO-RKP08955.
    UniPathwayiUPA00070; UER00115.
    UPA00070; UER00116.
    UPA00070; UER00117.

    Protein family/group databases

    MEROPSiM38.972.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CAD protein
    Including the following 3 domains:
    Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5)
    Aspartate carbamoyltransferase (EC:2.1.3.2)
    Dihydroorotase (EC:3.5.2.3)
    Gene namesi
    Name:CAD
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Subcellular locationi

    Cytoplasm. Nucleus By similarity
    Note: Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: BHF-UCL
    3. mitochondrion Source: BHF-UCL
    4. nuclear matrix Source: BHF-UCL
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1406 – 14061S → A: No effect on enzyme kinetics. 1 Publication
    Mutagenesisi1406 – 14061S → D: Increases CPSase activity and reduces sensitivy to feedback inhibition by UTP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 22252224CAD proteinPRO_0000199507Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei456 – 4561Phosphothreonine; by MAPK1By similarity
    Modified residuei747 – 7471N6-acetyllysineBy similarity
    Modified residuei1406 – 14061Phosphoserine; by PKA1 Publication
    Modified residuei1411 – 14111N6-acetyllysineBy similarity
    Modified residuei1556 – 15561N6-carboxylysineBy similarity
    Modified residuei1859 – 18591Phosphoserine; by RPS6KB1 and PKABy similarity
    Modified residuei1873 – 18731Phosphoserine; by PKC; in vitroBy similarity
    Modified residuei1884 – 18841PhosphothreonineBy similarity
    Modified residuei1900 – 19001PhosphoserineBy similarity

    Post-translational modificationi

    Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity By similarity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP08955.

    Interactioni

    Subunit structurei

    Homohexamer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP08955.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini177 – 363187Glutamine amidotransferase type-1Add
    BLAST
    Domaini519 – 711193ATP-grasp 1Add
    BLAST
    Domaini1052 – 1243192ATP-grasp 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 365364GATase (Glutamine amidotransferase)Add
    BLAST
    Regioni366 – 39429LinkerAdd
    BLAST
    Regioni395 – 14551061CPSase (Carbamoyl-phosphate synthase)Add
    BLAST
    Regioni395 – 933539CPSase AAdd
    BLAST
    Regioni934 – 1455522CPSase BAdd
    BLAST
    Regioni1456 – 1788333DHOase (dihydroorotase)Add
    BLAST
    Regioni1789 – 1917129LinkerAdd
    BLAST
    Regioni1918 – 2225308ATCase (Aspartate transcarbamylase)Add
    BLAST

    Sequence similaritiesi

    In the central section; belongs to the DHOase family.Curated
    Contains 2 ATP-grasp domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG000279.

    Family and domain databases

    Gene3Di1.10.1030.10. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 2 hits.
    3.40.50.1370. 2 hits.
    3.40.50.1380. 1 hit.
    3.40.50.20. 2 hits.
    3.40.50.880. 1 hit.
    3.50.30.20. 1 hit.
    HAMAPiMF_00001. Asp_carb_tr.
    MF_01209. CPSase_S_chain.
    InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR002082. Asp_carbamoyltransf.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006275. CarbamoylP_synth_lsu.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005480. CarbamoylP_synth_lsu_oligo.
    IPR006274. CarbamoylP_synth_ssu.
    IPR002474. CarbamoylP_synth_ssu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR005483. CbamoylP_synth_lsu_CPSase_dom.
    IPR029062. Class_I_gatase-like.
    IPR002195. Dihydroorotase_CS.
    IPR017926. GATASE.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR011607. MGS-like_dom.
    IPR016185. PreATP-grasp_dom.
    [Graphical view]
    PfamiPF00289. CPSase_L_chain. 2 hits.
    PF02786. CPSase_L_D2. 2 hits.
    PF02787. CPSase_L_D3. 1 hit.
    PF00988. CPSase_sm_chain. 1 hit.
    PF00117. GATase. 1 hit.
    PF02142. MGS. 1 hit.
    PF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view]
    PRINTSiPR00100. AOTCASE.
    PR00101. ATCASE.
    PR00098. CPSASE.
    SMARTiSM01096. CPSase_L_D3. 1 hit.
    SM01097. CPSase_sm_chain. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48108. SSF48108. 1 hit.
    SSF51338. SSF51338. 1 hit.
    SSF52021. SSF52021. 1 hit.
    SSF52317. SSF52317. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    SSF53671. SSF53671. 1 hit.
    TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
    TIGR01369. CPSaseII_lrg. 1 hit.
    TIGR01368. CPSaseIIsmall. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 2 hits.
    PS00097. CARBAMOYLTRANSFERASE. 1 hit.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    PS00482. DIHYDROOROTASE_1. 1 hit.
    PS00483. DIHYDROOROTASE_2. 1 hit.
    PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08955-1 [UniParc]FASTAAdd to Basket

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    MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL     50
    VLTYPLIGNY GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA 100
    TCTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF 150
    VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV 200
    TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL SEPNPRPVFG 250
    ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 300
    ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF 350
    DVFLETVREA VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG 400
    SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV 450
    YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR 500
    VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY 550
    PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI 600
    EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR 650
    TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY 700
    PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR 750
    VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDV 800
    ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL 850
    EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 900
    KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE 950
    FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM 1000
    DIYELENPDG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK 1050
    FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV 1100
    AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGVVSAIA 1150
    ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 1200
    LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI 1250
    GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL 1300
    KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD 1350
    FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LDQLAENHFE LVINLSMRGA 1400
    GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK 1450
    VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV 1500
    CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG 1550
    SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL 1600
    MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL 1650
    ERLGPGRGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP 1700
    PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV 1750
    EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL 1800
    VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH 1850
    LPPRIHRASD PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS 1900
    PQNLGSSGLL HPQTSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM 1950
    VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS 2000
    VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG 2050
    EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 2100
    LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE 2150
    RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR 2200
    AAYFRQAENG MYIRMALLAT VLGRF 2225
    Length:2,225
    Mass (Da):243,128
    Last modified:August 1, 1992 - v4
    Checksum:i9F6EBA9BD4C6EC5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05503 mRNA. Translation: AAA37062.1.
    M28866 mRNA. Translation: AAA37073.1.
    M60078 mRNA. Translation: AAA63617.1.
    M11242 mRNA. Translation: AAA37061.1.
    M23652 mRNA. Translation: AAA37064.1.
    M21927 mRNA. Translation: AAA37063.1.
    PIRiA38653. A23443.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05503 mRNA. Translation: AAA37062.1 .
    M28866 mRNA. Translation: AAA37073.1 .
    M60078 mRNA. Translation: AAA63617.1 .
    M11242 mRNA. Translation: AAA37061.1 .
    M23652 mRNA. Translation: AAA37064.1 .
    M21927 mRNA. Translation: AAA37063.1 .
    PIRi A38653. A23443.

    3D structure databases

    ProteinModelPortali P08955.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M38.972.

    Proteomic databases

    PRIDEi P08955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000279.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00115 .
    UPA00070 ; UER00116 .
    UPA00070 ; UER00117 .
    BRENDAi 3.5.2.3. 3239.
    SABIO-RK P08955.

    Family and domain databases

    Gene3Di 1.10.1030.10. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 2 hits.
    3.40.50.1370. 2 hits.
    3.40.50.1380. 1 hit.
    3.40.50.20. 2 hits.
    3.40.50.880. 1 hit.
    3.50.30.20. 1 hit.
    HAMAPi MF_00001. Asp_carb_tr.
    MF_01209. CPSase_S_chain.
    InterProi IPR006132. Asp/Orn_carbamoyltranf_P-bd.
    IPR006130. Asp/Orn_carbamoylTrfase.
    IPR002082. Asp_carbamoyltransf.
    IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006275. CarbamoylP_synth_lsu.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005480. CarbamoylP_synth_lsu_oligo.
    IPR006274. CarbamoylP_synth_ssu.
    IPR002474. CarbamoylP_synth_ssu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR005483. CbamoylP_synth_lsu_CPSase_dom.
    IPR029062. Class_I_gatase-like.
    IPR002195. Dihydroorotase_CS.
    IPR017926. GATASE.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR011607. MGS-like_dom.
    IPR016185. PreATP-grasp_dom.
    [Graphical view ]
    Pfami PF00289. CPSase_L_chain. 2 hits.
    PF02786. CPSase_L_D2. 2 hits.
    PF02787. CPSase_L_D3. 1 hit.
    PF00988. CPSase_sm_chain. 1 hit.
    PF00117. GATase. 1 hit.
    PF02142. MGS. 1 hit.
    PF00185. OTCace. 1 hit.
    PF02729. OTCace_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00100. AOTCASE.
    PR00101. ATCASE.
    PR00098. CPSASE.
    SMARTi SM01096. CPSase_L_D3. 1 hit.
    SM01097. CPSase_sm_chain. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48108. SSF48108. 1 hit.
    SSF51338. SSF51338. 1 hit.
    SSF52021. SSF52021. 1 hit.
    SSF52317. SSF52317. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    SSF53671. SSF53671. 1 hit.
    TIGRFAMsi TIGR00670. asp_carb_tr. 1 hit.
    TIGR01369. CPSaseII_lrg. 1 hit.
    TIGR01368. CPSaseIIsmall. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 2 hits.
    PS00097. CARBAMOYLTRANSFERASE. 1 hit.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    PS00482. DIHYDROOROTASE_1. 1 hit.
    PS00483. DIHYDROOROTASE_2. 1 hit.
    PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5'-flanking region of the CAD gene."
      Bein K., Simmer J.P., Evans D.R.
      J. Biol. Chem. 266:3791-3799(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
    2. "Characterization of the 5' end of the growth-regulated Syrian hamster CAD gene."
      Farnham P.J., Kollmar R.
      Cell Growth Differ. 1:179-189(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
    3. "Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD."
      Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R.
      J. Biol. Chem. 265:10395-10402(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 156-1455.
    4. "Identification of the junction between the glutamine amidotransferase and carbamyl phosphate synthetase domains of the mammalian CAD protein."
      Maley J.A., Davidson J.N.
      Biochem. Biophys. Res. Commun. 154:1047-1053(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 246-513.
    5. "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD."
      Simmer J.P., Kelly R.E., Rinker A.G. Jr., Zimmermann B.H., Scully J.L., Kim H., Evans D.R.
      Proc. Natl. Acad. Sci. U.S.A. 87:174-178(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1870.
    6. "Location of the dihydroorotase domain within trifunctional hamster dihydroorotate synthetase."
      Williams N.K., Simpson R.J., Moritz R.L., Peide Y., Crofts L., Minasian E., Leach S.J., Wake R.G., Christopherson R.I.
      Gene 94:283-288(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1403-2110.
    7. "Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain."
      Simmer J.P., Kelly R.E., Scully J.L., Grayson D.R., Rinker A.G. Jr., Bergh S.T., Evans D.R.
      Proc. Natl. Acad. Sci. U.S.A. 86:4382-4386(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1774-2225.
    8. "Construction of a cDNA to the hamster CAD gene and its application toward defining the domain for aspartate transcarbamylase."
      Shigesada K., Stark G.R., Maley J.A., Niswander L.A., Davidson J.N.
      Mol. Cell. Biol. 5:1735-1742(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2225.
    9. "Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells."
      Lee L., Kelly R.E., Pastra-Landis S.C., Evans D.R.
      Proc. Natl. Acad. Sci. U.S.A. 82:6802-6806(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    10. "The structural organization of the hamster multifunctional protein CAD. Controlled proteolysis, domains, and linkers."
      Kim H., Kelly R.E., Evans D.R.
      J. Biol. Chem. 267:7177-7184(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS, PARTIAL PROTEIN SEQUENCE.
    11. "Site-directed substitution of Ser1406 of hamster CAD with glutamic acid alters allosteric regulation of carbamyl phosphate synthetase II."
      Banerjei L.C., Davidson J.N.
      Somat. Cell Mol. Genet. 23:37-49(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1406, MUTAGENESIS OF SER-1406.
    12. "Comparative modeling of mammalian aspartate transcarbamylase."
      Scully J.L., Evans D.R.
      Proteins 9:191-206(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF ATCASE DOMAIN.

    Entry informationi

    Entry nameiPYR1_MESAU
    AccessioniPrimary (citable) accession number: P08955
    Secondary accession number(s): P70108
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 139 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

    Keywords - Technical termi

    Allosteric enzyme, Direct protein sequencing, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3