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B2RQC6

- PYR1_MOUSE

UniProt

B2RQC6 - PYR1_MOUSE

Protein

CAD protein

Gene

Cad

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      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).By similarity

    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 By similarity.By similarity

    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. amino acid binding Source: InterPro
    2. aspartate carbamoyltransferase activity Source: UniProtKB-EC
    3. ATP binding Source: UniProtKB-KW
    4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
    5. dihydroorotase activity Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' pyrimidine nucleobase biosynthetic process Source: UniProtKB
    2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    3. carbamoyl phosphate biosynthetic process Source: InterPro
    4. cellular response to drug Source: Ensembl
    5. cellular response to epidermal growth factor stimulus Source: Ensembl
    6. drug metabolic process Source: Ensembl
    7. embryo development Source: Ensembl
    8. female pregnancy Source: Ensembl
    9. glutamine catabolic process Source: InterPro
    10. lactation Source: Ensembl
    11. organ regeneration Source: Ensembl
    12. response to amine Source: Ensembl
    13. response to caffeine Source: Ensembl
    14. response to cortisol Source: Ensembl
    15. response to testosterone Source: Ensembl
    16. UTP biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Ligase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    UniPathwayiUPA00070; UER00115.
    UPA00070; UER00116.
    UPA00070; UER00117.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1916969. Cad.

    Subcellular locationi

    Cytoplasm By similarity. 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. cytosol Source: Ensembl
    2. neuronal cell body Source: Ensembl
    3. nuclear matrix Source: Ensembl
    4. protein complex Source: Ensembl
    5. terminal bouton Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 22252224CAD proteinPRO_0000425955Add
    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 PKABy similarity
    Modified residuei1411 – 14111N6-acetyllysineBy similarity
    Modified residuei1556 – 15561N6-carboxylysineBy similarity
    Modified residuei1859 – 18591Phosphoserine; by RPS6KB1 and PKABy 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. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiB2RQC6.

    Expressioni

    Gene expression databases

    ArrayExpressiB2RQC6.
    GenevestigatoriB2RQC6.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    IntActiB2RQC6. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliB2RQC6.
    SMRiB2RQC6. Positions 1460-1823.
    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

    eggNOGiCOG0458.
    GeneTreeiENSGT00390000015604.
    HOGENOMiHOG000234584.
    HOVERGENiHBG000279.
    InParanoidiB2RQC6.
    KOiK11540.
    OMAiKRIVTHA.
    OrthoDBiEOG7M6D6F.
    PhylomeDBiB2RQC6.
    TreeFamiTF105604.

    Family and domain databases

    Gene3Di1.10.1030.10. 1 hit.
    3.30.1490.20. 2 hits.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: B2RQC6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL     50
    VLTYPLIGNY GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA 100
    NCTLHEWLQQ RGIPGLQGVD TRELTKKLRE QGSLLGKLVQ KGTEPSALPF 150
    VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV 200
    TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL SEPNPRPVFG 250
    ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 300
    ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF 350
    DVFLETVREA AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG 400
    SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV 450
    YFLPITLHYV 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 DHTVKPVSDM 800
    ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL 850
    EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 900
    KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE 950
    FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM 1000
    DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK 1050
    FSRLLDTIGI SQPQWRELSD LESARQFCHT VGYPCVVRPS YVLSGAAMNV 1100
    AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGIVSAIA 1150
    ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 1200
    LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV 1250
    GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL 1300
    KAMLSTGFKI PEKNILLTIG 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 FTLFLGASSE NAGTLGAVAG 1550
    SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL 1600
    MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL 1650
    ERLGPGKGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP 1700
    PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV 1750
    EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL 1800
    VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH 1850
    LPPRIHRASD PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS 1900
    PQNLGSSGLL HPQMSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM 1950
    VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS 2000
    VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR PVINAGDGVG 2050
    EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 2100
    LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE 2150
    RFGSVQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR 2200
    AAYFRQAENG MYIRMALLAT VLGRF 2225
    Length:2,225
    Mass (Da):243,238
    Last modified:July 1, 2008 - v1
    Checksum:iE7E606A0F650ABB4
    GO
    Isoform 2 (identifier: B2RQC6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1962-2032: Missing.

    Show »
    Length:2,154
    Mass (Da):235,851
    Checksum:iA83FA6E22929070C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1962 – 203271Missing in isoform 2. 1 PublicationVSP_053912Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC109608 Genomic DNA. No translation available.
    CH466524 Genomic DNA. Translation: EDL37329.1.
    BC137856 mRNA. Translation: AAI37857.1.
    BC144972 mRNA. Translation: AAI44973.1.
    CCDSiCCDS19171.1. [B2RQC6-1]
    RefSeqiNP_001276451.1. NM_001289522.1. [B2RQC6-2]
    NP_076014.1. NM_023525.2. [B2RQC6-1]
    UniGeneiMm.305535.

    Genome annotation databases

    EnsembliENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629. [B2RQC6-1]
    ENSMUST00000170329; ENSMUSP00000130789; ENSMUSG00000013629. [B2RQC6-2]
    GeneIDi69719.
    KEGGimmu:69719.
    UCSCiuc008wwz.1. mouse. [B2RQC6-1]
    uc012duk.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC109608 Genomic DNA. No translation available.
    CH466524 Genomic DNA. Translation: EDL37329.1 .
    BC137856 mRNA. Translation: AAI37857.1 .
    BC144972 mRNA. Translation: AAI44973.1 .
    CCDSi CCDS19171.1. [B2RQC6-1 ]
    RefSeqi NP_001276451.1. NM_001289522.1. [B2RQC6-2 ]
    NP_076014.1. NM_023525.2. [B2RQC6-1 ]
    UniGenei Mm.305535.

    3D structure databases

    ProteinModelPortali B2RQC6.
    SMRi B2RQC6. Positions 1460-1823.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi B2RQC6. 3 interactions.

    Chemistry

    ChEMBLi CHEMBL2774.

    Proteomic databases

    MaxQBi B2RQC6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000013773 ; ENSMUSP00000013773 ; ENSMUSG00000013629 . [B2RQC6-1 ]
    ENSMUST00000170329 ; ENSMUSP00000130789 ; ENSMUSG00000013629 . [B2RQC6-2 ]
    GeneIDi 69719.
    KEGGi mmu:69719.
    UCSCi uc008wwz.1. mouse. [B2RQC6-1 ]
    uc012duk.1. mouse.

    Organism-specific databases

    CTDi 790.
    MGIi MGI:1916969. Cad.

    Phylogenomic databases

    eggNOGi COG0458.
    GeneTreei ENSGT00390000015604.
    HOGENOMi HOG000234584.
    HOVERGENi HBG000279.
    InParanoidi B2RQC6.
    KOi K11540.
    OMAi KRIVTHA.
    OrthoDBi EOG7M6D6F.
    PhylomeDBi B2RQC6.
    TreeFami TF105604.

    Enzyme and pathway databases

    UniPathwayi UPA00070 ; UER00115 .
    UPA00070 ; UER00116 .
    UPA00070 ; UER00117 .

    Miscellaneous databases

    ChiTaRSi cad. mouse.
    NextBioi 330178.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi B2RQC6.
    Genevestigatori B2RQC6.

    Family and domain databases

    Gene3Di 1.10.1030.10. 1 hit.
    3.30.1490.20. 2 hits.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.

    Entry informationi

    Entry nameiPYR1_MOUSE
    AccessioniPrimary (citable) accession number: B2RQC6
    Secondary accession number(s): B7ZN27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 19, 2014
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 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, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3