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P08955

- PYR1_MESAU

UniProt

P08955 - PYR1_MESAU

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Protein

CAD protein

Gene

CAD

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Zn2+By similarityNote: Binds 3 Zn(2+) 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
Complete GO annotation...

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
Complete GO annotation...

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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        10         20         30         40         50
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
60 70 80 90 100
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA
110 120 130 140 150
TCTLHEWLQQ HGIPGLQGVD TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF
160 170 180 190 200
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV
210 220 230 240 250
TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL SEPNPRPVFG
260 270 280 290 300
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
310 320 330 340 350
ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF
360 370 380 390 400
DVFLETVREA VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG
410 420 430 440 450
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
460 470 480 490 500
YFLPITPHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR
510 520 530 540 550
VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY
560 570 580 590 600
PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
610 620 630 640 650
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR
660 670 680 690 700
TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY
710 720 730 740 750
PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR
760 770 780 790 800
VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDV
810 820 830 840 850
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL
860 870 880 890 900
EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
910 920 930 940 950
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE
960 970 980 990 1000
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
1010 1020 1030 1040 1050
DIYELENPDG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
1060 1070 1080 1090 1100
FSRLLDTIGI SQPQWRELSD LESARQFCQT VGYPCVVRPS YVLSGAAMNV
1110 1120 1130 1140 1150
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGVVSAIA
1160 1170 1180 1190 1200
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
1210 1220 1230 1240 1250
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI
1260 1270 1280 1290 1300
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
1310 1320 1330 1340 1350
KAMLSTGFKI PKKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD
1360 1370 1380 1390 1400
FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LDQLAENHFE LVINLSMRGA
1410 1420 1430 1440 1450
GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK
1460 1470 1480 1490 1500
VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
1510 1520 1530 1540 1550
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG
1560 1570 1580 1590 1600
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL
1610 1620 1630 1640 1650
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL
1660 1670 1680 1690 1700
ERLGPGRGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP
1710 1720 1730 1740 1750
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV
1760 1770 1780 1790 1800
EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL
1810 1820 1830 1840 1850
VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH
1860 1870 1880 1890 1900
LPPRIHRASD PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS
1910 1920 1930 1940 1950
PQNLGSSGLL HPQTSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM
1960 1970 1980 1990 2000
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
2010 2020 2030 2040 2050
VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR PVINAGDGVG
2060 2070 2080 2090 2100
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
2110 2120 2130 2140 2150
LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
2160 2170 2180 2190 2200
RFGSTQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
2210 2220
AAYFRQAENG MYIRMALLAT VLGRF
Length:2,225
Mass (Da):243,128
Last modified:August 1, 1992 - v4
Checksum:i9F6EBA9BD4C6EC5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 140 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