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Protein

CAD protein

Gene

Cad

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).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

Zn2+By similarityNote: Binds 3 Zn2+ 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: UMP biosynthesis via de novo pathway

This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (Cad)
  2. CAD protein (Cad)
  3. CAD protein (Cad)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei252For GATase activityBy similarity1
Active sitei336For GATase activityBy similarity1
Active sitei338For GATase activityBy similarity1
Metal bindingi1471Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1471Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1473Zinc 1; via tele nitrogenBy similarity1
Binding sitei1475N-carbamoyl-L-aspartateBy similarity1
Binding sitei1505N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1556Zinc 1; via carbamate groupBy similarity1
Metal bindingi1556Zinc 3; via carbamate groupBy similarity1
Metal bindingi1590Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1613Zinc 2By similarity1
Metal bindingi1614Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1637Zinc 2By similarity1
Binding sitei1661N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1686Zinc 1By similarity1
Binding sitei1686N-carbamoyl-L-aspartateBy similarity1
Binding sitei1690N-carbamoyl-L-aspartateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Hydrolase, Ligase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-500753. Pyrimidine biosynthesis.
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
Proteomesi
  • UP000000589 Componenti: 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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2774.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00004259552 – 2225CAD proteinAdd BLAST2224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei456Phosphothreonine; by MAPK1By similarity1
Modified residuei747N6-acetyllysineBy similarity1
Modified residuei1038PhosphoserineBy similarity1
Modified residuei1406Phosphoserine; by PKABy similarity1
Modified residuei1411N6-acetyllysineBy similarity1
Modified residuei1556N6-carboxylysineBy similarity1
Modified residuei1859PhosphoserineCombined sources1
Modified residuei1884PhosphothreonineBy similarity1
Modified residuei1900PhosphoserineBy similarity1
Modified residuei1938PhosphoserineBy similarity1

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

EPDiB2RQC6.
MaxQBiB2RQC6.
PaxDbiB2RQC6.
PeptideAtlasiB2RQC6.
PRIDEiB2RQC6.

PTM databases

iPTMnetiB2RQC6.
PhosphoSitePlusiB2RQC6.
SwissPalmiB2RQC6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000013629.
ExpressionAtlasiB2RQC6. baseline and differential.
GenevisibleiB2RQC6. MM.

Interactioni

Subunit structurei

Homohexamer. Interacts with CIPC.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213636. 5 interactors.
DIPiDIP-61412N.
IntActiB2RQC6. 6 interactors.
STRINGi10090.ENSMUSP00000013773.

Chemistry databases

BindingDBiB2RQC6.

Structurei

3D structure databases

ProteinModelPortaliB2RQC6.
SMRiB2RQC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini177 – 363Glutamine amidotransferase type-1Add BLAST187
Domaini519 – 711ATP-grasp 1Add BLAST193
Domaini1052 – 1243ATP-grasp 2Add BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 365GATase (Glutamine amidotransferase)Add BLAST364
Regioni366 – 394LinkerAdd BLAST29
Regioni395 – 1455CPSase (Carbamoyl-phosphate synthase)Add BLAST1061
Regioni395 – 933CPSase AAdd BLAST539
Regioni934 – 1455CPSase BAdd BLAST522
Regioni1456 – 1788DHOase (dihydroorotase)Add BLAST333
Regioni1789 – 1917LinkerAdd BLAST129
Regioni1918 – 2225ATCase (Aspartate transcarbamylase)Add BLAST308

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
HOVERGENiHBG000279.
InParanoidiB2RQC6.
KOiK11540.
OMAiLYSVRLN.
OrthoDBiEOG091G00DC.
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. 1 hit.
MF_01209. CPSase_S_chain. 1 hit.
InterProiIPR006680. Amidohydro-rel.
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.
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.
IPR032466. Metal_Hydrolase.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
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.
SSF51556. SSF51556. 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. AlignAdd to basket

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

        10         20         30         40         50
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
60 70 80 90 100
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA
110 120 130 140 150
NCTLHEWLQQ RGIPGLQGVD TRELTKKLRE QGSLLGKLVQ KGTEPSALPF
160 170 180 190 200
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV
210 220 230 240 250
TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL SEPNPRPVFG
260 270 280 290 300
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
310 320 330 340 350
ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF
360 370 380 390 400
DVFLETVREA AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG
410 420 430 440 450
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
460 470 480 490 500
YFLPITLHYV 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 DHTVKPVSDM
810 820 830 840 850
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL
860 870 880 890 900
EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
910 920 930 940 950
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE
960 970 980 990 1000
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
1010 1020 1030 1040 1050
DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
1060 1070 1080 1090 1100
FSRLLDTIGI SQPQWRELSD LESARQFCHT VGYPCVVRPS YVLSGAAMNV
1110 1120 1130 1140 1150
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGIVSAIA
1160 1170 1180 1190 1200
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
1210 1220 1230 1240 1250
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV
1260 1270 1280 1290 1300
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
1310 1320 1330 1340 1350
KAMLSTGFKI PEKNILLTIG 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 FTLFLGASSE NAGTLGAVAG
1560 1570 1580 1590 1600
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL
1610 1620 1630 1640 1650
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL
1660 1670 1680 1690 1700
ERLGPGKGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP
1710 1720 1730 1740 1750
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV
1760 1770 1780 1790 1800
EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
1810 1820 1830 1840 1850
VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH
1860 1870 1880 1890 1900
LPPRIHRASD PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS
1910 1920 1930 1940 1950
PQNLGSSGLL HPQMSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM
1960 1970 1980 1990 2000
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
2010 2020 2030 2040 2050
VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR PVINAGDGVG
2060 2070 2080 2090 2100
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
2110 2120 2130 2140 2150
LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
2160 2170 2180 2190 2200
RFGSVQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
2210 2220
AAYFRQAENG MYIRMALLAT VLGRF
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0539121962 – 2032Missing in isoform 2. 1 PublicationAdd BLAST71

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS80246.1. [B2RQC6-2]
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]
ENSMUST00000201182; ENSMUSP00000144684; ENSMUSG00000013629. [B2RQC6-2]
GeneIDi69719.
KEGGimmu:69719.
UCSCiuc008wwz.2. mouse. [B2RQC6-1]
uc012duk.2. mouse. [B2RQC6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS80246.1. [B2RQC6-2]
RefSeqiNP_001276451.1. NM_001289522.1. [B2RQC6-2]
NP_076014.1. NM_023525.2. [B2RQC6-1]
UniGeneiMm.305535.

3D structure databases

ProteinModelPortaliB2RQC6.
SMRiB2RQC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213636. 5 interactors.
DIPiDIP-61412N.
IntActiB2RQC6. 6 interactors.
STRINGi10090.ENSMUSP00000013773.

Chemistry databases

BindingDBiB2RQC6.
ChEMBLiCHEMBL2774.

PTM databases

iPTMnetiB2RQC6.
PhosphoSitePlusiB2RQC6.
SwissPalmiB2RQC6.

Proteomic databases

EPDiB2RQC6.
MaxQBiB2RQC6.
PaxDbiB2RQC6.
PeptideAtlasiB2RQC6.
PRIDEiB2RQC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629. [B2RQC6-1]
ENSMUST00000201182; ENSMUSP00000144684; ENSMUSG00000013629. [B2RQC6-2]
GeneIDi69719.
KEGGimmu:69719.
UCSCiuc008wwz.2. mouse. [B2RQC6-1]
uc012duk.2. mouse. [B2RQC6-2]

Organism-specific databases

CTDi790.
MGIiMGI:1916969. Cad.

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
HOVERGENiHBG000279.
InParanoidiB2RQC6.
KOiK11540.
OMAiLYSVRLN.
OrthoDBiEOG091G00DC.
PhylomeDBiB2RQC6.
TreeFamiTF105604.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.
ReactomeiR-MMU-500753. Pyrimidine biosynthesis.

Miscellaneous databases

ChiTaRSiCad. mouse.
PROiB2RQC6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000013629.
ExpressionAtlasiB2RQC6. baseline and differential.
GenevisibleiB2RQC6. MM.

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. 1 hit.
MF_01209. CPSase_S_chain. 1 hit.
InterProiIPR006680. Amidohydro-rel.
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.
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.
IPR032466. Metal_Hydrolase.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
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.
SSF51556. SSF51556. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.