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P08955 (PYR1_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CAD protein

Including the following 3 domains:

  1. Glutamine-dependent carbamoyl-phosphate synthase
    EC=6.3.5.5
  2. Aspartate carbamoyltransferase
    EC=2.1.3.2
  3. Dihydroorotase
    EC=3.5.2.3
Gene names
Name:CAD
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length2225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase). HAMAP-Rule MF_00001

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP-Rule MF_00001

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP-Rule MF_00001

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00001

Cofactor

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

Enzyme regulation

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction. HAMAP-Rule MF_00001

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP-Rule MF_00001

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.

Subunit structure

Homohexamer. Ref.9

Subcellular location

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. HAMAP-Rule MF_00001

Post-translational modification

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. HAMAP-Rule MF_00001

Miscellaneous

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

Sequence similarities

In the central section; belongs to the DHOase family.

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
Ligase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Direct protein sequencing
Multifunctional enzyme
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from direct assay PubMed 19472. Source: BHF-UCL

carbamoyl phosphate biosynthetic process

Inferred from electronic annotation. Source: InterPro

glutamine catabolic process

Inferred from electronic annotation. Source: InterPro

glutamine metabolic process

Inferred from direct assay PubMed 19472. Source: BHF-UCL

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 11986331. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay PubMed 11986331. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15890648. Source: MGI

cytosol

Inferred from direct assay PubMed 15890648. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 15890648. Source: BHF-UCL

nuclear matrix

Inferred from direct assay PubMed 15890648. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 15890648. Source: MGI

   Molecular_functionATP binding

Inferred from direct assay PubMed 11986331. Source: BHF-UCL

UTP binding

Inferred from direct assay PubMed 11986331. Source: MGI

aspartate binding

Inferred from direct assay PubMed 19472. Source: BHF-UCL

aspartate carbamoyltransferase activity

Inferred from direct assay PubMed 19472. Source: BHF-UCL

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

Inferred from direct assay PubMed 19472. Source: BHF-UCL

dihydroorotase activity

Inferred from direct assay PubMed 19472. Source: BHF-UCL

protein kinase activity

Inferred from direct assay PubMed 11986331. Source: BHF-UCL

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 22252224CAD protein HAMAP-Rule MF_00001
PRO_0000199507

Regions

Domain177 – 363187Glutamine amidotransferase type-1
Domain519 – 711193ATP-grasp 1
Domain1052 – 1243192ATP-grasp 2
Region2 – 365364GATase (Glutamine amidotransferase) HAMAP-Rule MF_00001
Region366 – 39429Linker HAMAP-Rule MF_00001
Region395 – 14551061CPSase (Carbamoyl-phosphate synthase) HAMAP-Rule MF_00001
Region395 – 933539CPSase A HAMAP-Rule MF_00001
Region934 – 1455522CPSase B HAMAP-Rule MF_00001
Region1456 – 1788333DHOase (dihydroorotase) HAMAP-Rule MF_00001
Region1789 – 1917129Linker HAMAP-Rule MF_00001
Region1918 – 2225308ATCase (Aspartate transcarbamylase) HAMAP-Rule MF_00001

Sites

Active site2521For GATase activity By similarity
Active site3361For GATase activity By similarity
Active site3381For GATase activity By similarity
Metal binding14711Zinc 1; via tele nitrogen By similarity
Metal binding14711Zinc 2; via pros nitrogen By similarity
Metal binding14731Zinc 1; via tele nitrogen By similarity
Metal binding15561Zinc 1; via carbamate group By similarity
Metal binding15561Zinc 3; via carbamate group By similarity
Metal binding15901Zinc 3; via pros nitrogen By similarity
Metal binding16131Zinc 2 By similarity
Metal binding16141Zinc 3; via tele nitrogen By similarity
Metal binding16371Zinc 2 By similarity
Metal binding16861Zinc 1 By similarity
Binding site14751N-carbamoyl-L-aspartate By similarity
Binding site15051N-carbamoyl-L-aspartate By similarity
Binding site16611N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygen By similarity
Binding site16861N-carbamoyl-L-aspartate By similarity
Binding site16901N-carbamoyl-L-aspartate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4561Phosphothreonine; by MAPK1 By similarity
Modified residue7471N6-acetyllysine By similarity
Modified residue14061Phosphoserine; by PKA Ref.11
Modified residue14111N6-acetyllysine By similarity
Modified residue15561N6-carboxylysine By similarity
Modified residue18591Phosphoserine; by RPS6KB1 and PKA By similarity
Modified residue18731Phosphoserine; by PKC; in vitro By similarity
Modified residue18841Phosphothreonine By similarity
Modified residue19001Phosphoserine By similarity

Experimental info

Mutagenesis14061S → A: No effect on enzyme kinetics. Ref.11
Mutagenesis14061S → D: Increases CPSase activity and reduces sensitivy to feedback inhibition by UTP. Ref.11

Sequences

Sequence LengthMass (Da)Tools
P08955 [UniParc].

Last modified August 1, 1992. Version 4.
Checksum: 9F6EBA9BD4C6EC5A

FASTA2,225243,128
        10         20         30         40         50         60 
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY 

        70         80         90        100        110        120 
GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA TCTLHEWLQQ HGIPGLQGVD 

       130        140        150        160        170        180 
TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA 

       190        200        210        220        230        240 
LDCGLKYNQI RCLCQLGAEV TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL 

       250        260        270        280        290        300 
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 

       310        320        330        340        350        360 
ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA 

       370        380        390        400        410        420 
VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI 

       430        440        450        460        470        480 
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT 

       490        500        510        520        530        540 
ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ 

       550        560        570        580        590        600 
AQAAAERLGY PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI 

       610        620        630        640        650        660 
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR TAIKVTQHLG 

       670        680        690        700        710        720 
IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN 

       730        740        750        760        770        780 
SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL 

       790        800        810        820        830        840 
RMVDENCVGF DHTVKPVSDV ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM 

       850        860        870        880        890        900 
KRIVTHAQLL EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 

       910        920        930        940        950        960 
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ 

       970        980        990       1000       1010       1020 
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPDG VILSMGGQLP 

      1030       1040       1050       1060       1070       1080 
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT 

      1090       1100       1110       1120       1130       1140 
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV 

      1150       1160       1170       1180       1190       1200 
ACDGVVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 

      1210       1220       1230       1240       1250       1260 
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI GLMTGSGVVG 

      1270       1280       1290       1300       1310       1320 
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG 

      1330       1340       1350       1360       1370       1380 
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI 

      1390       1400       1410       1420       1430       1440 
LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL 

      1450       1460       1470       1480       1490       1500 
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV 

      1510       1520       1530       1540       1550       1560 
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG SAAGLKLYLN 

      1570       1580       1590       1600       1610       1620 
ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE 

      1630       1640       1650       1660       1670       1680 
ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGRGEV RPELGSREDM EALWENMAVI 

      1690       1700       1710       1720       1730       1740 
DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF 

      1750       1760       1770       1780       1790       1800 
HLPLQEDTYV EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL 

      1810       1820       1830       1840       1850       1860 
VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD 

      1870       1880       1890       1900       1910       1920 
PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQTSPLLHS 

      1930       1940       1950       1960       1970       1980 
LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF 

      1990       2000       2010       2020       2030       2040 
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR 

      2050       2060       2070       2080       2090       2100 
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 

      2110       2120       2130       2140       2150       2160 
LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA 

      2170       2180       2190       2200       2210       2220 
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT 


VLGRF 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA23443. A38653.

3D structure databases

ProteinModelPortalP08955.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM38.972.

Proteomic databases

PRIDEP08955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000279.

Enzyme and pathway databases

BRENDA3.5.2.3. 3239.
SABIO-RKP08955.
UniPathwayUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.

Family and domain databases

Gene3D1.10.1030.10. 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.
3.50.30.20. 1 hit.
HAMAPMF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProIPR006132. 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.
IPR002195. Dihydroorotase_CS.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamPF00289. 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]
PRINTSPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
SSF53671. SSF53671. 1 hit.
TIGRFAMsTIGR00670. asp_carb_tr. 1 hit.
TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Entry information

Entry namePYR1_MESAU
AccessionPrimary (citable) accession number: P08955
Secondary accession number(s): P70108
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways