UniProtKB - P08955 (PYR1_MESAU)
Protein
CAD protein
Gene
CAD
Organism
Mesocricetus auratus (Golden hamster)
Status
Functioni
This protein is a 'fusion' protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).1 Publication
Miscellaneous
GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
Catalytic activityi
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate1 PublicationEC:6.3.5.51 Publication
- EC:2.1.3.21 Publication
- EC:3.5.2.31 Publication
Cofactori
Protein has several cofactor binding sites:- Zn2+By similarityNote: Binds 3 Zn2+ ions per subunit (for dihydroorotase activity).By similarity
- Mg2+PROSITE-ProRule annotation, Mn2+PROSITE-ProRule annotationNote: Binds 4 magnesium or manganese ions per subunit.PROSITE-ProRule annotation
Activity 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.
: UMP biosynthesis via de novo pathway Pathwayi
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:
- CAD protein (CAD)
- CAD protein (CAD)
- Aspartate carbamoyltransferase (Cad), CAD protein (CAD), Aspartate carbamoyltransferase (Cad)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 252 | Nucleophile; for GATase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 336 | For GATase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 338 | For GATase activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 668 | Magnesium or manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 682 | Magnesium or manganese 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 682 | Magnesium or manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 684 | Magnesium or manganese 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1202 | Magnesium or manganese 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1214 | Magnesium or manganese 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1214 | Magnesium or manganese 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1216 | Magnesium or manganese 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1471 | Zinc 1; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 1471 | Zinc 2; via pros nitrogenBy similarity | 1 | |
Metal bindingi | 1473 | Zinc 1; via tele nitrogenBy similarity | 1 | |
Binding sitei | 1475 | N-carbamoyl-L-aspartateBy similarity | 1 | |
Binding sitei | 1505 | N-carbamoyl-L-aspartateBy similarity | 1 | |
Metal bindingi | 1556 | Zinc 1; via carbamate groupBy similarity | 1 | |
Metal bindingi | 1556 | Zinc 3; via carbamate groupBy similarity | 1 | |
Metal bindingi | 1590 | Zinc 3; via pros nitrogenBy similarity | 1 | |
Metal bindingi | 1613 | Zinc 2By similarity | 1 | |
Metal bindingi | 1614 | Zinc 3; via tele nitrogenBy similarity | 1 | |
Metal bindingi | 1637 | Zinc 2By similarity | 1 | |
Binding sitei | 1661 | N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 1686 | Zinc 1By similarity | 1 | |
Binding sitei | 1686 | N-carbamoyl-L-aspartateBy similarity | 1 | |
Binding sitei | 1690 | N-carbamoyl-L-aspartateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 545 – 600 | ATPPROSITE-ProRule annotationAdd BLAST | 56 | |
Nucleotide bindingi | 1078 – 1135 | ATPPROSITE-ProRule annotationAdd BLAST | 58 |
GO - Molecular functioni
- aspartate binding Source: BHF-UCL
- aspartate carbamoyltransferase activity Source: BHF-UCL
- ATP binding Source: BHF-UCL
- carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: BHF-UCL
- dihydroorotase activity Source: BHF-UCL
- protein kinase activity Source: BHF-UCL
- UTP binding Source: MGI
- zinc ion binding Source: UniProtKB
GO - Biological processi
- 'de novo' pyrimidine nucleobase biosynthetic process Source: BHF-UCL
- 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
- glutamine metabolic process Source: BHF-UCL
- peptidyl-threonine phosphorylation Source: BHF-UCL
- protein autophosphorylation Source: BHF-UCL
Keywordsi
Molecular function | Allosteric enzyme, Hydrolase, Ligase, Multifunctional enzyme, Transferase |
Biological process | Pyrimidine biosynthesis |
Ligand | ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.5.2.3, 3239 |
SABIO-RKi | P08955 |
UniPathwayi | UPA00070;UER00115 UPA00070;UER00116 UPA00070;UER00117 |
Protein family/group databases
MEROPSi | M38.972 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:CAD |
Organismi | Mesocricetus auratus (Golden hamster) |
Taxonomic identifieri | 10036 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Cricetidae › Cricetinae › Mesocricetus |
Proteomesi |
|
Subcellular locationi
Cytosol
- cytosol Source: BHF-UCL
Mitochondrion
- mitochondrion Source: BHF-UCL
Nucleus
- nuclear matrix Source: BHF-UCL
- nucleus Source: MGI
Other locations
- cytoplasm Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1406 | S → A: No effect on enzyme kinetics. 1 Publication | 1 | |
Mutagenesisi | 1406 | S → D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000199507 | 2 – 2225 | CAD proteinAdd BLAST | 2224 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 456 | Phosphothreonine; by MAPK1By similarity | 1 | |
Modified residuei | 747 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1038 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1406 | Phosphoserine; by PKA1 Publication | 1 | |
Modified residuei | 1411 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1556 | N6-carboxylysineBy similarity | 1 | |
Modified residuei | 1859 | Phosphoserine; by RPS6KB1 and PKABy similarity | 1 | |
Modified residuei | 1873 | Phosphoserine; by PKC; in vitroBy similarity | 1 | |
Modified residuei | 1884 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1900 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1938 | PhosphoserineBy similarity | 1 |
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 sensitivity to feedback inhibition by UTP.By similarity1 Publication
Keywords - PTMi
Acetylation, PhosphoproteinPTM databases
iPTMneti | P08955 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 177 – 363 | Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST | 187 | |
Domaini | 519 – 711 | ATP-grasp 1PROSITE-ProRule annotationAdd BLAST | 193 | |
Domaini | 1052 – 1243 | ATP-grasp 2PROSITE-ProRule annotationAdd BLAST | 192 | |
Domaini | 1308 – 1462 | MGS-likePROSITE-ProRule annotationAdd BLAST | 155 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 365 | GATase (Glutamine amidotransferase)1 PublicationAdd BLAST | 364 | |
Regioni | 366 – 394 | Linker1 PublicationAdd BLAST | 29 | |
Regioni | 395 – 1455 | CPSase (Carbamoyl-phosphate synthase)1 PublicationAdd BLAST | 1061 | |
Regioni | 395 – 933 | CPSase A1 PublicationAdd BLAST | 539 | |
Regioni | 934 – 1455 | CPSase B1 PublicationAdd BLAST | 522 | |
Regioni | 1456 – 1788 | DHOase (dihydroorotase)1 PublicationAdd BLAST | 333 | |
Regioni | 1789 – 1917 | Linker1 PublicationAdd BLAST | 129 | |
Regioni | 1918 – 2225 | ATCase (Aspartate transcarbamylase)1 PublicationAdd BLAST | 308 |
Sequence similaritiesi
In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated
Keywords - Domaini
Glutamine amidotransferase, RepeatPhylogenomic databases
eggNOGi | KOG0370, Eukaryota |
Family and domain databases
CDDi | cd01744, GATase1_CPSase, 1 hit |
Gene3Di | 1.10.1030.10, 1 hit 3.30.1490.20, 1 hit 3.40.50.1370, 2 hits 3.40.50.1380, 1 hit 3.40.50.880, 1 hit 3.50.30.20, 1 hit |
HAMAPi | MF_00001, Asp_carb_tr, 1 hit MF_01209, CPSase_S_chain, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR006132, Asp/Orn_carbamoyltranf_P-bd IPR006130, Asp/Orn_carbamoylTrfase IPR036901, Asp/Orn_carbamoylTrfase_sf IPR002082, Asp_carbamoyltransf IPR006131, Asp_carbamoyltransf_Asp/Orn-bd IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR006275, CarbamoylP_synth_lsu IPR005480, CarbamoylP_synth_lsu_oligo IPR036897, CarbamoylP_synth_lsu_oligo_sf IPR006274, CarbamoylP_synth_ssu IPR002474, CarbamoylP_synth_ssu_N IPR036480, CarbP_synth_ssu_N_sf IPR005479, CbamoylP_synth_lsu-like_ATP-bd IPR005483, CbamoylP_synth_lsu_CPSase_dom IPR029062, Class_I_gatase-like IPR035686, CPSase_GATase1 IPR002195, Dihydroorotase_CS IPR017926, GATASE IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase IPR011607, MGS-like_dom IPR036914, MGS-like_dom_sf IPR016185, PreATP-grasp_dom_sf |
Pfami | View protein in Pfam PF01979, 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 |
PRINTSi | PR00100, AOTCASE PR00098, CPSASE |
SMARTi | View protein in SMART SM01096, CPSase_L_D3, 1 hit SM01097, CPSase_sm_chain, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF48108, 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 |
TIGRFAMsi | TIGR00670, asp_carb_tr, 1 hit TIGR01369, CPSaseII_lrg, 1 hit TIGR01368, CPSaseIIsmall, 1 hit |
PROSITEi | View protein in PROSITE 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 PS51855, MGS, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P08955-1 [UniParc]FASTAAdd to basket
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
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 |
Similar proteinsi
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
SMRi | P08955 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10036.XP_005073594.1 |
Protein family/group databases
MEROPSi | M38.972 |
PTM databases
iPTMneti | P08955 |
Phylogenomic databases
eggNOGi | KOG0370, Eukaryota |
Enzyme and pathway databases
UniPathwayi | UPA00070;UER00115 UPA00070;UER00116 UPA00070;UER00117 |
BRENDAi | 3.5.2.3, 3239 |
SABIO-RKi | P08955 |
Family and domain databases
CDDi | cd01744, GATase1_CPSase, 1 hit |
Gene3Di | 1.10.1030.10, 1 hit 3.30.1490.20, 1 hit 3.40.50.1370, 2 hits 3.40.50.1380, 1 hit 3.40.50.880, 1 hit 3.50.30.20, 1 hit |
HAMAPi | MF_00001, Asp_carb_tr, 1 hit MF_01209, CPSase_S_chain, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR006132, Asp/Orn_carbamoyltranf_P-bd IPR006130, Asp/Orn_carbamoylTrfase IPR036901, Asp/Orn_carbamoylTrfase_sf IPR002082, Asp_carbamoyltransf IPR006131, Asp_carbamoyltransf_Asp/Orn-bd IPR011761, ATP-grasp IPR013815, ATP_grasp_subdomain_1 IPR006275, CarbamoylP_synth_lsu IPR005480, CarbamoylP_synth_lsu_oligo IPR036897, CarbamoylP_synth_lsu_oligo_sf IPR006274, CarbamoylP_synth_ssu IPR002474, CarbamoylP_synth_ssu_N IPR036480, CarbP_synth_ssu_N_sf IPR005479, CbamoylP_synth_lsu-like_ATP-bd IPR005483, CbamoylP_synth_lsu_CPSase_dom IPR029062, Class_I_gatase-like IPR035686, CPSase_GATase1 IPR002195, Dihydroorotase_CS IPR017926, GATASE IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase IPR011607, MGS-like_dom IPR036914, MGS-like_dom_sf IPR016185, PreATP-grasp_dom_sf |
Pfami | View protein in Pfam PF01979, 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 |
PRINTSi | PR00100, AOTCASE PR00098, CPSASE |
SMARTi | View protein in SMART SM01096, CPSase_L_D3, 1 hit SM01097, CPSase_sm_chain, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF48108, 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 |
TIGRFAMsi | TIGR00670, asp_carb_tr, 1 hit TIGR01369, CPSaseII_lrg, 1 hit TIGR01368, CPSaseIIsmall, 1 hit |
PROSITEi | View protein in PROSITE 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 PS51855, MGS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PYR1_MESAU | |
Accessioni | P08955Primary (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: | December 2, 2020 | |
This is version 171 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families