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Protein

CAD protein

Gene

r

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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).

Miscellaneous

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

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.1 Publication
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.By similarity
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion 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

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 (r)
  2. CAD protein (r)
  3. CAD protein (r)
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 sitei269Nucleophile; for GATase activityPROSITE-ProRule annotation1
Active sitei353For GATase activityPROSITE-ProRule annotation1
Active sitei355For GATase activityPROSITE-ProRule annotation1
Metal bindingi678Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi692Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi692Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi694Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1228Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1228Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1230Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1486Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1486Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1488Zinc 1; via tele nitrogenBy similarity1
Binding sitei1490N-carbamoyl-L-aspartateBy similarity1
Binding sitei1520N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1571Zinc 1; via carbamate groupBy similarity1
Metal bindingi1571Zinc 3; via carbamate groupBy similarity1
Metal bindingi1605Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1628Zinc 2By similarity1
Metal bindingi1629Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1652Zinc 2By similarity1
Binding sitei1676N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1701Zinc 1By similarity1
Binding sitei1701N-carbamoyl-L-aspartateBy similarity1
Binding sitei1705N-carbamoyl-L-aspartateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi555 – 610ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1092 – 1149ATPPROSITE-ProRule annotationAdd BLAST58

GO - Molecular functioni

  • aspartate carbamoyltransferase activity Source: FlyBase
  • ATP binding Source: FlyBase
  • carbamoyl-phosphate synthase (ammonia) activity Source: GO_Central
  • carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: FlyBase
  • dihydroorotase activity Source: FlyBase
  • glutamine binding Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: FlyBase
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • arginine biosynthetic process Source: GO_Central
  • glutamine metabolic process Source: FlyBase
  • urea cycle Source: GO_Central

Keywordsi

Molecular functionHydrolase, Ligase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi6.3.5.5 1994
ReactomeiR-DME-500753 Pyrimidine biosynthesis
UniPathwayiUPA00070; UER00115
UPA00070; UER00116
UPA00070; UER00117

Protein family/group databases

MEROPSiM38.972

Names & Taxonomyi

Protein namesi
Recommended name:
CAD protein
Alternative name(s):
Protein rudimentary
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.51 Publication)
Aspartate carbamoyltransferase (EC:2.1.3.2By similarity)
Dihydroorotase (EC:3.5.2.3By similarity)
Gene namesi
Name:r
ORF Names:CG18572
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi

Organism-specific databases

FlyBaseiFBgn0003189 r

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1167E → K: Severely diminishes UTP inhibition of CPSase; in Su(b). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001995051 – 2224CAD proteinAdd BLAST2224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1571N6-carboxylysineBy similarity1
Modified residuei1883Phosphoserine1 Publication1
Modified residuei1885Phosphoserine1 Publication1
Modified residuei1892Phosphoserine1 Publication1
Modified residuei1894Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05990
PRIDEiP05990

PTM databases

iPTMnetiP05990

Expressioni

Gene expression databases

BgeeiFBgn0003189
ExpressionAtlasiP05990 baseline and differential
GenevisibleiP05990 DM

Interactioni

Protein-protein interaction databases

BioGridi58976, 39 interactors
IntActiP05990, 8 interactors
MINTiP05990
STRINGi7227.FBpp0088675

Structurei

3D structure databases

ProteinModelPortaliP05990
SMRiP05990
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini195 – 380Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST186
Domaini529 – 721ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini1066 – 1257ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192
Domaini1322 – 1477MGS-likePROSITE-ProRule annotationAdd BLAST156

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 369GATase (Glutamine amidotransferase)By similarityAdd BLAST369
Regioni370 – 415LinkerBy similarityAdd BLAST46
Regioni416 – 1470CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1055
Regioni1471 – 1484LinkerBy similarityAdd BLAST14
Regioni1485 – 1800DHOase (dihydroorotase)By similarityAdd BLAST316
Regioni1801 – 1912LinkerBy similarityAdd BLAST112
Regioni1913 – 2224ATCase (Aspartate transcarbamylase)By similarityAdd BLAST312

Sequence similaritiesi

In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiKOG0370 Eukaryota
COG0458 LUCA
COG0505 LUCA
COG0540 LUCA
InParanoidiP05990
KOiK11540
OMAiNIPCTSM
OrthoDBiEOG091G00DC
PhylomeDBiP05990

Family and domain databases

CDDicd01744 GATase1_CPSase, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 3 hits
3.40.50.1380, 1 hit
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
InterProiView 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
PfamiView 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
PRINTSiPR00100 AOTCASE
PR00101 ATCASE
PR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM01097 CPSase_sm_chain, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF51338 SSF51338, 2 hits
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
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00097 CARBAMOYLTRANSFERASE, 1 hit
PS00866 CPSASE_1, 1 hit
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

Sequencei

Sequence statusi: Complete.

P05990-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA
60 70 80 90 100
LTDRSYSGQI LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV
110 120 130 140 150
VGEVAEEAFH WRKWKTLPDW LKQHKVPGIQ DIDTRALTKK LREQGSMLGK
160 170 180 190 200
IVYEKPPVEG LPKSSFVDPN VRNLAKECSV KERQVYGNPN GKGPRIAILD
210 220 230 240 250
CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG PGNPESCDQI
260 270 280 290 300
VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR
310 320 330 340 350
ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV
360 370 380 390 400
QFHPEHHAGP QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP
410 420 430 440 450
VMPRKVLILG SGGLSIGQAG EFDYSGSQAI KAMRESNIQT VLINPNIATV
460 470 480 490 500
QTSKGMADKC YFLPLTPHYV EQVIKSERPN GVLLTFGGQT ALNCGVQLER
510 520 530 540 550
AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA PSEAVYSVAQ
560 570 580 590 600
ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV
610 620 630 640 650
DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL
660 670 680 690 700
SDREYQMLRS TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS
710 720 730 740 750
SALASKATGY PLAYVAAKLA LGLPLPDIKN SVTGNTTACF EPSLDYCVVK
760 770 780 790 800
IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG RNFEEAFQKA LRMVDSDVLG
810 820 830 840 850
FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE LHQLTNIDYW
860 870 880 890 900
FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA
910 920 930 940 950
VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI
960 970 980 990 1000
VVGSGVYRIG SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC
1010 1020 1030 1040 1050
DRLYFEEISF EVVMDIYEME NSEGIILSMG GQLPNNIAMD LHRQQAKVLG
1060 1070 1080 1090 1100
TSPESIDCAE NRFKFSRMLD RKGILQPRWK ELTNLQSAIE FCEEVGYPCL
1110 1120 1130 1140 1150
VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS KFLTEAKEID
1160 1170 1180 1190 1200
VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT
1210 1220 1230 1240 1250
CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA
1260 1270 1280 1290 1300
TATRAIVGLD VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG
1310 1320 1330 1340 1350
EVACFGDNRY EAYLKAMMST GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA
1360 1370 1380 1390 1400
KMGYKLYASM GTGDFYAEHG VNVESVQWTF DKTTPDDING ELRHLAEFLA
1410 1420 1430 1440 1450
NKQFDLVINL PMSGGGARRV SSFMTHGYRT RRLAVDYSIP LVTDVKCTKL
1460 1470 1480 1490 1500
LVESMRMNGG KPPMKTHTDC MTSRRIVKLP GFIDVHVHLR EPGATHKEDF
1510 1520 1530 1540 1550
ASGTAAALAG GVTLVCAMPN TNPSIVDRET FTQFQELAKA GARCDYALYV
1560 1570 1580 1590 1600
GASDDNWAQV NELASHACGL KMYLNDTFGT LKLSDMTSWQ RHLSHWPKRS
1610 1620 1630 1640 1650
PIVCHAERQS TAAVIMLAHL LDRSVHICHV ARKEEIQLIR SAKEKGVKVT
1660 1670 1680 1690 1700
CEVCPHHLFL STKDVERLGH GMSEVRPLLC SPEDQEALWE NIDYIDVFAT
1710 1720 1730 1740 1750
DHAPHTLAEK RSERPPPGFP GVETILPLLL QAVHEGRLTM EDIKRKFHRN
1760 1770 1780 1790 1800
PKIIFNLPDQ AQTYVEVDLD EEWTITGNEM KSKSGWTPFE GTKVKGRVHR
1810 1820 1830 1840 1850
VVLRGEVAFV DGQVLVQPGF GQNVRPKQSP LASEASQDLL PSDNDANDTF
1860 1870 1880 1890 1900
TRLLTSEGPG GGVHGISTKV HFVDGANFLR PNSPSPRIRL DSASNTTLRE
1910 1920 1930 1940 1950
YLQRTTNSNP VAHSLMGKHI LAVDMFNKDH LNDIFNLAQL LKLRGTKDRP
1960 1970 1980 1990 2000
VDELLPGKIM ASVFYEVSTR TQCSFAAAML RLGGRVISMD NITSSVKKGE
2010 2020 2030 2040 2050
SLEDSIKVVS SYADVVVLRH PSPGAVARAA TFSRKPLINA GDGVGEHPTQ
2060 2070 2080 2090 2100
ALLDIFTIRE EFGTVNGLTI TMVGDLKNGR TVHSLARLLT LYNVNLQYVA
2110 2120 2130 2140 2150
PNSLQMPDEV VQFVHQRGVK QLFARDLKNV LPDTDVLYMT RIQRERFDNV
2160 2170 2180 2190 2200
EDYEKCCGHL VLTPEHMMRA KKRSIVLHPL PRLNEISREI DSDPRAAYFR
2210 2220
QAEYGMYIRM ALLAMVVGGR NTAL
Length:2,224
Mass (Da):246,672
Last modified:October 25, 2005 - v3
Checksum:iF89DEAD44FEFAEC6
GO

Sequence cautioni

The sequence AAA28873 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence AAL90298 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA27509 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27510 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27511 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA27513 differs from that shown. Various problems, including DNA not present in the genome.Curated
The sequence CAA28502 differs from that shown. Various problems, including DNA not present in the genome.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34F → V in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti58G → A in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti172 – 173RN → QD in CAA27509 (PubMed:3023623).Curated2
Sequence conflicti220 – 221LL → FV in CAA27509 (PubMed:3023623).Curated2
Sequence conflicti288Y → I in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti394P → L in CAA27509 (PubMed:3023623).Curated1
Sequence conflicti2192S → L in CAA27513 (PubMed:3023623).Curated1
Sequence conflicti2222 – 2224TAL → RRS in CAA27513 (PubMed:3023623).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04813 Genomic DNA Translation: CAA28502.1 Sequence problems.
X03875 Genomic DNA Translation: CAA27509.1 Sequence problems.
X03876 Genomic DNA Translation: CAA27510.1 Sequence problems.
X03877 Genomic DNA Translation: CAA27511.1 Sequence problems.
X03878 Genomic DNA Translation: CAA27512.1
X03879 Genomic DNA Translation: CAA27513.1 Sequence problems.
AE014298 Genomic DNA Translation: AAF48639.3
AE014298 Genomic DNA Translation: AAS65389.2
BT046159 mRNA Translation: ACI46547.1
M37783 Genomic DNA Translation: AAA28873.1 Sequence problems.
AY089560 mRNA Translation: AAL90298.1 Different initiation.
AF129814 mRNA Translation: AAD18071.1
S74010 mRNA Translation: AAB32204.1
PIRiA29106 QZFF
RefSeqiNP_001285343.1, NM_001298414.1
NP_523377.1, NM_078653.2
NP_996488.2, NM_206765.3
UniGeneiDm.4956

Genome annotation databases

EnsemblMetazoaiFBtr0089734; FBpp0088675; FBgn0003189
FBtr0340155; FBpp0309141; FBgn0003189
FBtr0340156; FBpp0309142; FBgn0003189
GeneIDi32640
KEGGidme:Dmel_CG18572

Entry informationi

Entry nameiPYR1_DROME
AccessioniPrimary (citable) accession number: P05990
Secondary accession number(s): B5X540
, O97163, Q26376, Q7KUX4, Q8SXM0, Q9VXD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: May 23, 2018
This is version 199 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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