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Protein

CAD protein

Gene

r

Organism
Drosophila melanogaster (Fruit fly)
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).

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

Protein has several cofactor binding sites:
  • Zn2+CuratedNote: Binds 1 zinc ion per subunit (for dihydroorotase activity).Curated
  • Mn2+By similarityNote: Binds 2 manganese ions per subunit.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 (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei269 – 2691For GATase activityBy similarity
Active sitei353 – 3531For GATase activityBy similarity
Active sitei355 – 3551For GATase activityBy similarity
Metal bindingi678 – 6781Manganese 1By similarity
Metal bindingi692 – 6921Manganese 1By similarity
Metal bindingi692 – 6921Manganese 2By similarity
Metal bindingi694 – 6941Manganese 2By similarity
Metal bindingi1216 – 12161Manganese 3By similarity
Metal bindingi1228 – 12281Manganese 3By similarity
Metal bindingi1228 – 12281Manganese 4By similarity
Metal bindingi1230 – 12301Manganese 4By similarity
Metal bindingi1486 – 14861ZincSequence analysis
Metal bindingi1488 – 14881ZincSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi555 – 61056ATPBy similarityAdd
BLAST
Nucleotide bindingi1092 – 114958ATPBy similarityAdd
BLAST

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

Keywords - Molecular functioni

Hydrolase, Ligase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, 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:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
Dihydroorotase (EC:3.5.2.3)
Gene namesi
Name:r
ORF Names:CG18572
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0003189. r.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1167 – 11671E → K: Severely diminishes UTP inhibition of CPSase; in Su(b). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22242224CAD proteinPRO_0000199505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1883 – 18831Phosphoserine1 Publication
Modified residuei1885 – 18851Phosphoserine1 Publication
Modified residuei1892 – 18921Phosphoserine1 Publication
Modified residuei1894 – 18941Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05990.
PRIDEiP05990.

PTM databases

iPTMnetiP05990.

Expressioni

Gene expression databases

BgeeiP05990.
GenevisibleiP05990. DM.

Interactioni

Protein-protein interaction databases

BioGridi58976. 35 interactions.
IntActiP05990. 8 interactions.
MINTiMINT-889416.
STRINGi7227.FBpp0088675.

Structurei

3D structure databases

ProteinModelPortaliP05990.
SMRiP05990. Positions 1475-1825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini195 – 380186Glutamine amidotransferase type-1Add
BLAST
Domaini529 – 721193ATP-grasp 1Add
BLAST
Domaini1066 – 1257192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 369369GATase (Glutamine amidotransferase)Add
BLAST
Regioni370 – 41546LinkerAdd
BLAST
Regioni416 – 14701055CPSase (Carbamoyl-phosphate synthase)Add
BLAST
Regioni1471 – 148414LinkerAdd
BLAST
Regioni1485 – 1800316DHOase (dihydroorotase)Add
BLAST
Regioni1801 – 1912112LinkerAdd
BLAST
Regioni1913 – 2224312ATCase (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

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
InParanoidiP05990.
OMAiIEIDRPY.
OrthoDBiEOG7M6D6F.
PhylomeDBiP05990.

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.
MF_01209. CPSase_S_chain.
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. 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.
PROSITEiPS50975. 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.
[Graphical view]

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 AAA28873.1 differs from that shown.Various problems, including DNA not present in the genome.Curated
The sequence AAL90298.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA27509.1 differs from that shown.Various problems, including DNA not present in the genome.Curated
The sequence CAA27510.1 differs from that shown.Various problems, including DNA not present in the genome.Curated
The sequence CAA27511.1 differs from that shown.Various problems, including DNA not present in the genome.Curated
The sequence CAA27513.1 differs from that shown.Various problems, including DNA not present in the genome.Curated
The sequence CAA28502.1 differs from that shown.Various problems, including DNA not present in the genome.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341F → V in CAA27509 (PubMed:3023623).Curated
Sequence conflicti58 – 581G → A in CAA27509 (PubMed:3023623).Curated
Sequence conflicti172 – 1732RN → QD in CAA27509 (PubMed:3023623).Curated
Sequence conflicti220 – 2212LL → FV in CAA27509 (PubMed:3023623).Curated
Sequence conflicti288 – 2881Y → I in CAA27509 (PubMed:3023623).Curated
Sequence conflicti394 – 3941P → L in CAA27509 (PubMed:3023623).Curated
Sequence conflicti2192 – 21921S → L in CAA27513 (PubMed:3023623).Curated
Sequence conflicti2222 – 22243TAL → RRS in CAA27513 (PubMed:3023623).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP05990.
SMRiP05990. Positions 1475-1825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58976. 35 interactions.
IntActiP05990. 8 interactions.
MINTiMINT-889416.
STRINGi7227.FBpp0088675.

Protein family/group databases

MEROPSiM38.972.

PTM databases

iPTMnetiP05990.

Proteomic databases

PaxDbiP05990.
PRIDEiP05990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089734; FBpp0088675; FBgn0003189.
FBtr0340155; FBpp0309141; FBgn0003189.
FBtr0340156; FBpp0309142; FBgn0003189.
GeneIDi32640.

Organism-specific databases

CTDi32640.
FlyBaseiFBgn0003189. r.

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
InParanoidiP05990.
OMAiIEIDRPY.
OrthoDBiEOG7M6D6F.
PhylomeDBiP05990.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiR. fly.
GenomeRNAii32640.
PROiP05990.

Gene expression databases

BgeeiP05990.
GenevisibleiP05990. DM.

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.
MF_01209. CPSase_S_chain.
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. 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.
PROSITEiPS50975. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The rudimentary gene of Drosophila melanogaster encodes four enzymic functions."
    Freund J.-N., Jarry B.P.
    J. Mol. Biol. 193:1-13(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular organization of the rudimentary gene of Drosophila melanogaster."
    Freund J.-N., Zerges W., Schedl P., Jarry B.P.
    J. Mol. Biol. 189:25-36(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Erratum
    Freund J.-N., Zerges W., Schedl P., Jarry B.P.
    J. Mol. Biol. 191:727-727(1986)
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  7. "Molecular characterization of the 5' end of the rudimentary gene in Drosophila and analysis of three P element insertions."
    Zerges W., Udvardy A., Schedl P.
    Nucleic Acids Res. 20:4639-4647(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-2224.
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  9. "A mutation that uncouples allosteric regulation of carbamyl phosphate synthetase in Drosophila."
    Simmons A.J., Rawls J.M., Piskur J., Davidson J.N.
    J. Mol. Biol. 287:277-285(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 898-1649, CPSASE ACTIVITY, MUTAGENESIS OF GLU-1167.
  10. "Revision in sequence of CAD aspartate transcarbamylase domain of Drosophila."
    Davidson J.N., Kern C.B.
    J. Mol. Biol. 243:364-366(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 2066-2146.
  11. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1883; SER-1885; SER-1892 AND SER-1894, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiPYR1_DROME
AccessioniPrimary (citable) accession number: P05990
Secondary accession number(s): B5X540
, O97163, Q26376, Q7KUX4, Q8SXM0, Q9VXD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: July 6, 2016
This is version 182 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, 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

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.