P05990 (PYR1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CAD protein

Alternative name(s):
Protein rudimentary

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:	r
ORF Names:	CG18572

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	2224 AA.
Sequence status	Complete.
Protein existence	Evidence 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).
Catalytic activity	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.
Cofactor	Binds 1 zinc ion per subunit (for dihydroorotase activity) Potential. Binds 2 manganese ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. 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.
Subcellular location	Cytoplasm.
Miscellaneous	GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) together form 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.
Sequence caution	The sequence AAA28873.1 differs from that shown. Reason: Various problems, including DNA not present in the genome. The sequence AAL90298.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA27509.1 differs from that shown. Reason: Various problems, including DNA not present in the genome. The sequence CAA27510.1 differs from that shown. Reason: Various problems, including DNA not present in the genome. The sequence CAA27511.1 differs from that shown. Reason: Various problems, including DNA not present in the genome. The sequence CAA27513.1 differs from that shown. Reason: Various problems, including DNA not present in the genome. The sequence CAA28502.1 differs from that shown. Reason: Various problems, including DNA not present in the genome.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase Ligase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
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 mutant phenotype PubMed 4218218PubMed 5004701. Source: FlyBase carbamoyl phosphate biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine catabolic process Inferred from electronic annotation. Source: InterPro glutamine metabolic process Inferred from mutant phenotype PubMed 28118. Source: FlyBase
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from direct assay PubMed 28118. Source: FlyBase carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from direct assay PubMed 28118. Source: FlyBase dihydroorotase activity Inferred from direct assay PubMed 28118. Source: FlyBase metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P05990-1)

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.

Isoform B (identifier: P05990-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1374-1386: ESVQWTFDKTTPD → SIFMSVCLLYIMQ
     1387-2224: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2224	2224	CAD protein		PRO_0000199505
Regions
	Domain	195 – 380	186	Glutamine amidotransferase type-1
	Domain	529 – 721	193	ATP-grasp 1
	Domain	1066 – 1257	192	ATP-grasp 2
	Nucleotide binding	555 – 610	56	ATP By similarity
	Nucleotide binding	1092 – 1149	58	ATP By similarity
	Region	1 – 369	369	GATase (Glutamine amidotransferase)
	Region	370 – 415	46	Linker
	Region	416 – 1470	1055	CPSase (Carbamoyl-phosphate synthase)
	Region	1471 – 1484	14	Linker
	Region	1485 – 1800	316	DHOase (dihydroorotase)
	Region	1801 – 1912	112	Linker
	Region	1913 – 2224	312	ATCase (Aspartate transcarbamylase)
Sites
	Active site	269	1	For GATase activity By similarity
	Active site	353	1	For GATase activity By similarity
	Active site	355	1	For GATase activity By similarity
	Metal binding	678	1	Manganese 1 By similarity
	Metal binding	692	1	Manganese 1 By similarity
	Metal binding	692	1	Manganese 2 By similarity
	Metal binding	694	1	Manganese 2 By similarity
	Metal binding	1216	1	Manganese 3 By similarity
	Metal binding	1228	1	Manganese 3 By similarity
	Metal binding	1228	1	Manganese 4 By similarity
	Metal binding	1230	1	Manganese 4 By similarity
	Metal binding	1486	1	Zinc Potential
	Metal binding	1488	1	Zinc Potential
Amino acid modifications
	Modified residue	1883	1	Phosphoserine Ref.11
	Modified residue	1885	1	Phosphoserine Ref.11
	Modified residue	1892	1	Phosphoserine Ref.11
	Modified residue	1894	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	1374 – 1386	13	ESVQW…KTTPD → SIFMSVCLLYIMQ in isoform B.		VSP_016004
	Alternative sequence	1387 – 2224	838	Missing in isoform B.		VSP_016005
Experimental info
	Mutagenesis	1167	1	E → K: Severely diminishes UTP inhibition of CPSase; in Su(b). Ref.9
	Sequence conflict	34	1	F → V in CAA27509. Ref.2
	Sequence conflict	58	1	G → A in CAA27509. Ref.2
	Sequence conflict	172 – 173	2	RN → QD in CAA27509. Ref.2
	Sequence conflict	220 – 221	2	LL → FV in CAA27509. Ref.2
	Sequence conflict	288	1	Y → I in CAA27509. Ref.2
	Sequence conflict	394	1	P → L in CAA27509. Ref.2
	Sequence conflict	2192	1	S → L in CAA27513. Ref.2
	Sequence conflict	2222 – 2224	3	TAL → RRS in CAA27513. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified October 25, 2005. Version 3. Checksum: F89DEAD44FEFAEC6	FASTA	2,224	246,672
	10 20 30 40 50 60 MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA LTDRSYSGQI 70 80 90 100 110 120 LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV VGEVAEEAFH WRKWKTLPDW 130 140 150 160 170 180 LKQHKVPGIQ DIDTRALTKK LREQGSMLGK IVYEKPPVEG LPKSSFVDPN VRNLAKECSV 190 200 210 220 230 240 KERQVYGNPN GKGPRIAILD CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG 250 260 270 280 290 300 PGNPESCDQI VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR 310 320 330 340 350 360 ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV QFHPEHHAGP 370 380 390 400 410 420 QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP VMPRKVLILG SGGLSIGQAG 430 440 450 460 470 480 EFDYSGSQAI KAMRESNIQT VLINPNIATV QTSKGMADKC YFLPLTPHYV EQVIKSERPN 490 500 510 520 530 540 GVLLTFGGQT ALNCGVQLER AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA 550 560 570 580 590 600 PSEAVYSVAQ ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV 610 620 630 640 650 660 DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL SDREYQMLRS 670 680 690 700 710 720 TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA 730 740 750 760 770 780 LGLPLPDIKN SVTGNTTACF EPSLDYCVVK IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG 790 800 810 820 830 840 RNFEEAFQKA LRMVDSDVLG FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE 850 860 870 880 890 900 LHQLTNIDYW FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA 910 920 930 940 950 960 VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI VVGSGVYRIG 970 980 990 1000 1010 1020 SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC DRLYFEEISF EVVMDIYEME 1030 1040 1050 1060 1070 1080 NSEGIILSMG GQLPNNIAMD LHRQQAKVLG TSPESIDCAE NRFKFSRMLD RKGILQPRWK 1090 1100 1110 1120 1130 1140 ELTNLQSAIE FCEEVGYPCL VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS 1150 1160 1170 1180 1190 1200 KFLTEAKEID VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT 1210 1220 1230 1240 1250 1260 CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA TATRAIVGLD 1270 1280 1290 1300 1310 1320 VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG EVACFGDNRY EAYLKAMMST 1330 1340 1350 1360 1370 1380 GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA KMGYKLYASM GTGDFYAEHG VNVESVQWTF 1390 1400 1410 1420 1430 1440 DKTTPDDING ELRHLAEFLA NKQFDLVINL PMSGGGARRV SSFMTHGYRT RRLAVDYSIP 1450 1460 1470 1480 1490 1500 LVTDVKCTKL LVESMRMNGG KPPMKTHTDC MTSRRIVKLP GFIDVHVHLR EPGATHKEDF 1510 1520 1530 1540 1550 1560 ASGTAAALAG GVTLVCAMPN TNPSIVDRET FTQFQELAKA GARCDYALYV GASDDNWAQV 1570 1580 1590 1600 1610 1620 NELASHACGL KMYLNDTFGT LKLSDMTSWQ RHLSHWPKRS PIVCHAERQS TAAVIMLAHL 1630 1640 1650 1660 1670 1680 LDRSVHICHV ARKEEIQLIR SAKEKGVKVT CEVCPHHLFL STKDVERLGH GMSEVRPLLC 1690 1700 1710 1720 1730 1740 SPEDQEALWE NIDYIDVFAT DHAPHTLAEK RSERPPPGFP GVETILPLLL QAVHEGRLTM 1750 1760 1770 1780 1790 1800 EDIKRKFHRN PKIIFNLPDQ AQTYVEVDLD EEWTITGNEM KSKSGWTPFE GTKVKGRVHR 1810 1820 1830 1840 1850 1860 VVLRGEVAFV DGQVLVQPGF GQNVRPKQSP LASEASQDLL PSDNDANDTF TRLLTSEGPG 1870 1880 1890 1900 1910 1920 GGVHGISTKV HFVDGANFLR PNSPSPRIRL DSASNTTLRE YLQRTTNSNP VAHSLMGKHI 1930 1940 1950 1960 1970 1980 LAVDMFNKDH LNDIFNLAQL LKLRGTKDRP VDELLPGKIM ASVFYEVSTR TQCSFAAAML 1990 2000 2010 2020 2030 2040 RLGGRVISMD NITSSVKKGE SLEDSIKVVS SYADVVVLRH PSPGAVARAA TFSRKPLINA 2050 2060 2070 2080 2090 2100 GDGVGEHPTQ ALLDIFTIRE EFGTVNGLTI TMVGDLKNGR TVHSLARLLT LYNVNLQYVA 2110 2120 2130 2140 2150 2160 PNSLQMPDEV VQFVHQRGVK QLFARDLKNV LPDTDVLYMT RIQRERFDNV EDYEKCCGHL 2170 2180 2190 2200 2210 2220 VLTPEHMMRA KKRSIVLHPL PRLNEISREI DSDPRAAYFR QAEYGMYIRM ALLAMVVGGR NTAL
	Isoform B [UniParc]. Checksum: 6A819A2EA7341FF6	FASTA	1,386	153,287
	10 20 30 40 50 60 MASTDCYLAL EDGTVLPGYS FGYVPSENES KVGFGGEVVF QTGMVGYTEA LTDRSYSGQI 70 80 90 100 110 120 LVLTYPLIGN YGVPAPDEDE HGLPLHFEWM KGVVQATALV VGEVAEEAFH WRKWKTLPDW 130 140 150 160 170 180 LKQHKVPGIQ DIDTRALTKK LREQGSMLGK IVYEKPPVEG LPKSSFVDPN VRNLAKECSV 190 200 210 220 230 240 KERQVYGNPN GKGPRIAILD CGLKLNQLRC LLQRGASVTL LPWSARLEDE QFDALFLSNG 250 260 270 280 290 300 PGNPESCDQI VQQVRKVIEE GQKPVFGICL GHQLLAKAIG CSTYKMKYGN RGHNLPCLHR 310 320 330 340 350 360 ATGRCLMTSQ NHGYAVDLEQ LPDGWSELFV NANDGTNEGI VHASKPYFSV QFHPEHHAGP 370 380 390 400 410 420 QDTEFLFDVF MESIQQKDLT IPQLIEQRLR PTTPAIDSAP VMPRKVLILG SGGLSIGQAG 430 440 450 460 470 480 EFDYSGSQAI KAMRESNIQT VLINPNIATV QTSKGMADKC YFLPLTPHYV EQVIKSERPN 490 500 510 520 530 540 GVLLTFGGQT ALNCGVQLER AGVFSKYNVR ILGTPIQSII ETEDRKLFAE RVNEIGEQVA 550 560 570 580 590 600 PSEAVYSVAQ ALDAASRLGY PVMARAAFSL GGLGSGFANN EEELQSLAQQ ALAHSSQLIV 610 620 630 640 650 660 DKSLKGWKEV EYEVVRDAYN NCITVCNMEN FDPLGIHTGE SIVVAPSQTL SDREYQMLRS 670 680 690 700 710 720 TALKVIRHFG VVGECNIQYA LCPHSEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA 730 740 750 760 770 780 LGLPLPDIKN SVTGNTTACF EPSLDYCVVK IPRWDLAKFV RVSKHIGSSM KSVGEVMAIG 790 800 810 820 830 840 RNFEEAFQKA LRMVDSDVLG FDPDVVPLNK EQLAEQLSEP TDRRPFVIAA ALQLGMSLRE 850 860 870 880 890 900 LHQLTNIDYW FLEKLERIIL LQSLLTRNGS RTDAALLLKA KRFGFSDKQI AKYIKSTELA 910 920 930 940 950 960 VRHQRQEFGI RPHVKQIDTV AGEWPASTNY LYHTYNGSEH DVDFPGGHTI VVGSGVYRIG 970 980 990 1000 1010 1020 SSVEFDWCAV GCLRELRKLQ RPTIMINYNP ETVSTDYDMC DRLYFEEISF EVVMDIYEME 1030 1040 1050 1060 1070 1080 NSEGIILSMG GQLPNNIAMD LHRQQAKVLG TSPESIDCAE NRFKFSRMLD RKGILQPRWK 1090 1100 1110 1120 1130 1140 ELTNLQSAIE FCEEVGYPCL VRPSYVLSGA AMNVAYSNQD LETYLNAASE VSREHPVVIS 1150 1160 1170 1180 1190 1200 KFLTEAKEID VDAVASDGRI LCMAVSEHVE NAGVHSGDAT LVTPPQDLNA ETLEAIKRIT 1210 1220 1230 1240 1250 1260 CDLASVLDVT GPFNMQLIAK NNELKVIECN VRVSRSFPFV SKTLDHDFVA TATRAIVGLD 1270 1280 1290 1300 1310 1320 VEPLDVLHGV GKVGVKVPQF SFSRLAGADV QLGVEMASTG EVACFGDNRY EAYLKAMMST 1330 1340 1350 1360 1370 1380 GFQIPKNAVL LSIGSFKHKM ELLPSIRDLA KMGYKLYASM GTGDFYAEHG VNVSIFMSVC LLYIMQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. 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]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-2224 (ISOFORM B). 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 (ISOFORM A), 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, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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: AAS65389.1. 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.
PIR	QZFF. A29106.
RefSeq	NP_523377.1. NM_078653.1. NP_996488.1. NM_206765.1.
UniGene	Dm.4956.
3D structure databases
ProteinModelPortal	P05990.
SMR	P05990. Positions 8-376, 545-730, 1310-1456, 1480-1809, 1917-2218.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05990. 4 interactions.
MINT	MINT-889416.
Protein family/group databases
MEROPS	M38.972.
Proteomic databases
PaxDb	P05990.
PRIDE	P05990.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089734; FBpp0088675; FBgn0003189.
GeneID	32640.
KEGG	dme:Dmel_CG18572.
Organism-specific databases
CTD	32640.
FlyBase	FBgn0003189. r.
Phylogenomic databases
eggNOG	COG0458.
GeneTree	ENSGT00390000015604.
InParanoid	P05990.
KO	K11540.
OMA	QRPVHIC.
OrthoDB	EOG4547DF.
PhylomeDB	P05990.
Enzyme and pathway databases
UniPathway	UPA00070; UER00115. UPA00070; UER00116. UPA00070; UER00117.
Gene expression databases
Bgee	P05990.
GermOnline	CG18572. Drosophila melanogaster.
Family and domain databases
Gene3D	1.10.1030.10. 1 hit. 3.30.1490.20. 2 hits. 3.30.470.20. 2 hits. 3.40.50.1380. 1 hit. 3.40.50.20. 2 hits. 3.50.30.20. 1 hit.
InterPro	IPR006680. Amidohydro_1. 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. 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_1. IPR011059. Metal-dep_hydrolase_composite. IPR011607. MGS-like_dom. IPR016185. PreATP-grasp_dom. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. PF00289. 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]
PRINTS	PR00100. AOTCASE. PR00101. ATCASE. PR00098. CPSASE.
SMART	SM01096. CPSase_L_D3. 1 hit. SM01097. CPSase_sm_chain. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53671. Asp/Orn_carbamoyltranf. 1 hit. SSF48108. CarbamoylP_synth_lsu_oligo. 1 hit. SSF52021. CP_synthsmall. 1 hit. SSF51338. Metalo_hydrolase. 1 hit. SSF52335. MGS-like_dom. 1 hit. SSF52440. PreATP-grasp-like. 2 hits.
TIGRFAMs	TIGR00670. asp_carb_tr. 1 hit. TIGR01369. CPSaseII_lrg. 1 hit. TIGR01368. CPSaseIIsmall. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	R. drosophila.
GenomeRNAi	32640.
NextBio	779598.

Entry information

Entry name

PYR1_DROME

Accession

Primary (citable) accession number: P05990
Secondary accession number(s): B5X540 , O97163, Q26376, Q7KUX4, Q8SXM0, Q9VXD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 25, 2005
Last modified:	May 1, 2013
This is version 150 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project