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Protein

CAD protein

Gene

pyr-1

Organism
Caenorhabditis elegans
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) (By similarity). Involved in the elongation of the pharyngeal isthmus during development, probably by providing precursors of UDP-sugars required for heparan sulfate proteoglycan biosynthesis (PubMed:16828468). Regulates the organization of the actin and intermediate filaments cytoskeleton in the pharyngeal muscles (PubMed:16828468).By similarity1 Publication

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.By similarity
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 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

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.By similarity
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (pyr-1)
  2. CAD protein (pyr-1)
  3. CAD protein (pyr-1)
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 sitei255Nucleophile; for GATase activityPROSITE-ProRule annotation1
Active sitei339For GATase activityPROSITE-ProRule annotation1
Active sitei341For GATase activityPROSITE-ProRule annotation1
Metal bindingi665Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi679Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi679Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi681Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi1204Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1218Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1483Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1483Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1485Zinc 1; via tele nitrogenBy similarity1
Binding sitei1487N-carbamoyl-L-aspartateBy similarity1
Binding sitei1517N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1568Zinc 1; via carbamate groupBy similarity1
Metal bindingi1568Zinc 3; via carbamate groupBy similarity1
Metal bindingi1602Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1626Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1649Zinc 2By similarity1
Binding sitei1670N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1695Zinc 1By similarity1
Binding sitei1695N-carbamoyl-L-aspartateBy similarity1
Binding sitei1699N-carbamoyl-L-aspartateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi542 – 597ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1080 – 1137ATPPROSITE-ProRule annotationAdd BLAST58

GO - Molecular functioni

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: GO_Central
  • arginine biosynthetic process Source: GO_Central
  • glutamine metabolic process Source: InterPro
  • pharynx development Source: WormBase
  • pyrimidine nucleobase biosynthetic process Source: WormBase
  • urea cycle Source: GO_Central

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-CEL-500753. Pyrimidine biosynthesis.
UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
CAD proteinBy similarity
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthaseBy similarity (EC:6.3.5.5By similarity)
Aspartate carbamoyltransferaseBy similarity (EC:2.1.3.2By similarity)
DihydroorotaseBy similarity (EC:3.5.2.3By similarity)
Gene namesi
Name:pyr-11 PublicationImported
ORF Names:D2085.1Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiD2085.1; CE41886; WBGene00004259; pyr-1.

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown causes an arrest at the embryonic stage or at the L1 larval stage (PubMed:16828468). The few surviving animals grow more slowly (PubMed:16828468). L1 larvae have incomplete pharyngeal isthmus elongation, 36 percent of which have the pharynx detached from the buccal cavity (PubMed:16828468). In an umps-1 zu456 mutant background embryo, prevents the formation of abnormally enlarged gut granules (PubMed:20148972).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1602H → Q in cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background embryo, prevents the formation of abnormally enlarged gut granules. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004387711 – 2198CAD proteinCuratedAdd BLAST2198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1568N6-carboxylysineBy similarity1

Proteomic databases

EPDiQ18990.
PaxDbiQ18990.
PeptideAtlasiQ18990.

Expressioni

Tissue specificityi

Expressed in the intestine.1 Publication

Developmental stagei

Expressed predominantly in gut precursor cells from the 4E embryonic stage until the bean stage. Expression resumes at the L1 larval stage and continues into adulthood.1 Publication

Gene expression databases

BgeeiWBGene00004259.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi6239.D2085.1.

Structurei

3D structure databases

ProteinModelPortaliQ18990.
SMRiQ18990.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini180 – 366Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST187
Domaini516 – 708ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini1054 – 1245ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 368GATase (Glutamine amidotransferase)By similarityAdd BLAST366
Regioni392 – 1467CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1076
Regioni392 – 934CPSase ABy similarityAdd BLAST543
Regioni935 – 1467CPSase BBy similarityAdd BLAST533
Regioni1468 – 1799DHOase (dihydroorotase)By similarityAdd BLAST332
Regioni1800 – 1870LinkerBy similarityAdd BLAST71
Regioni1871 – 2196ATCase (Aspartate transcarbamylase)By similarityAdd BLAST326

Sequence similaritiesi

In the central section; belongs to the DHOase family.Curated
Contains 2 ATP-grasp domains.PROSITE-ProRule annotation
Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
InParanoidiQ18990.
KOiK11540.
OMAiLYSVRLN.
OrthoDBiEOG091G00DC.
PhylomeDBiQ18990.

Family and domain databases

Gene3Di1.10.1030.10. 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.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr. 1 hit.
MF_01209. CPSase_S_chain. 1 hit.
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. 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.
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. 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]

Sequencei

Sequence statusi: Complete.

Q18990-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRATLHLEDG STFVGSIYGA TKSVVGEIVF QTGMVGYVES LTDPSYAKQL
60 70 80 90 100
LTLTYPLIGN YGVPSAEILD QFKLPAEFES DRIWPAALIV EKICVDGEHS
110 120 130 140 150
HWQAVQSLSE WLRKADVPCL SGIDVRQLVK KIRETGTMKA KLVIESDNAQ
160 170 180 190 200
NFDYVDVNAE NLVDFVSRKE PVVYGSGDQT ILAVDCGLKN NQIRCLAKRG
210 220 230 240 250
FRVKVVPWNH PIDTESDYDG LFLSNGPGDP EICAPLVDRL AKVIARGDKP
260 270 280 290 300
IFGICLGHQI LSRAIGAKTY KLKYGNRGHN QPCTHYATGR CYITSQNHGY
310 320 330 340 350
AVDPDSLPAD WKALFTNEND KTNEGIVHSS KPFFSVQFHP EHTAGPTDCE
360 370 380 390 400
FLFDVFADSV RQAKSGTFMN VDQELTRLMT FTPIYHAKEQ RKVLVLGSGG
410 420 430 440 450
LTIGQAGEFD YSGAQALKAL REEGIRTVLI NPNIATVQTS KGFADFTYFL
460 470 480 490 500
PITKEYVTDV IKKERPTGIL CTFGGQTALN CAIDLYKDGI FEQYDVQVLG
510 520 530 540 550
TQINTIMKTE DRDLFNQEIS AIGEKVAPSK AATTMEGAIE AAEELGYPVL
560 570 580 590 600
VRAAYALGGL GSGFADNREE LIAIAQQALA HSNQVLVDKS LKGWKEVEYE
610 620 630 640 650
VVRDAYDNCI TVCNMENVDP LGIHTGESVV VAPSQTLSDR EYNALRTCAI
660 670 680 690 700
KVIRHLGIIG ECNIQYALDP YSLTYYIIEV NARLSRSSAL ASKATGYPLA
710 720 730 740 750
YVAAKLALGQ HLPVIRNSVT GTTTACFEPS LDYCVVKIPR WDLGKFARVS
760 770 780 790 800
TQIGSSMKSV GEVMGIGRCF EEALQKALRM VSDHADGFSP YTFSRPTTAD
810 820 830 840 850
DLSKPTDKRM FALARGMYYG DFDVEKAHEL TRIDRWFLFR MQNIVDIYHR
860 870 880 890 900
LEKTDVNTVS AELLLEAKQA GFSDRQIAKK IGSNEYTVRE ARFVKGITPC
910 920 930 940 950
VKQIDTVAGE WPAQTNYLYT TFNGIENDVS FNMKNAVMVL GSGVYRIGSS
960 970 980 990 1000
VEFDSSCVGC IRELKALGYS TITVNCNPET VSTDYDICDR LYFEEISFET
1010 1020 1030 1040 1050
VLDVYHLEKP KGVILAFGGQ APNNIAMSLS RAQVKIFGTS PNDIDNAEDR
1060 1070 1080 1090 1100
FKFSRKLESL KISQPQWKKS ENMEDAKNFC AQVGYPCLIR PSYVLSGAAM
1110 1120 1130 1140 1150
NVAHNAEDLE VFLKQAAVVA KEHPVVVSKF INEAKELDVD AVALDGKLVV
1160 1170 1180 1190 1200
MAVSEHIENA GVHSGDATLV TPAQDMNKLT LDRIKDITFR IAEAFNVNGP
1210 1220 1230 1240 1250
FNMQLIAKNN ELKVIECNLR VSRSFPFVSK TLDYDFVALA TRAMMASDSP
1260 1270 1280 1290 1300
AIRATIKPTA TLLKGKGRVG VKVPQFSFSR LAGADVMLGV EMASTGEVAC
1310 1320 1330 1340 1350
FGTSRCDAYL KALLSTGFVV PKQNIFISIG GYHAKAEMLK SVEALLKLGY
1360 1370 1380 1390 1400
ELYGSKGTAD YFQSNKINVK PVDWPFEEGS SDEKTASGTR SVVEFLENKE
1410 1420 1430 1440 1450
FHLVINLPIR GSGAYRVSAF RTHGYKTRRM AIDNGIPLIT DIKCAKTFIQ
1460 1470 1480 1490 1500
ALEMVGKRPT MNSLVDCVTS KSLKRLPGMV DIHVHVREPG ATHKEDWATC
1510 1520 1530 1540 1550
SKAALAGGVT TILAMPNTSP VLVDTDSFYQ TEQLASAKSV VDYALYIGAT
1560 1570 1580 1590 1600
PNNSKFAAEF ADKAAGLKMY LNETFSTLKM DNISDWAKHL SAFPANRPIV
1610 1620 1630 1640 1650
CHAEKQTLAA ILCMAQMANR AVHIAHVATA DEINLVKEAK QRGWNVTCEV
1660 1670 1680 1690 1700
CPHHLFLIEE DLPDGIREVR PRLVKPEDRQ ALWDNMEYID CFATDHAPHT
1710 1720 1730 1740 1750
WAEKTGKDGK IPPGFPGVEY MLPLLLTAVH DGKLTMKELT DRMSTNPRRI
1760 1770 1780 1790 1800
FNLPPQDDTY IEVDLNEEWT IPENGGQSKA GWTPFAGRKV FGKVHNVIIR
1810 1820 1830 1840 1850
GEEAVIDGRI VAIPGFGKNV RLYPHSGTAH RGDSDFDQIL EPIPQQMIES
1860 1870 1880 1890 1900
SSDEQSPLHT PPRAHTPIAF PGELLAKNCI SVKHLDKGQI NRIFELADRY
1910 1920 1930 1940 1950
KHDVEKGHPL THILNGKVLV NLFYEVSTRT SCSFSAAMQR LGGSVISVDS
1960 1970 1980 1990 2000
QSSSVQKGET LEDTVQVLGS YGDILVLRSN ENGAADRAAR VCDQPVINGG
2010 2020 2030 2040 2050
DGTGEHPTQA LLDVYTIRQE MGTVNGLTIA LVGDLKNGRT VHSLAKLLCL
2060 2070 2080 2090 2100
YKDITLHYVA PSTELEMPQE VLDYVSSKSN FVQKKFTSLA EGINHVDVVY
2110 2120 2130 2140 2150
VTRIQKERFS SPDEYNKVKG SYVINAKLLN EAARDVEEPS SLLVPARSLP
2160 2170 2180 2190
IVMHPLPRVD EIAVELDHDE RAAYFRQAKN GVFVRMSILS LLLGRGHL
Length:2,198
Mass (Da):242,582
Last modified:February 5, 2008 - v2
Checksum:i31CFC62E64D21B1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284602 Genomic DNA. Translation: CAA91059.2.
RefSeqiNP_495838.2. NM_063437.4.
UniGeneiCel.33265.

Genome annotation databases

EnsemblMetazoaiD2085.1; D2085.1; WBGene00004259.
GeneIDi174385.
KEGGicel:CELE_D2085.1.
UCSCiD2085.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284602 Genomic DNA. Translation: CAA91059.2.
RefSeqiNP_495838.2. NM_063437.4.
UniGeneiCel.33265.

3D structure databases

ProteinModelPortaliQ18990.
SMRiQ18990.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.D2085.1.

Proteomic databases

EPDiQ18990.
PaxDbiQ18990.
PeptideAtlasiQ18990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiD2085.1; D2085.1; WBGene00004259.
GeneIDi174385.
KEGGicel:CELE_D2085.1.
UCSCiD2085.1. c. elegans.

Organism-specific databases

CTDi174385.
WormBaseiD2085.1; CE41886; WBGene00004259; pyr-1.

Phylogenomic databases

eggNOGiKOG0370. Eukaryota.
COG0458. LUCA.
COG0505. LUCA.
COG0540. LUCA.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
InParanoidiQ18990.
KOiK11540.
OMAiLYSVRLN.
OrthoDBiEOG091G00DC.
PhylomeDBiQ18990.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.
ReactomeiR-CEL-500753. Pyrimidine biosynthesis.

Gene expression databases

BgeeiWBGene00004259.

Family and domain databases

Gene3Di1.10.1030.10. 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.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr. 1 hit.
MF_01209. CPSase_S_chain. 1 hit.
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. 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.
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. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPYR1_CAEEL
AccessioniPrimary (citable) accession number: Q18990
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 18, 2017
Last sequence update: February 5, 2008
Last modified: January 18, 2017
This is version 136 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.