ID U3JAV8_DANRE Unreviewed; 2230 AA.
AC U3JAV8; A0A8M1P7L3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=CAD protein {ECO:0000313|RefSeq:NP_001295754.1};
DE EC=2.1.3.2 {ECO:0000313|RefSeq:NP_001295754.1};
DE SubName: Full=Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase {ECO:0000313|Ensembl:ENSDARP00000127377};
GN Name=cad {ECO:0000313|Ensembl:ENSDARP00000127377,
GN ECO:0000313|RefSeq:NP_001295754.1,
GN ECO:0000313|ZFIN:ZDB-GENE-021030-4};
GN Synonyms=cb456 {ECO:0000313|RefSeq:NP_001295754.1}, si:dkey-221h15.3
GN {ECO:0000313|RefSeq:NP_001295754.1}, wu:fc30c12
GN {ECO:0000313|RefSeq:NP_001295754.1}, wu:fc33d01
GN {ECO:0000313|RefSeq:NP_001295754.1}, wu:fc67g02
GN {ECO:0000313|RefSeq:NP_001295754.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000127377};
RN [1] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=11116086;
RA Woods I.G., Kelly P.D., Chu F., Ngo-Hazelett P., Yan Y.L., Huang H.,
RA Postlethwait J.H., Talbot W.S.;
RT "A comparative map of the zebrafish genome.";
RL Genome Res. 10:1903-1914(2000).
RN [2] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=11476583;
RA Link B.A., Kainz P.M., Ryou T., Dowling J.E.;
RT "The perplexed and confused mutations affect distinct stages during the
RT transition from proliferating to post-mitotic cells within the zebrafish
RT retina.";
RL Dev. Biol. 236:436-453(2001).
RN [3] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [4] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.D., Sun X.J., Deng M., Zhang G.W., Zhou Y., Wu X.Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [5] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=15937129; DOI=10.1534/genetics.105.041608;
RA Willer G.B., Lee V.M., Gregg R.G., Link B.A.;
RT "Analysis of the Zebrafish perplexed mutation reveals tissue-specific roles
RT for de novo pyrimidine synthesis during development.";
RL Genetics 170:1827-1837(2005).
RN [6] {ECO:0000313|Ensembl:ENSDARP00000127377, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127377};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [7] {ECO:0000313|Ensembl:ENSDARP00000127377}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000127377};
RG Ensembl;
RL Submitted (SEP-2013) to UniProtKB.
RN [8] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=24812435;
RA Danilova N., Bibikova E., Covey T.M., Nathanson D., Dimitrova E., Konto Y.,
RA Lindgren A., Glader B., Radu C.G., Sakamoto K.M., Lin S.;
RT "The role of the DNA damage response in zebrafish and cellular models of
RT Diamond Blackfan anemia.";
RL Dis. Model. Mech. 7:895-905(2014).
RN [9] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=25294789;
RA Coxam B., Neyt C., Grassini D.R., Le Guen L., Smith K.A.,
RA Schulte-Merker S., Hogan B.M.;
RT "carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and
RT dihydroorotase (cad) regulates Notch signaling and vascular development in
RT zebrafish.";
RL Dev. Dyn. 244:1-9(2015).
RN [10] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [11] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=26061167;
RA Aceto J., Nourizadeh-Lillabadi R., Maree R., Dardenne N., Jeanray N.,
RA Wehenkel L., Alestrom P., van Loon J.J., Muller M.;
RT "Zebrafish Bone and General Physiology Are Differently Affected by Hormones
RT or Changes in Gravity.";
RL PLoS ONE 10:e0126928-e0126928(2015).
RN [12] {ECO:0000313|RefSeq:NP_001295754.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [13] {ECO:0000313|RefSeq:NP_001295754.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001295754.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001363};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004812}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004852}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004880}.
CC -!- SIMILARITY: In the 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
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DR EMBL; BX511178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001295754.1; NM_001308825.1.
DR STRING; 7955.ENSDARP00000127377; -.
DR PaxDb; 7955-ENSDARP00000127377; -.
DR Ensembl; ENSDART00000153310; ENSDARP00000127377; ENSDARG00000041895.
DR Ensembl; ENSDART00000153310.3; ENSDARP00000127377.1; ENSDARG00000041895.10.
DR GeneID; 266992; -.
DR KEGG; dre:266992; -.
DR AGR; ZFIN:ZDB-GENE-021030-4; -.
DR CTD; 790; -.
DR ZFIN; ZDB-GENE-021030-4; cad.
DR eggNOG; KOG0370; Eukaryota.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR Reactome; R-DRE-500753; Pyrimidine biosynthesis.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000437; Chromosome 20.
DR Bgee; ENSDARG00000041895; Expressed in somite and 49 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:ZFIN.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0021610; P:facial nerve morphogenesis; IMP:ZFIN.
DR GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IMP:ZFIN.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:ZFIN.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:ZFIN.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IGI:ZFIN.
DR GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IGI:ZFIN.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0021636; P:trigeminal nerve morphogenesis; IMP:ZFIN.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0021644; P:vagus nerve morphogenesis; IMP:ZFIN.
DR CDD; cd01316; CAD_DHOase; 1.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR00670; asp_carb_tr; 1.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Proteomics identification {ECO:0007829|PeptideAtlas:U3JAV8};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 521..713
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1057..1248
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1313..1468
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1843..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 342
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2230 AA; 247303 MW; 5E64FDB9C9AAB5C4 CRC64;
MSLKMASLVL EDGTTFKGRL FGAVSSVSGE VVFQTGMVGY PEALTDPSYK SQILTLTYPM
IGNYGIPKDE DGEFGLSKWF ESSQIHAAAL IVGEVSENPS HWSAAKSLDE WLREQGIPGL
QGVDTRCLTK KIREKGTMLG KLVVEGTPAD NIPFDNPDAR NLVKEVSMKA PKVFNPEGTV
RITAIDCGIK YNQIRCLCQR GARVTVVPWD QPLDSNDFDG LFISNGPGNP EYCKETVENI
RKVACVENPK PIFGICLGHQ LLSLVIGAKT YKMKYGNRGH NQPCIHKGTS RCYITSQNHG
FAVDPETLPK DWDVLFTNAN DQTSEGIVHN HKPLFSVQFH PEHMAGPTDL VGLFDVFLDT
VRDVKENKAG KSVKQRLMEH LTFPGSPDPN AFVRPRKVLV LGSGGLSIGQ AGEFDYSGSQ
AIKAMKEENI QTILINPNIA TVQTSKGLAD KVYFLPITPE YVTQVIKNER PDGVLLTFGG
QTALNCGVEL KKQGVLEKYK VRVLGTPVAS IEMTEDRKIF VEKMEEINEH VAPSEAAMSV
EQAVAAAERL GYPVLVRSAF ALGGLGSGFA NNRDEMITLV TQAFAHTSQV LVDKSLKGWK
EIEYEVVRDA YDNCVTVCNM ENIDPLGIHT GESIVVAPSQ TLNDYEYNML RNTAIKVIRH
LGVVGECNIQ YALNPESEQY YIIEVNARLS RSSALASKAT GYPLAYVAAK LSLGIPLPVL
KNSVTNSTTA NFEPSLDYCV VKVPRWDLSK FLRVSTKIGS SMKSVGEVMA IGRSFEEAFQ
KALRMVDENC VGFDHTIKPE SEEELQTPTD KRIFVLAAAL HAGYTVERLY ELTKIDHWFL
HKMKNIADHK KLLETYKQDE SAMPPEIMRK AKQLGFSDKQ IAQAVQSTEL AVRKLRRDWK
IFPVVKQIDT VAAEWPAQTN YLYLTYHGSE SDVVFEQPHV MVIGSGVYRI GSSVEFDWCA
VGCIMELRKM GYKTIMVNYN PETVSTDYDM CDRLYFDEIS FEVVMDIYEM ENPEGVILSM
GGQLPNNIAM SLHRQQCRIL GTSPEFIDNA ENRFKFSRML DTIGISQPRW KELSDTESAV
NFCETVGYPC LVRPSYVLSG AAMNVAYSDT DMEKFLSSAV AVSKEHPVVI SKFIQEAKEI
DVDAVACDGE VIAIAVSEHV ENAGVHSGDA TLVTPPQDIN QKTMERIKMI VHAIGQELQV
TGPFNLQLIA KDDQLKVIEC NVRVSRSFPY VSKTLGVDLV ALATRVILGE EVEAVGLMRG
NGIVGVKVPQ FSFSRLAGAD VVLGVEMTST GEVACFGENR YEAYLKAMLS TGFKIPKKNI
LLSIGSYKNK SELLPTVQTL ESLGYNLYAS LGTADFYTEH GVKVMAVDWP FEEESDCPNK
DKQRNIMDYL EENHFDLVIN LSMRNSGGRR LSSFVTKGYR TRRMAIDFSV PLITDIKCTK
LFVQALKQIG QAPRVKTHVD SMTSQKLIRL PGLIDVHVHL REPGATHKED FSSGTAAALA
GGITMVCAMP NTNPAIIDPN SFTMAQKLAK AGCRCDYALF VGASSDNAAL LPSIASSTAG
LKMYLNDTYS TLKMDNVSLW MEHFEKWPKH LPIVAHAEKQ TVAAILLVAQ LYQRPVHICH
VAKKEEILII RAAKQKGIQV TCEVAPHHLF LCEDNVPVIG KDKAQVRPML GTREDMEALW
ENLDIIDCFA TDHAPHSAEE KISEKPPPGY PGLETMLPLL FTAVSEGRLT VDDIIKRLYE
NPRKIFSLPA QEDTYVEVDL EQEWIIPKHM QFTKSKWTPF EGMKVKGKVM RVVLRGEVAY
IDGQVLVPPG YGQDVKSWSA TPTATTEVIM DAPKRVIEAM TPERPRQAAP VDVVRSRAPS
PRRSAGDGRF ILPPRIHRSS DPGLPPELAL PAEAYAHPPP LARILSPQAG QPQILPHPQT
SPLLHPLVGQ HILSVRQFSK EQMSHLFNVA HTLRLMVQKE RPLDILKGKV MASMFYEVST
RTSSSFAAAM HRLGGSVVHF CESTSSTQKG ESLVDSVNTM SCYADVIVLR HPIPGAVESA
ARHCRRPVIN AGDGVGEHPT QALLDIFTIR EELGTVNGMT ITMVGDLKHG RTVHSLARLL
TQYRITLRYV APKNLSMPAE IIDFVASKGI KQEEFNSIEE ALPDTDVLYM TRIQKERFSS
EKEYNACFGQ FILTPHIMTG AKRKMVVMHP LPRVNEISVE VDTDPRAAYF RQAENGMYIR
MALLATVLGR
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