ID PYRB_ECOLI Reviewed; 311 AA.
AC P0A786; P00479; Q2M662; Q47555; Q47557;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000269|PubMed:13319326};
DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN Name=pyrB; OrderedLocusNames=b4245, JW4204;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6302686; DOI=10.1073/pnas.80.9.2462;
RA Hoover T.A., Roof W.D., Foltermann K.F., O'Donovan G.A., Bencini D.A.,
RA Wild J.R.;
RT "Nucleotide sequence of the structural gene (pyrB) that encodes the
RT catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2462-2466(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6364131; DOI=10.1073/pnas.81.1.115;
RA Schachman H.K., Pauza C.D., Navre M., Karels M.J., Wu L., Yang Y.R.;
RT "Location of amino acid alterations in mutants of aspartate
RT transcarbamoylase: structural aspects of interallelic complementation.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:115-119(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 195.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-311.
RX PubMed=6341995; DOI=10.1073/pnas.80.9.2467;
RA Konigsberg W.H., Henderson L.;
RT "Amino acid sequence of the catalytic subunit of aspartate
RT transcarbamoylase from Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2467-2471(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=2459698; DOI=10.1073/pnas.85.19.7149;
RA Roland K.L., Liu C., Turnbough C.L. Jr.;
RT "Role of the ribosome in suppressing transcriptional termination at the
RT pyrBI attenuator of Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7149-7153(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RC STRAIN=K12;
RX PubMed=3928602; DOI=10.1128/jb.163.3.991-999.1985;
RA Roland K.L., Powell F.E., Turnbough C.L. Jr.;
RT "Role of translation and attenuation in the control of pyrBI operon
RT expression in Escherichia coli K-12.";
RL J. Bacteriol. 163:991-999(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RC STRAIN=K12;
RX PubMed=6300835; DOI=10.1073/pnas.80.2.368;
RA Turnbough C.L. Jr., Hicks K.L., Donahue J.P.;
RT "Attenuation control of pyrBI operon expression in Escherichia coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:368-372(1983).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC STRAIN=K12;
RX PubMed=1699940; DOI=10.1016/s0021-9258(17)30629-4;
RA Donahue J.P., Turnbough C.L. Jr.;
RT "Characterization of transcriptional initiation from promoters P1 and P2 of
RT the pyrBI operon of Escherichia coli K12.";
RL J. Biol. Chem. 265:19091-19099(1990).
RN [11]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 2-21.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [13]
RP PROTEIN SEQUENCE OF 2-6.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9629924; DOI=10.1002/elps.1150190539;
RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT "Extraction of membrane proteins by differential solubilization for
RT separation using two-dimensional gel electrophoresis.";
RL Electrophoresis 19:837-844(1998).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=13319326; DOI=10.1016/s0021-9258(18)65332-3;
RA Lowenstein J.M., Cohen P.P.;
RT "Studies on the biosynthesis of carbamylaspartic acid.";
RL J. Biol. Chem. 220:57-70(1956).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SUBUNIT.
RX PubMed=6377306; DOI=10.1073/pnas.81.13.4037;
RA Ke H.-M., Honzatko R.B., Lipscomb W.N.;
RT "Structure of unligated aspartate carbamoyltransferase of Escherichia coli
RT at 2.6-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4037-4040(1984).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CARBAMOYL PHOSPHATE
RP AND SUCCINATE.
RX PubMed=3380787; DOI=10.1073/pnas.85.12.4205;
RA Gouaux J.E., Lipscomb W.N.;
RT "Three-dimensional structure of carbamoyl phosphate and succinate bound to
RT aspartate carbamoyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4205-4208(1988).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=2271528; DOI=10.1021/bi00485a019;
RA Stevens R.C., Gouaux J.E., Lipscomb W.N.;
RT "Structural consequences of effector binding to the T state of aspartate
RT carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-
RT complexed enzymes at 2.6-A resolution.";
RL Biochemistry 29:7691-7701(1990).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=2271529; DOI=10.1021/bi00485a020;
RA Gouaux J.E., Stevens R.C., Lipscomb W.N.;
RT "Crystal structures of aspartate carbamoyltransferase ligated with
RT phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and
RT neutral pH.";
RL Biochemistry 29:7702-7715(1990).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
RX PubMed=10318893; DOI=10.1073/pnas.96.10.5388;
RA Beernink P.T., Endrizzi J.A., Alber T., Schachman H.K.;
RT "Assessment of the allosteric mechanism of aspartate transcarbamoylase
RT based on the crystalline structure of the unregulated catalytic subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5388-5393(1999).
CC -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC committed step in the de novo pyrimidine nucleotide biosynthesis
CC pathway. {ECO:0000255|HAMAP-Rule:MF_00001,
CC ECO:0000269|PubMed:13319326}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00001, ECO:0000269|PubMed:13319326};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00001, ECO:0000305|PubMed:13319326}.
CC -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC organized as two trimers (C3), and six regulatory PyrI chains organized
CC as three dimers (R2). {ECO:0000255|HAMAP-Rule:MF_00001,
CC ECO:0000269|PubMed:6377306}.
CC -!- INTERACTION:
CC P0A786; P0A786: pyrB; NbExp=4; IntAct=EBI-906620, EBI-906620;
CC P0A786; P0A7F3: pyrI; NbExp=18; IntAct=EBI-906620, EBI-906630;
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR EMBL; J01670; AAA24474.1; -; Genomic_DNA.
DR EMBL; K01472; AAA24476.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97142.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77202.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78244.1; -; Genomic_DNA.
DR EMBL; M10743; AAA24479.1; -; Genomic_DNA.
DR EMBL; M60508; AAA24481.1; -; Genomic_DNA.
DR PIR; H65236; DTECC.
DR RefSeq; NP_418666.1; NC_000913.3.
DR RefSeq; WP_000013046.1; NZ_STEB01000013.1.
DR PDB; 1ACM; X-ray; 2.80 A; A/C=2-311.
DR PDB; 1AT1; X-ray; 2.80 A; A/C=2-311.
DR PDB; 1D09; X-ray; 2.10 A; A/C=2-311.
DR PDB; 1EKX; X-ray; 1.95 A; A/B/C=1-311.
DR PDB; 1EZZ; X-ray; 2.70 A; A/C=2-311.
DR PDB; 1F1B; X-ray; 2.30 A; A/C=2-311.
DR PDB; 1I5O; X-ray; 2.80 A; A/C=2-311.
DR PDB; 1NBE; X-ray; 2.60 A; A/C=2-311.
DR PDB; 1Q95; X-ray; 2.46 A; A/B/C/D/E/F=2-311.
DR PDB; 1R0B; X-ray; 2.90 A; A/B/C/D/E/F=2-311.
DR PDB; 1R0C; X-ray; 2.37 A; A/G=2-311.
DR PDB; 1RAA; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAB; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAC; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAD; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAE; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAF; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAG; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAH; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1RAI; X-ray; 2.50 A; A/C=2-311.
DR PDB; 1SKU; X-ray; 2.60 A; A/C=2-311.
DR PDB; 1TTH; X-ray; 2.80 A; A/C=2-311.
DR PDB; 1TU0; X-ray; 2.55 A; A/C=2-311.
DR PDB; 1TUG; X-ray; 2.10 A; A/C=2-311.
DR PDB; 1XJW; X-ray; 2.71 A; A/C=2-311.
DR PDB; 1ZA1; X-ray; 2.20 A; A/C=2-311.
DR PDB; 1ZA2; X-ray; 2.50 A; A/C=2-311.
DR PDB; 2A0F; X-ray; 2.90 A; A/C=2-311.
DR PDB; 2AIR; X-ray; 2.00 A; A/G=2-311.
DR PDB; 2AT1; X-ray; 2.80 A; A/C=2-311.
DR PDB; 2ATC; X-ray; 3.00 A; A=2-311.
DR PDB; 2FZC; X-ray; 2.10 A; A/C=2-311.
DR PDB; 2FZG; X-ray; 2.25 A; A/C=2-311.
DR PDB; 2FZK; X-ray; 2.50 A; A/C=2-311.
DR PDB; 2H3E; X-ray; 2.30 A; A/C=2-311.
DR PDB; 2HSE; X-ray; 2.60 A; A/C=2-311.
DR PDB; 2IPO; X-ray; 2.60 A; A/C=2-311.
DR PDB; 2QG9; X-ray; 2.70 A; A/C=2-311.
DR PDB; 2QGF; X-ray; 2.20 A; A/C=2-311.
DR PDB; 3AT1; X-ray; 2.80 A; A/C=2-311.
DR PDB; 3CSU; X-ray; 1.88 A; A/B/C=2-311.
DR PDB; 3D7S; X-ray; 2.80 A; A/C=2-311.
DR PDB; 3MPU; X-ray; 2.86 A; A/C/E=2-311.
DR PDB; 3NPM; X-ray; 2.10 A; A=2-311.
DR PDB; 4AT1; X-ray; 2.60 A; A/C=2-311.
DR PDB; 4E2F; X-ray; 2.80 A; A/C/E/G/I/K=2-311.
DR PDB; 4F04; X-ray; 2.30 A; A/C=2-311.
DR PDB; 4FYV; X-ray; 2.10 A; A/C=2-311.
DR PDB; 4FYW; X-ray; 2.10 A; A/C=2-311.
DR PDB; 4FYX; X-ray; 2.09 A; A/C=2-311.
DR PDB; 4FYY; X-ray; 1.94 A; A/C=2-311.
DR PDB; 5AT1; X-ray; 2.60 A; A/C=2-311.
DR PDB; 5VMQ; X-ray; 2.01 A; A/B/C=2-311.
DR PDB; 6AT1; X-ray; 2.60 A; A/C=2-311.
DR PDB; 6KJ7; X-ray; 2.84 A; A=2-311.
DR PDB; 6KJ8; X-ray; 3.01 A; A/C/E=2-311.
DR PDB; 6KJ9; X-ray; 2.50 A; A/B/C/D/E/F=2-311.
DR PDB; 6KJA; X-ray; 3.06 A; A/C/E=2-311.
DR PDB; 6KJB; X-ray; 2.06 A; A=2-311.
DR PDB; 7AT1; X-ray; 2.80 A; A/C=2-311.
DR PDB; 8AT1; X-ray; 2.80 A; A/C=2-311.
DR PDB; 8ATC; X-ray; 2.50 A; A/C=2-311.
DR PDB; 9ATC; X-ray; 2.40 A; A=2-311.
DR PDBsum; 1ACM; -.
DR PDBsum; 1AT1; -.
DR PDBsum; 1D09; -.
DR PDBsum; 1EKX; -.
DR PDBsum; 1EZZ; -.
DR PDBsum; 1F1B; -.
DR PDBsum; 1I5O; -.
DR PDBsum; 1NBE; -.
DR PDBsum; 1Q95; -.
DR PDBsum; 1R0B; -.
DR PDBsum; 1R0C; -.
DR PDBsum; 1RAA; -.
DR PDBsum; 1RAB; -.
DR PDBsum; 1RAC; -.
DR PDBsum; 1RAD; -.
DR PDBsum; 1RAE; -.
DR PDBsum; 1RAF; -.
DR PDBsum; 1RAG; -.
DR PDBsum; 1RAH; -.
DR PDBsum; 1RAI; -.
DR PDBsum; 1SKU; -.
DR PDBsum; 1TTH; -.
DR PDBsum; 1TU0; -.
DR PDBsum; 1TUG; -.
DR PDBsum; 1XJW; -.
DR PDBsum; 1ZA1; -.
DR PDBsum; 1ZA2; -.
DR PDBsum; 2A0F; -.
DR PDBsum; 2AIR; -.
DR PDBsum; 2AT1; -.
DR PDBsum; 2ATC; -.
DR PDBsum; 2FZC; -.
DR PDBsum; 2FZG; -.
DR PDBsum; 2FZK; -.
DR PDBsum; 2H3E; -.
DR PDBsum; 2HSE; -.
DR PDBsum; 2IPO; -.
DR PDBsum; 2QG9; -.
DR PDBsum; 2QGF; -.
DR PDBsum; 3AT1; -.
DR PDBsum; 3CSU; -.
DR PDBsum; 3D7S; -.
DR PDBsum; 3MPU; -.
DR PDBsum; 3NPM; -.
DR PDBsum; 4AT1; -.
DR PDBsum; 4E2F; -.
DR PDBsum; 4F04; -.
DR PDBsum; 4FYV; -.
DR PDBsum; 4FYW; -.
DR PDBsum; 4FYX; -.
DR PDBsum; 4FYY; -.
DR PDBsum; 5AT1; -.
DR PDBsum; 5VMQ; -.
DR PDBsum; 6AT1; -.
DR PDBsum; 6KJ7; -.
DR PDBsum; 6KJ8; -.
DR PDBsum; 6KJ9; -.
DR PDBsum; 6KJA; -.
DR PDBsum; 6KJB; -.
DR PDBsum; 7AT1; -.
DR PDBsum; 8AT1; -.
DR PDBsum; 8ATC; -.
DR PDBsum; 9ATC; -.
DR AlphaFoldDB; P0A786; -.
DR SMR; P0A786; -.
DR BioGRID; 4260722; 54.
DR BioGRID; 853055; 1.
DR ComplexPortal; CPX-3091; Aspartate carbamoyltransferase complex.
DR DIP; DIP-35089N; -.
DR IntAct; P0A786; 3.
DR MINT; P0A786; -.
DR STRING; 511145.b4245; -.
DR DrugBank; DB05540; Alanosine.
DR SWISS-2DPAGE; P0A786; -.
DR jPOST; P0A786; -.
DR PaxDb; 511145-b4245; -.
DR EnsemblBacteria; AAC77202; AAC77202; b4245.
DR GeneID; 75169767; -.
DR GeneID; 948767; -.
DR KEGG; ecj:JW4204; -.
DR KEGG; eco:b4245; -.
DR PATRIC; fig|1411691.4.peg.2456; -.
DR EchoBASE; EB0798; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_1_2_6; -.
DR InParanoid; P0A786; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 9774690at2; -.
DR PhylomeDB; P0A786; -.
DR BioCyc; EcoCyc:ASPCARBCAT-MONOMER; -.
DR BioCyc; MetaCyc:ASPCARBCAT-MONOMER; -.
DR BRENDA; 2.1.3.2; 2026.
DR SABIO-RK; P0A786; -.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; P0A786; -.
DR PRO; PR:P0A786; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0070207; P:protein homotrimerization; IDA:EcoCyc.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
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 NCBIfam; TIGR00670; asp_carb_tr; 1.
DR PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6341995,
FT ECO:0000269|PubMed:9298646, ECO:0000269|PubMed:9629924,
FT ECO:0000269|Ref.11"
FT CHAIN 2..311
FT /note="Aspartate carbamoyltransferase catalytic subunit"
FT /id="PRO_0000113128"
FT BINDING 55
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 56
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 85
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000305|PubMed:3380787"
FT BINDING 106
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 135
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 168
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000305|PubMed:3380787"
FT BINDING 230
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000305|PubMed:3380787"
FT BINDING 268
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT BINDING 269
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001,
FT ECO:0000269|PubMed:3380787"
FT CONFLICT 61
FT /note="E -> Q (in Ref. 1; AAA24474 and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="Q -> E (in Ref. 2; AAA24476)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="P -> R (in Ref. 3; AAA97142)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="A -> V (in Ref. 1; AAA24474 and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..262
FT /note="ANM -> MNA (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="R -> L (in Ref. 1; AAA24474)"
FT /evidence="ECO:0000305"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1D09"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4FYY"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2AIR"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2QGF"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3CSU"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1Q95"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2AIR"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1TTH"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:2H3E"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:3CSU"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:3CSU"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1TUG"
SQ SEQUENCE 311 AA; 34427 MW; CC2F5ACBD73E0E3E CRC64;
MANPLYQKHI ISINDLSRDD LNLVLATAAK LKANPQPELL KHKVIASCFF EASTRTRLSF
ETSMHRLGAS VVGFSDSANT SLGKKGETLA DTISVISTYV DAIVMRHPQE GAARLATEFS
GNVPVLNAGD GSNQHPTQTL LDLFTIQETQ GRLDNLHVAM VGDLKYGRTV HSLTQALAKF
DGNRFYFIAP DALAMPQYIL DMLDEKGIAW SLHSSIEEVM AEVDILYMTR VQKERLDPSE
YANVKAQFVL RASDLHNAKA NMKVLHPLPR VDEIATDVDK TPHAWYFQQA GNGIFARQAL
LALVLNRDLV L
//
