PYRI_ECOLI
ID PYRI_ECOLI Reviewed; 153 AA.
AC P0A7F3; P00478; Q2M663;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN Name=pyrI; OrderedLocusNames=b4244, JW4203;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-11.
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 [6]
RP PROTEIN SEQUENCE OF 2-13.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-153.
RX PubMed=3912513; DOI=10.1016/0022-2836(85)90390-0;
RA Cunin R., Jacobs A., Charlier D.R.M., Crabeel M., Herve G., Glansdorff N.,
RA Pierard A.;
RT "Structure-function relationship in allosteric aspartate
RT carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI
RT gene encoding a modified regulatory subunit.";
RL J. Mol. Biol. 186:707-713(1985).
RN [8]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-153.
RX PubMed=4872216; DOI=10.1038/2181116a0;
RA Weber K.;
RT "New structural model of E. coli aspartate transcarbamylase and the amino-
RT acid sequence of the regulatory polypeptide chain.";
RL Nature 218:1116-1119(1968).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=364472; DOI=10.1073/pnas.75.11.5276;
RA Monaco H.L., Crawford J.L., Lipscomb W.N.;
RT "Three-dimensional structures of aspartate carbamoyltransferase from
RT Escherichia coli and of its complex with cytidine triphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:5276-5280(1978).
RN [11]
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 [12]
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 [13]
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).
CC -!- FUNCTION: Involved in allosteric regulation of aspartate
CC carbamoyltransferase.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
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:0000269|PubMed:6377306}.
CC -!- INTERACTION:
CC P0A7F3; P0A786: pyrB; NbExp=18; IntAct=EBI-906630, EBI-906620;
CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000305}.
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DR EMBL; K01472; AAA24477.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97141.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77201.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78243.1; -; Genomic_DNA.
DR EMBL; M28578; AAA24487.1; -; Genomic_DNA.
DR PIR; A93985; DTECR.
DR RefSeq; NP_418665.1; NC_000913.3.
DR RefSeq; WP_000148581.1; NZ_STEB01000013.1.
DR PDB; 1ACM; X-ray; 2.80 A; B/D=1-153.
DR PDB; 1AT1; X-ray; 2.80 A; B/D=1-153.
DR PDB; 1D09; X-ray; 2.10 A; B/D=1-153.
DR PDB; 1EZZ; X-ray; 2.70 A; B/D=1-153.
DR PDB; 1F1B; X-ray; 2.30 A; B/D=1-153.
DR PDB; 1I5O; X-ray; 2.80 A; B/D=1-153.
DR PDB; 1NBE; X-ray; 2.60 A; B/D=1-153.
DR PDB; 1Q95; X-ray; 2.46 A; G/H/I/J/K/L=1-153.
DR PDB; 1R0B; X-ray; 2.90 A; G/H/I/J/K/L=1-153.
DR PDB; 1R0C; X-ray; 2.37 A; B/H=1-153.
DR PDB; 1RAA; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAB; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAC; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAD; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAE; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAF; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAG; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAH; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1RAI; X-ray; 2.50 A; B/D=1-153.
DR PDB; 1SKU; X-ray; 2.60 A; B/D=1-153.
DR PDB; 1TTH; X-ray; 2.80 A; B/D=1-153.
DR PDB; 1TU0; X-ray; 2.55 A; B/D=1-153.
DR PDB; 1TUG; X-ray; 2.10 A; B/D=1-153.
DR PDB; 1XJW; X-ray; 2.71 A; B/D=1-153.
DR PDB; 1ZA1; X-ray; 2.20 A; B/D=1-153.
DR PDB; 1ZA2; X-ray; 2.50 A; B/D=1-153.
DR PDB; 2A0F; X-ray; 2.90 A; B/D=1-153.
DR PDB; 2AIR; X-ray; 2.00 A; B/H=1-153.
DR PDB; 2AT1; X-ray; 2.80 A; B/D=1-153.
DR PDB; 2ATC; X-ray; 3.00 A; B=1-153.
DR PDB; 2FZC; X-ray; 2.10 A; B/D=1-153.
DR PDB; 2FZG; X-ray; 2.25 A; B/D=1-153.
DR PDB; 2FZK; X-ray; 2.50 A; B/D=1-153.
DR PDB; 2H3E; X-ray; 2.30 A; B/D=1-153.
DR PDB; 2HSE; X-ray; 2.60 A; B/D=1-153.
DR PDB; 2IPO; X-ray; 2.60 A; B/D=1-153.
DR PDB; 2QG9; X-ray; 2.70 A; B/D=1-153.
DR PDB; 2QGF; X-ray; 2.20 A; B/D=1-153.
DR PDB; 3AT1; X-ray; 2.80 A; B/D=1-153.
DR PDB; 3D7S; X-ray; 2.80 A; B/D=1-153.
DR PDB; 3MPU; X-ray; 2.86 A; B/D/F=1-153.
DR PDB; 4AT1; X-ray; 2.60 A; B/D=1-153.
DR PDB; 4E2F; X-ray; 2.80 A; B/D/F/H/J/L=1-153.
DR PDB; 4F04; X-ray; 2.30 A; B/D=1-153.
DR PDB; 4FYV; X-ray; 2.10 A; B/D=1-153.
DR PDB; 4FYW; X-ray; 2.10 A; B/D=1-153.
DR PDB; 4FYX; X-ray; 2.09 A; B/D=1-153.
DR PDB; 4FYY; X-ray; 1.94 A; B/D=1-153.
DR PDB; 5AT1; X-ray; 2.60 A; B/D=1-153.
DR PDB; 6AT1; X-ray; 2.60 A; B/D=1-153.
DR PDB; 6KJ8; X-ray; 3.01 A; B/D/F=1-153.
DR PDB; 6KJA; X-ray; 3.06 A; B/D/F=1-153.
DR PDB; 6KJB; X-ray; 2.06 A; B=1-153.
DR PDB; 7AT1; X-ray; 2.80 A; B/D=1-153.
DR PDB; 8AT1; X-ray; 2.80 A; B/D=1-153.
DR PDB; 8ATC; X-ray; 2.50 A; B/D=1-153.
DR PDB; 9ATC; X-ray; 2.40 A; B=8-153.
DR PDBsum; 1ACM; -.
DR PDBsum; 1AT1; -.
DR PDBsum; 1D09; -.
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; 3D7S; -.
DR PDBsum; 3MPU; -.
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; 6AT1; -.
DR PDBsum; 6KJ8; -.
DR PDBsum; 6KJA; -.
DR PDBsum; 6KJB; -.
DR PDBsum; 7AT1; -.
DR PDBsum; 8AT1; -.
DR PDBsum; 8ATC; -.
DR PDBsum; 9ATC; -.
DR AlphaFoldDB; P0A7F3; -.
DR SMR; P0A7F3; -.
DR BioGRID; 4263117; 11.
DR BioGRID; 853052; 1.
DR ComplexPortal; CPX-3091; Aspartate carbamoyltransferase complex.
DR DIP; DIP-35088N; -.
DR IntAct; P0A7F3; 2.
DR MINT; P0A7F3; -.
DR STRING; 511145.b4244; -.
DR SWISS-2DPAGE; P0A7F3; -.
DR jPOST; P0A7F3; -.
DR PaxDb; P0A7F3; -.
DR PRIDE; P0A7F3; -.
DR EnsemblBacteria; AAC77201; AAC77201; b4244.
DR EnsemblBacteria; BAE78243; BAE78243; BAE78243.
DR GeneID; 67414869; -.
DR GeneID; 948763; -.
DR KEGG; ecj:JW4203; -.
DR KEGG; eco:b4244; -.
DR PATRIC; fig|1411691.4.peg.2457; -.
DR EchoBASE; EB0804; -.
DR eggNOG; COG1781; Bacteria.
DR HOGENOM; CLU_128576_0_0_6; -.
DR InParanoid; P0A7F3; -.
DR OMA; CPNRNCI; -.
DR PhylomeDB; P0A7F3; -.
DR BioCyc; EcoCyc:ASPCARBREG-MON; -.
DR BioCyc; MetaCyc:ASPCARBREG-MON; -.
DR EvolutionaryTrace; P0A7F3; -.
DR PRO; PR:P0A7F3; -.
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:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.140; -; 1.
DR HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR PANTHER; PTHR35805; PTHR35805; 1.
DR Pfam; PF01948; PyrI; 1.
DR Pfam; PF02748; PyrI_C; 1.
DR SUPFAM; SSF54893; SSF54893; 1.
DR SUPFAM; SSF57825; SSF57825; 1.
DR TIGRFAMs; TIGR00240; ATCase_reg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding;
KW Pyrimidine biosynthesis; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.5"
FT CHAIN 2..153
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000142303"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1TUG"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:4FYY"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4FYY"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:4FYY"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:4FYY"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:4FYY"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:4FYY"
FT TURN 73..77
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2QG9"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1EZZ"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1RAD"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:4FYY"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:4FYY"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4FYY"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4FYY"
SQ SEQUENCE 153 AA; 17121 MW; 81A1631614E549EA CRC64;
MTHDNKLQVE AIKRGTVIDH IPAQIGFKLL SLFKLTETDQ RITIGLNLPS GEMGRKDLIK
IENTFLSEDQ VDQLALYAPQ ATVNRIDNYE VVGKSRPSLP ERIDNVLVCP NSNCISHAEP
VSSSFAVRKR ANDIALKCKY CEKEFSHNVV LAN
