GALU_ECOLI
ID GALU_ECOLI Reviewed; 302 AA.
AC P0AEP3; P25520;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000303|PubMed:7961613};
DE EC=2.7.7.9 {ECO:0000269|PubMed:7961613};
DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase {ECO:0000303|PubMed:8169209};
DE AltName: Full=UDP-Glc PPase {ECO:0000303|PubMed:7961613};
DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000303|PubMed:7961613};
DE Short=UDPGP;
DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase;
GN Name=galU; Synonyms=ychD; OrderedLocusNames=b1236, JW1224;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1537791; DOI=10.1128/jb.174.5.1454-1461.1992;
RA Ueguchi C., Ito K.;
RT "Multicopy suppression: an approach to understanding intracellular
RT functioning of the protein export system.";
RL J. Bacteriol. 174:1454-1461(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=8169209; DOI=10.1128/jb.176.9.2611-2618.1994;
RA Weissborn A.C., Liu Q., Rumley M.K., Kennedy E.P.;
RT "UTP: alpha-D-glucose-1-phosphate uridylyltransferase of Escherichia coli:
RT isolation and DNA sequence of the galU gene and purification of the
RT enzyme.";
RL J. Bacteriol. 176:2611-2618(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RC STRAIN=K12;
RX PubMed=7961613; DOI=10.1093/oxfordjournals.jbchem.a124446;
RA Hossain S.A., Tanizawa K., Kazuta Y., Fukui T.;
RT "Overproduction and characterization of recombinant UDP-glucose
RT pyrophosphorylase from Escherichia coli K-12.";
RL J. Biochem. 115:965-972(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-18.
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).
CC -!- FUNCTION: May play a role in stationary phase survival.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58885; EC=2.7.7.9; Evidence={ECO:0000269|PubMed:7961613};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:7961613};
CC -!- SUBUNIT: Homotetramer or homopentamer. {ECO:0000269|PubMed:8169209}.
CC -!- SIMILARITY: Belongs to the UDPGP type 2 family. {ECO:0000305}.
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DR EMBL; X59940; CAA42564.1; -; Genomic_DNA.
DR EMBL; M98830; AAA20118.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC74318.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36104.1; -; Genomic_DNA.
DR PIR; G64870; JC2265.
DR RefSeq; NP_415752.1; NC_000913.3.
DR RefSeq; WP_000718995.1; NZ_STEB01000005.1.
DR PDB; 2E3D; X-ray; 1.95 A; A/B/C/D=1-302.
DR PDBsum; 2E3D; -.
DR AlphaFoldDB; P0AEP3; -.
DR SMR; P0AEP3; -.
DR BioGRID; 4260121; 447.
DR DIP; DIP-35950N; -.
DR IntAct; P0AEP3; 3.
DR STRING; 511145.b1236; -.
DR jPOST; P0AEP3; -.
DR PaxDb; P0AEP3; -.
DR PRIDE; P0AEP3; -.
DR EnsemblBacteria; AAC74318; AAC74318; b1236.
DR EnsemblBacteria; BAA36104; BAA36104; BAA36104.
DR GeneID; 66674942; -.
DR GeneID; 945730; -.
DR KEGG; ecj:JW1224; -.
DR KEGG; eco:b1236; -.
DR PATRIC; fig|1411691.4.peg.1049; -.
DR EchoBASE; EB1295; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_1_6; -.
DR InParanoid; P0AEP3; -.
DR OMA; KRYDVGN; -.
DR PhylomeDB; P0AEP3; -.
DR BioCyc; EcoCyc:GLUC1PURIDYLTRANS-MON; -.
DR BioCyc; MetaCyc:GLUC1PURIDYLTRANS-MON; -.
DR BRENDA; 2.7.7.9; 2026.
DR SABIO-RK; P0AEP3; -.
DR EvolutionaryTrace; P0AEP3; -.
DR PRO; PR:P0AEP3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0009242; P:colanic acid biosynthetic process; IMP:EcoCyc.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IMP:EcoCyc.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR GO; GO:1900727; P:osmoregulated periplasmic glucan biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IMP:EcoCyc.
DR CDD; cd02541; UGPase_prokaryotic; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43197; PTHR43197; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01099; galU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Magnesium; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8169209,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..302
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000201354"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2E3D"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2E3D"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:2E3D"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2E3D"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:2E3D"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2E3D"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:2E3D"
SQ SEQUENCE 302 AA; 32942 MW; ADEAEB3F6A1194CB CRC64;
MAAINTKVKK AVIPVAGLGT RMLPATKAIP KEMLPLVDKP LIQYVVNECI AAGITEIVLV
THSSKNSIEN HFDTSFELEA MLEKRVKRQL LDEVQSICPP HVTIMQVRQG LAKGLGHAVL
CAHPVVGDEP VAVILPDVIL DEYESDLSQD NLAEMIRRFD ETGHSQIMVE PVADVTAYGV
VDCKGVELAP GESVPMVGVV EKPKADVAPS NLAIVGRYVL SADIWPLLAK TPPGAGDEIQ
LTDAIDMLIE KETVEAYHMK GKSHDCGNKL GYMQAFVEYG IRHNTLGTEF KAWLEEEMGI
KK
