GLMU_ECOLI
ID GLMU_ECOLI Reviewed; 456 AA.
AC P0ACC7; P17114; P76746; Q2M848;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Bifunctional protein GlmU {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.7.7.23 {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE Includes:
DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01631};
DE EC=2.3.1.157 {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230};
GN Name=glmU {ECO:0000255|HAMAP-Rule:MF_01631}; Synonyms=yieA;
GN OrderedLocusNames=b3730, JW3708;
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=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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 IDENTIFICATION.
RX PubMed=8407787; DOI=10.1128/jb.175.19.6150-6157.1993;
RA Mengin-Lecreulx D., van Heijenoort J.;
RT "Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate
RT uridyltransferase in Escherichia coli.";
RL J. Bacteriol. 175:6150-6157(1993).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=8083170; DOI=10.1128/jb.176.18.5788-5795.1994;
RA Mengin-Lecreulx D., van Heijenoort J.;
RT "Copurification of glucosamine-1-phosphate acetyltransferase and N-
RT acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia
RT coli: characterization of the glmU gene product as a bifunctional enzyme
RT catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine
RT synthesis.";
RL J. Bacteriol. 176:5788-5795(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8555230; DOI=10.1021/bi952275a;
RA Gehring A.M., Lees W.J., Mindiola D.J., Walsh C.T., Brown E.D.;
RT "Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-
RT acetylglucosamine in separable active sites of the bifunctional GlmU
RT protein of Escherichia coli.";
RL Biochemistry 35:579-585(1996).
RN [8]
RP MUTAGENESIS OF CYS-296; CYS-307; CYS-324 AND CYS-385, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9733680; DOI=10.1128/jb.180.18.4799-4803.1998;
RA Pompeo F., van Heijenoort J., Mengin-Lecreulx D.;
RT "Probing the role of cysteine residues in glucosamine-1-phosphate
RT acetyltransferase activity of the bifunctional protein glmU from
RT Escherichia coli: site-directed mutagenesis and characterization of the
RT mutant enzymes.";
RL J. Bacteriol. 180:4799-4803(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF THE TRUNCATED FORM AND IN COMPLEX
RP WITH UDP-GLCNAC, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF GLY-14; ARG-18 AND LYS-25, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=10428949; DOI=10.1093/emboj/18.15.4096;
RA Brown K., Pompeo F., Dixon S., Mengin-Lecreulx D., Cambillau C., Bourne Y.;
RT "Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate
RT uridyltransferase from Escherichia coli: a paradigm for the related
RT pyrophosphorylase superfamily.";
RL EMBO J. 18:4096-4107(1999).
RN [10] {ECO:0007744|PDB:1HV9}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; COA AND
RP COBALT ION, COFACTOR, AND SUBUNIT.
RX PubMed=11329257; DOI=10.1021/bi002503n;
RA Olsen L.R., Roderick S.L.;
RT "Structure of the Escherichia coli glmU pyrophosphorylase and
RT acetyltransferase active sites.";
RL Biochemistry 40:1913-1921(2001).
RN [11] {ECO:0007744|PDB:2OI5, ECO:0007744|PDB:2OI6, ECO:0007744|PDB:2OI7}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC, COA AND
RP MAGNESIUM IONS, COFACTOR, AND SUBUNIT.
RX PubMed=17473010; DOI=10.1110/ps.072779707;
RA Olsen L.R., Vetting M.W., Roderick S.L.;
RT "Structure of the E. coli bifunctional GlmU acetyltransferase active site
RT with substrates and products.";
RL Protein Sci. 16:1230-1235(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 233-452 ACETYL-COA ANALOG,
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=21984832; DOI=10.1074/jbc.m111.274068;
RA Buurman E.T., Andrews B., Gao N., Hu J., Keating T.A., Lahiri S.,
RA Otterbein L.R., Patten A.D., Stokes S.S., Shapiro A.B.;
RT "In vitro validation of acetyltransferase activity of GlmU as an
RT antibacterial target in Haemophilus influenzae.";
RL J. Biol. Chem. 286:40734-40742(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 227-456, FUNCTION, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=22297115; DOI=10.1016/j.bmcl.2012.01.016;
RA Green O.M., McKenzie A.R., Shapiro A.B., Otterbein L., Ni H., Patten A.,
RA Stokes S., Albert R., Kawatkar S., Breed J.;
RT "Inhibitors of acetyltransferase domain of N-acetylglucosamine-1-phosphate-
RT uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). Part 1:
RT Hit to lead evaluation of a novel arylsulfonamide series.";
RL Bioorg. Med. Chem. Lett. 22:1510-1519(2012).
CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de novo
CC biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-
CC terminal domain catalyzes the transfer of acetyl group from acetyl
CC coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-
CC acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into
CC UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-
CC triphosphate), a reaction catalyzed by the N-terminal domain.
CC {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949,
CC ECO:0000269|PubMed:21984832, ECO:0000269|PubMed:22297115,
CC ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + H(+) + N-
CC acetyl-alpha-D-glucosamine 1-phosphate; Xref=Rhea:RHEA:13725,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57776, ChEBI:CHEBI:58516; EC=2.3.1.157;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17473010};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:11329257};
CC Note=Binds 1 Mg(2+) ion per subunit (PubMed:17473010). Can also use
CC Co(2+) ion to a lesser extent (PubMed:11329257).
CC {ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010};
CC -!- ACTIVITY REGULATION: Inhibited by its reaction product N-
CC acetylglucosamine-1-phosphate and by UDP-N-acetylmuramic acid, which is
CC one of the first precursors specific for the peptidoglycan pathway.
CC {ECO:0000269|PubMed:21984832, ECO:0000269|PubMed:22297115,
CC ECO:0000269|PubMed:8083170}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.018 mM for N-acetylglucosamine 1-phosphate
CC {ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230,
CC ECO:0000269|PubMed:9733680};
CC KM=0.07 mM for alpha-D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:10428949};
CC KM=0.1 mM for UTP {ECO:0000269|PubMed:10428949};
CC KM=0.15 mM for alpha-D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230,
CC ECO:0000269|PubMed:9733680};
CC KM=0.25 mM for alpha-D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230,
CC ECO:0000269|PubMed:9733680};
CC KM=0.32 mM for acetyl-CoA {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=0.6 mM for acetyl-CoA {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=0.84 mM for n-propionyl-CoA {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=1.3 mM for UDP-glucosamine {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=2 mM for glucose-1-P {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=3.7 mM for N-acetylgalactosamine-1-P {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC KM=15 mM for galactosamine-1-phosphate {ECO:0000269|PubMed:8083170,
CC ECO:0000269|PubMed:8555230, ECO:0000269|PubMed:9733680};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route II): step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01631}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01631}.
CC -!- SUBUNIT: Homotrimer. In vivo forms a hexameric aggregate.
CC {ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
CC ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832,
CC ECO:0000269|PubMed:22297115}.
CC -!- INTERACTION:
CC P0ACC7; P0A7V0: rpsB; NbExp=2; IntAct=EBI-370256, EBI-543439;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000269|PubMed:10428949}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000255|HAMAP-Rule:MF_01631,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62081.1; Type=Frameshift; Note=Produces two ORFs.; Evidence={ECO:0000305};
CC Sequence=AAA62082.1; Type=Frameshift; Note=Produces two ORFs.; Evidence={ECO:0000305};
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DR EMBL; X01631; CAA25784.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62082.1; ALT_FRAME; Genomic_DNA.
DR EMBL; L10328; AAA62081.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC76753.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77558.1; -; Genomic_DNA.
DR PIR; C65176; C65176.
DR RefSeq; NP_418186.1; NC_000913.3.
DR RefSeq; WP_000933736.1; NZ_STEB01000015.1.
DR PDB; 1FWY; X-ray; 2.30 A; A/B=1-331.
DR PDB; 1FXJ; X-ray; 2.25 A; A/B=1-331.
DR PDB; 1HV9; X-ray; 2.10 A; A/B=1-456.
DR PDB; 2OI5; X-ray; 2.25 A; A/B=1-456.
DR PDB; 2OI6; X-ray; 2.20 A; A/B=1-456.
DR PDB; 2OI7; X-ray; 2.54 A; A/B=1-456.
DR PDB; 3TWD; X-ray; 1.90 A; A/B=233-452.
DR PDB; 4AA7; X-ray; 2.00 A; A/B=227-456.
DR PDBsum; 1FWY; -.
DR PDBsum; 1FXJ; -.
DR PDBsum; 1HV9; -.
DR PDBsum; 2OI5; -.
DR PDBsum; 2OI6; -.
DR PDBsum; 2OI7; -.
DR PDBsum; 3TWD; -.
DR PDBsum; 4AA7; -.
DR AlphaFoldDB; P0ACC7; -.
DR SMR; P0ACC7; -.
DR BioGRID; 4262143; 312.
DR BioGRID; 852548; 1.
DR DIP; DIP-31844N; -.
DR IntAct; P0ACC7; 19.
DR STRING; 511145.b3730; -.
DR BindingDB; P0ACC7; -.
DR ChEMBL; CHEMBL3414415; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03397; Uridine-Diphosphate-N-Acetylglucosamine.
DR jPOST; P0ACC7; -.
DR PaxDb; P0ACC7; -.
DR PRIDE; P0ACC7; -.
DR EnsemblBacteria; AAC76753; AAC76753; b3730.
DR EnsemblBacteria; BAE77558; BAE77558; BAE77558.
DR GeneID; 66672366; -.
DR GeneID; 948246; -.
DR KEGG; ecj:JW3708; -.
DR KEGG; eco:b3730; -.
DR PATRIC; fig|1411691.4.peg.2970; -.
DR EchoBASE; EB1184; -.
DR eggNOG; COG1207; Bacteria.
DR HOGENOM; CLU_029499_15_2_6; -.
DR InParanoid; P0ACC7; -.
DR OMA; TAIVEHK; -.
DR PhylomeDB; P0ACC7; -.
DR BioCyc; EcoCyc:NAG1P-URIDYLTRANS-MON; -.
DR BioCyc; MetaCyc:NAG1P-URIDYLTRANS-MON; -.
DR BRENDA; 2.3.1.157; 2026.
DR BRENDA; 2.7.7.23; 2026.
DR SABIO-RK; P0ACC7; -.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR UniPathway; UPA00973; -.
DR EvolutionaryTrace; P0ACC7; -.
DR PRO; PR:P0ACC7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; 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:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:EcoCyc.
DR GO; GO:0000902; P:cell morphogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc.
DR CDD; cd03353; LbH_GlmU_C; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01631; GlmU; 1.
DR InterPro; IPR005882; Bifunctional_GlmU.
DR InterPro; IPR038009; GlmU_C_LbH.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF14602; Hexapep_2; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01173; glmU; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell shape;
KW Cell wall biogenesis/degradation; Cobalt; Cytoplasm; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotidyltransferase;
KW Peptidoglycan synthesis; Reference proteome; Repeat; Transferase.
FT CHAIN 1..456
FT /note="Bifunctional protein GlmU"
FT /id="PRO_0000068701"
FT REGION 1..229
FT /note="Pyrophosphorylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8555230"
FT REGION 230..250
FT /note="Linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8555230"
FT REGION 251..456
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:8555230"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 11..14
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 25
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 76
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 81..82
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 103..105
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 105
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11329257,
FT ECO:0007744|PDB:1HV9"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17473010,
FT ECO:0007744|PDB:2OI5"
FT BINDING 140
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 154
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 169
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257,
FT ECO:0000269|PubMed:17473010"
FT BINDING 227
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000269|PubMed:11329257,
FT ECO:0007744|PDB:1HV9"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17473010,
FT ECO:0007744|PDB:2OI5"
FT BINDING 227
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 333
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010"
FT BINDING 351
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010"
FT BINDING 366
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010"
FT BINDING 377
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010,
FT ECO:0000269|PubMed:21984832"
FT BINDING 380
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:17473010, ECO:0000269|PubMed:21984832"
FT BINDING 386..387
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631"
FT BINDING 405
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010,
FT ECO:0000269|PubMed:21984832"
FT BINDING 423
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010,
FT ECO:0000269|PubMed:21984832"
FT BINDING 440
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01631,
FT ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010,
FT ECO:0000269|PubMed:21984832"
FT MUTAGEN 14
FT /note="G->A: 8-fold decrease in uridyltransferase activity.
FT Creates steric conflict and decreases affinity for UTP."
FT /evidence="ECO:0000269|PubMed:10428949"
FT MUTAGEN 18
FT /note="R->A: Dramatically impairs the uridyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:10428949"
FT MUTAGEN 25
FT /note="K->A: 8-fold decrease in uridyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:10428949"
FT MUTAGEN 296
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9733680"
FT MUTAGEN 307
FT /note="C->A: 1350-fold decrease in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:9733680"
FT MUTAGEN 324
FT /note="C->A: 8-fold decrease in acetyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:9733680"
FT MUTAGEN 385
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:9733680"
FT CONFLICT 186..187
FT /note="KL -> NV (in Ref. 1; CAA25784)"
FT /evidence="ECO:0000305"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:1HV9"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1FXJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1HV9"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1HV9"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1HV9"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1HV9"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3TWD"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1FXJ"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4AA7"
FT STRAND 343..355
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 360..372
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:2OI6"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:3TWD"
FT STRAND 408..415
FT /evidence="ECO:0007829|PDB:3TWD"
SQ SEQUENCE 456 AA; 49190 MW; 2F3C5C84F673C8A3 CRC64;
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD
LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA
KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM
KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ
SEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK
AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT
IAAGTTVTRN VGENALAISR VPQTQKEGWR RPVKKK
