S1PNA_SULTO
ID S1PNA_SULTO Reviewed; 401 AA.
AC Q975F9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase {ECO:0000305};
DE Includes:
DE RecName: Full=Sugar-1-phosphate nucleotidylyltransferase {ECO:0000303|PubMed:15598657};
DE Short=Sugar-1-P NTase {ECO:0000303|PubMed:20400541};
DE AltName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000303|PubMed:15598657};
DE EC=2.7.7.24 {ECO:0000269|PubMed:15598657};
DE AltName: Full=Glucose-1-phosphate uridylyltransferase {ECO:0000305};
DE Short=Glc-1-P UTase {ECO:0000303|PubMed:27864169};
DE EC=2.7.7.9 {ECO:0000269|PubMed:27864169, ECO:0000269|PubMed:30291121};
DE AltName: Full=N-acetylgalactosamine-1-phosphate uridyltransferase {ECO:0000303|PubMed:20400541};
DE Short=GalNAc-1-P UTase {ECO:0000303|PubMed:20400541};
DE EC=2.7.7.83 {ECO:0000269|PubMed:20400541};
DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase {ECO:0000303|PubMed:15598657};
DE Short=GlcNAc-1-P UTase {ECO:0000303|PubMed:20400541};
DE EC=2.7.7.23 {ECO:0000269|PubMed:15598657, ECO:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746, ECO:0000269|PubMed:27864169, ECO:0000269|PubMed:30291121};
DE Includes:
DE RecName: Full=Sugar-1-phosphate acetyltransferase {ECO:0000305};
DE AltName: Full=Galactosamine-1-phosphate N-acetyltransferase {ECO:0000303|PubMed:20400541};
DE Short=GalN-1-P AcTase {ECO:0000303|PubMed:25567746};
DE Short=GalN-1-P acetyltransferase {ECO:0000303|PubMed:20400541};
DE EC=2.3.1.276 {ECO:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746};
DE AltName: Full=Glucosamine-1-phosphate N-acetyltransferase {ECO:0000303|PubMed:20400541};
DE Short=GlcN-1-P AcTase {ECO:0000303|PubMed:25567746};
DE Short=GlcN-1-P acetyltransferase {ECO:0000303|PubMed:20400541};
DE EC=2.3.1.157 {ECO:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746};
GN OrderedLocusNames=STK_04520 {ECO:0000312|EMBL:BAB65442.1};
GN ORFNames=ST0452 {ECO:0000303|PubMed:15598657};
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP FUNCTION AS A NUCLEOTIDYLYLTRANSFERASE, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=15598657; DOI=10.1074/jbc.m411211200;
RA Zhang Z., Tsujimura M., Akutsu J., Sasaki M., Tajima H., Kawarabayasi Y.;
RT "Identification of an extremely thermostable enzyme with dual sugar-1-
RT phosphate nucleotidylyltransferase activities from an acidothermophilic
RT archaeon, Sulfolobus tokodaii strain 7.";
RL J. Biol. Chem. 280:9698-9705(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=20400541; DOI=10.1128/jb.01683-09;
RA Zhang Z., Akutsu J., Kawarabayasi Y.;
RT "Identification of novel acetyltransferase activity on the thermostable
RT protein ST0452 from Sulfolobus tokodaii strain 7.";
RL J. Bacteriol. 192:3287-3293(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF HIS-308; TYR-311; ASN-331; LYS-337; LYS-340;
RP 391-ARG--VAL-401 AND 397-GLU--VAL-401.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=25567746; DOI=10.1007/s00792-014-0727-9;
RA Zhang Z., Shimizu Y., Kawarabayasi Y.;
RT "Characterization of the amino acid residues mediating the unique amino-
RT sugar-1-phosphate acetyltransferase activity of the archaeal ST0452
RT protein.";
RL Extremophiles 19:417-427(2015).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF TYR-97.
RX PubMed=27864169; DOI=10.1128/aem.02291-16;
RA Honda Y., Zang Q., Shimizu Y., Dadashipour M., Zhang Z., Kawarabayasi Y.;
RT "Increasing the thermostable sugar-1-phosphate nucleotidylyltransferase
RT activities of the archaeal ST0452 protein through site saturation
RT mutagenesis of the 97th amino acid position.";
RL Appl. Environ. Microbiol. 83:E02291-E02291(2017).
RN [6] {ECO:0007744|PDB:2GGO, ECO:0007744|PDB:2GGQ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP TTP.
RA Rajakannan V., Yamane T.;
RT "Crystal structure of glucose-1-phosphate thymidylyltransferase from
RT Sulfolobus tokodaii.";
RL Submitted (MAR-2006) to the PDB data bank.
RN [7] {ECO:0007744|PDB:5Z09, ECO:0007744|PDB:5Z0A}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF MUTANT ASN-97 IN COMPLEXES WITH
RP UTP AND GLCNAC, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-80;
RP TYR-97 AND GLU-146.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=30291121; DOI=10.1128/aem.02213-18;
RA Honda Y., Nakano S., Ito S., Dadashipour M., Zhang Z., Kawarabayasi Y.;
RT "Improvement of ST0452 GlcNAc-1-phosphate uridyltransferase activity by the
RT cooperative effect of two single mutations identified through structure-
RT based protein engineering.";
RL Appl. Environ. Microbiol. 84:E02213-E02213(2018).
CC -!- FUNCTION: Bifunctional enzyme involved in the synthesis of UDP-N-
CC acetylglucosamine (UDP-GlcNAc) and UDP-N-acetylgalactosamine (UDP-
CC GalNAc). It has multiple amino-sugar-1-phosphate acetyltransferase
CC activities, including glucosamine-1-phosphate (GlcN-1-P)
CC acetyltransferase and galactosamine-1-phosphate (GalN-1-P)
CC acetyltransferase activities, and multiple sugar-1-phosphate
CC nucleotidylyltransferase activities, including N-acetylglucosamine-1-
CC phosphate (GlcNAc-1-P) uridyltransferase and N-acetylgalactosamine-1-
CC phosphate (GalNAc-1-P) uridyltransferase activities (PubMed:15598657,
CC PubMed:20400541, PubMed:25567746). Also catalyzes the formation of
CC dTDP-glucose from dTTP and glucose-1-phosphate (Glc-1-P), and the
CC reverse reaction, which produces dTTP from dTDP-glucose and diphosphate
CC (PubMed:15598657). Can also catalyze the formation of UDP-glucose from
CC UTP and glucose-1-phosphate (PubMed:27864169, PubMed:30291121).
CC {ECO:0000269|PubMed:15598657, ECO:0000269|PubMed:20400541,
CC ECO:0000269|PubMed:25567746, ECO:0000269|PubMed:27864169,
CC ECO:0000269|PubMed:30291121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:58601; EC=2.7.7.24;
CC Evidence={ECO:0000269|PubMed:15598657};
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:27864169,
CC ECO:0000269|PubMed:30291121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:34363, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61970, ChEBI:CHEBI:67138; EC=2.7.7.83;
CC Evidence={ECO:0000269|PubMed:20400541};
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:0000269|PubMed:15598657, ECO:0000269|PubMed:20400541,
CC ECO:0000269|PubMed:25567746, ECO:0000269|PubMed:27864169,
CC ECO:0000269|PubMed:30291121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + alpha-D-galactosamine 1-phosphate = CoA + H(+) +
CC N-acetyl-alpha-D-galactosamine 1-phosphate; Xref=Rhea:RHEA:17169,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61970, ChEBI:CHEBI:142399; EC=2.3.1.276;
CC Evidence={ECO:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746};
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:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15598657};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15598657};
CC Note=Can also use Mg(2+) and Zn(2+), with lower efficiency. Important
CC for nucleotidylyltransferase activity. {ECO:0000269|PubMed:15598657};
CC -!- ACTIVITY REGULATION: GlcN-1-P acetyltransferase activity is inhibited
CC by divalent cations. GalN-1-P acetyltransferase activity is enhanced by
CC Co(2+), Mg(2+) and Ca(2+), but inhibited by Zn(2+) or Mn(2+).
CC {ECO:0000269|PubMed:20400541}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.71 mM for GalN-1-P {ECO:0000269|PubMed:20400541,
CC ECO:0000269|PubMed:25567746};
CC KM=0.59 mM for GlcN-1-P {ECO:0000269|PubMed:20400541,
CC ECO:0000269|PubMed:25567746};
CC KM=0.63 mM for acetyl-CoA (in the presence of GalN-1-P or GlcN-1-P)
CC {ECO:0000269|PubMed:20400541, ECO:0000269|PubMed:25567746};
CC KM=0.068 mM for GlcNAc-1-P {ECO:0000269|PubMed:27864169};
CC KM=1.23 mM for Glc-1-P (in the presence of UTP)
CC {ECO:0000269|PubMed:27864169};
CC KM=1.12 mM for Glc-1-P (in the presence of dTTP)
CC {ECO:0000269|PubMed:15598657};
CC KM=0.02 mM for dTTP {ECO:0000269|PubMed:15598657};
CC KM=0.05 mM for dTDP-alpha-D-glucose for the reverse reaction of the
CC glucose-1-phosphate thymidylyltransferase activity
CC {ECO:0000269|PubMed:15598657};
CC KM=0.39 mM for diphosphate for the reverse reaction of the glucose-1-
CC phosphate thymidylyltransferase activity
CC {ECO:0000269|PubMed:15598657};
CC KM=0.056 mM for UDP-GalNAc for the reverse reaction of the GalNAc-1-P
CC UTase activity {ECO:0000269|PubMed:20400541};
CC KM=0.016 mM for UDP-GlcNAc for the reverse reaction of the GlcNAc-1-P
CC UTase activity {ECO:0000269|PubMed:20400541};
CC Vmax=1.46 umol/min/mg enzyme for the forward reaction with alpha-D-
CC glucose 1-phosphate as substrate {ECO:0000269|PubMed:15598657};
CC Vmax=13.65 umol/min/mg enzyme for the reverse reaction with dTDP-
CC alpha-D-glucose as substrate {ECO:0000269|PubMed:15598657};
CC Note=kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity.
CC kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.
CC {ECO:0000269|PubMed:20400541};
CC pH dependence:
CC Optimum pH is 8.5 for glucose-1-phosphate thymidylyltransferase
CC activity. {ECO:0000269|PubMed:15598657};
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius for glucose-1-phosphate
CC thymidylyltransferase activity. {ECO:0000269|PubMed:15598657};
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:0000269|PubMed:20400541}.
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.
CC {ECO:0000269|PubMed:20400541}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:25567746}.
CC -!- DOMAIN: The C-terminal domain is essential for the formation of the
CC trimer and the high thermostability of the entire protein. The C-
CC terminal 11 residues are important for GalN-1-P AcTase activity, but
CC they have an inhibitory effect on the GlcN-1-P AcTase activity.
CC {ECO:0000269|PubMed:25567746}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-
CC acetylglucosamine-1-phosphate uridyltransferase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase
CC hexapeptide repeat family. {ECO:0000305}.
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DR EMBL; BA000023; BAB65442.1; -; Genomic_DNA.
DR RefSeq; WP_010978425.1; NC_003106.2.
DR PDB; 2GGO; X-ray; 1.80 A; A=1-401.
DR PDB; 2GGQ; X-ray; 2.00 A; A=1-401.
DR PDB; 5Z09; X-ray; 2.91 A; A/B/C/D/E/F=1-401.
DR PDB; 5Z0A; X-ray; 2.09 A; A/B/C/D/E/F=1-401.
DR PDBsum; 2GGO; -.
DR PDBsum; 2GGQ; -.
DR PDBsum; 5Z09; -.
DR PDBsum; 5Z0A; -.
DR AlphaFoldDB; Q975F9; -.
DR SMR; Q975F9; -.
DR STRING; 273063.STK_04520; -.
DR EnsemblBacteria; BAB65442; BAB65442; STK_04520.
DR GeneID; 42799991; -.
DR KEGG; sto:STK_04520; -.
DR PATRIC; fig|273063.9.peg.524; -.
DR eggNOG; arCOG00666; Archaea.
DR OMA; TAIVEHK; -.
DR OrthoDB; 61185at2157; -.
DR BioCyc; MetaCyc:MON-20592; -.
DR BRENDA; 2.3.1.157; 15396.
DR BRENDA; 2.3.1.276; 15396.
DR BRENDA; 2.7.7.23; 15396.
DR BRENDA; 2.7.7.24; 15396.
DR BRENDA; 2.7.7.37; 15396.
DR BRENDA; 2.7.7.83; 15396.
DR BRENDA; 2.7.7.9; 15396.
DR BRENDA; 2.7.7.B18; 15396.
DR BRENDA; 2.7.7.B19; 15396.
DR BRENDA; 2.7.7.B20; 15396.
DR BRENDA; 2.7.7.B21; 15396.
DR UniPathway; UPA00113; UER00532.
DR UniPathway; UPA00113; UER00533.
DR EvolutionaryTrace; Q975F9; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0052630; F:UDP-N-acetylgalactosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03992; Arch_glmU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cobalt; Manganese; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..401
FT /note="Bifunctional sugar-1-phosphate
FT nucleotidylyltransferase/acetyltransferase"
FT /id="PRO_0000448068"
FT REGION 1..220
FT /note="Nucleotidylyltransferase"
FT /evidence="ECO:0000305"
FT REGION 236..401
FT /note="Acetyltransferase"
FT /evidence="ECO:0000305"
FT BINDING 8..13
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:30291121, ECO:0000269|Ref.6"
FT BINDING 73
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:30291121, ECO:0000269|Ref.6"
FT BINDING 79
FT /ligand="a ribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61557"
FT /evidence="ECO:0000269|PubMed:30291121, ECO:0000269|Ref.6"
FT BINDING 80
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000305|PubMed:30291121,
FT ECO:0007744|PDB:5Z0A"
FT BINDING 97
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000305|PubMed:30291121,
FT ECO:0007744|PDB:5Z0A"
FT BINDING 131
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000305|PubMed:30291121,
FT ECO:0007744|PDB:5Z0A"
FT BINDING 146
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000305|PubMed:30291121,
FT ECO:0007744|PDB:5Z0A"
FT BINDING 157
FT /ligand="N-acetyl-alpha-D-glucosamine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57776"
FT /evidence="ECO:0000305|PubMed:30291121,
FT ECO:0007744|PDB:5Z0A"
FT MUTAGEN 80
FT /note="T->A,G,Q: Increases both GlcNAc-1-P UTase and Glc-1-
FT P UTase activities."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 80
FT /note="T->D,H: Decrease in GlcNAc-1-P UTase activity but
FT increase in Glc-1-P UTase activity."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 80
FT /note="T->E,K,L,M,R,W,Y: Strong decrease in GlcNAc-1-P
FT UTase activity and loss of Glc-1-P UTase activity."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 80
FT /note="T->F,I: Loss of both GlcNAc-1-P UTase and Glc-1-P
FT UTase activities."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 80
FT /note="T->N,S: Strong increase in GlcNAc-1-P UTase activity
FT and decrease in Glc-1-P UTase activity."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 80
FT /note="T->N: Loss of GlcNAc-1-P UTase activity; when
FT associated with V-97."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 97
FT /note="Y->A,D,F,G,I,K,T,V: Increases GlcNAc-1-P UTase
FT activity. Decreases Glc-1-P UTase activity."
FT /evidence="ECO:0000269|PubMed:27864169"
FT MUTAGEN 97
FT /note="Y->C,E,P,R,W: Decreases GlcNAc-1-P UTase and Glc-1-P
FT UTase activities."
FT /evidence="ECO:0000269|PubMed:27864169"
FT MUTAGEN 97
FT /note="Y->H,L,M,N,Q,S: Increases GlcNAc-1-P UTase and Glc-
FT 1-P UTase activities."
FT /evidence="ECO:0000269|PubMed:27864169"
FT MUTAGEN 97
FT /note="Y->V: Loss of GlcNAc-1-P UTase activity; when
FT associated with N-80."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 146
FT /note="E->A,C,F,G,I,K,L,M,P,Q,R,V,W,Y: Loss of both GlcNAc-
FT 1-P UTase and Glc-1-P UTase activities."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 146
FT /note="E->D,N: Decrease in GlcNAc-1-P UTase and Glc-1-P
FT UTase activities."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 146
FT /note="E->H,S,T: Decrease in GlcNAc-1-P UTase activity and
FT loss of Glc-1-P UTase activity."
FT /evidence="ECO:0000269|PubMed:30291121"
FT MUTAGEN 308
FT /note="H->A: Strong decrease in GalN-1-P AcTase activity
FT and almost loss of GlcN-1-P AcTase activity."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 311
FT /note="Y->A: Strong decrease in GalN-1-P AcTase activity
FT and increase in GlcN-1-P AcTase activity."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 331
FT /note="N->A: Strong decrease in GalN-1-P AcTase activity
FT and decrease in GlcN-1-P AcTase activity."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 337
FT /note="K->A: Slight decrease in GalN-1-P AcTase activity
FT and increase in GlcN-1-P AcTase activity."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 340
FT /note="K->A: Decrease in GalN-1-P AcTase activity and
FT increase in GlcN-1-P AcTase activity."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 391..401
FT /note="Missing: No change in GlcNAc-1-P UTase activity.
FT Shows 38% less GalN-1-P AcTase activity than the wild-type,
FT but increases GlcN-1-P AcTase activity 16.8 times.
FT Significantly affects the thermostability of the entire
FT protein."
FT /evidence="ECO:0000269|PubMed:25567746"
FT MUTAGEN 397..401
FT /note="Missing: No change in GlcNAc-1-P UTase activity.
FT Shows 20% less GalN-1-P AcTase activity than the wild-type,
FT but increases GlcN-1-P AcTase activity 4.8 times. Does not
FT affect thermostability."
FT /evidence="ECO:0000269|PubMed:25567746"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5Z09"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2GGO"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2GGO"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:2GGO"
SQ SEQUENCE 401 AA; 44516 MW; 5EF240CCDFFBF976 CRC64;
MKAFILAAGS GERLEPITHT RPKAFVPILS KPLIEYQIEY LRKCGIRDIT VIVSSKNKEY
FEKKLKEISI VTQKDDIKGT GAAILSAKFN DEALIIYGDL FFSNEKEICN IITLKENAII
GVKVSNPKDY GVLVLDNQNN LSKIIEKPEI PPSNLINAGI YKLNSDIFTY LDKISISERG
ELELTDAINL MAKDHRVKVI EYEGYWMDIG KPWNIIDVNK WALDNLVFSQ NLGNVEDNVK
IKGKVIIEED AEIKSGTYIE GPVYIGKGSE IGPNSYLRPY TILVEKNKIG ASVEVKESVI
MEGSKIPHLS YVGDSVIAED VNFGAGTLIA NLRFDEKEVK VNVKGKRISS GRRKLGAFIG
GHVRTGINVT ILPGVKIGAY ARIYPGAVVN RDVGYGEFFK V
