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Database: UniProt
Entry: S5UYY1_STRC3
LinkDB: S5UYY1_STRC3
Original site: S5UYY1_STRC3 
ID   S5UYY1_STRC3            Unreviewed;       322 AA.
AC   S5UYY1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00012415, ECO:0000256|RuleBase:RU361259};
DE            EC=2.7.7.9 {ECO:0000256|ARBA:ARBA00012415, ECO:0000256|RuleBase:RU361259};
DE   AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU361259};
GN   ORFNames=B446_06825 {ECO:0000313|EMBL:AGS68189.1};
OS   Streptomyces collinus (strain DSM 40733 / Tue 365).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS68189.1, ECO:0000313|Proteomes:UP000015423};
RN   [1] {ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA   Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA   Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT   "The complete genome sequence of Streptomyces collinus Tu 365.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGS68189.1, ECO:0000313|Proteomes:UP000015423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX   PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA   Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT   "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT   Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL   J. Biotechnol. 168:739-740(2013).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000872,
CC         ECO:0000256|RuleBase:RU361259};
CC   -!- SIMILARITY: Belongs to the UDPGP type 2 family.
CC       {ECO:0000256|ARBA:ARBA00006890, ECO:0000256|RuleBase:RU361259}.
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DR   EMBL; CP006259; AGS68189.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5UYY1; -.
DR   STRING; 1214242.B446_06825; -.
DR   KEGG; sci:B446_06825; -.
DR   PATRIC; fig|1214242.5.peg.1417; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_0_11; -.
DR   Proteomes; UP000015423; Chromosome.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
DR   CDD; cd02541; UGPase_prokaryotic; 1.
DR   InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR01099; galU; 1.
DR   PANTHER; PTHR43197; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR43197:SF1; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU361259,
KW   ECO:0000313|EMBL:AGS68189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AGS68189.1}.
FT   DOMAIN          3..263
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   REGION          291..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   322 AA;  34585 MW;  F92A9D1EA76C5BEA CRC64;
     MRKAVVPAAG LGTRFLPATK ATPKEMLPVV DKPAIQYVVE EAAAAGLVDI LMVTGRHKRA
     IEDHFDHAFE LEQALAAKGD TVRLDAVRDP ARLADIHHIR QGDPLGLGHA VLCARHHVGD
     QPFAVLLGDD LIDPRETLLS RMLDVRDRYA GSVVALMEVE PELIGLYGCA AVEPAEDGEE
     GVVRVTGLVE KPAPGQAPSR YAVIGRYVLD PAVFGVLERT APGRGGEIQL TDALQELAAA
     GTVHGVVFDG LRYDTGDKAD YLRTVVRLAC ARPDLGPAFA RWLRDFVADL DGESDGDRDG
     DRDGDRETAV EGITAREGRR AA
//
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