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Database: UniProt
Entry: A0A2S4YDL9_9ACTN
LinkDB: A0A2S4YDL9_9ACTN
Original site: A0A2S4YDL9_9ACTN 
ID   A0A2S4YDL9_9ACTN        Unreviewed;       300 AA.
AC   A0A2S4YDL9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   Name=galU {ECO:0000313|EMBL:POX47027.1};
GN   ORFNames=C3488_24735 {ECO:0000313|EMBL:POX47027.1};
OS   Streptomyces sp. Ru72.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX47027.1, ECO:0000313|Proteomes:UP000237426};
RN   [1] {ECO:0000313|EMBL:POX47027.1, ECO:0000313|Proteomes:UP000237426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru72 {ECO:0000313|EMBL:POX47027.1,
RC   ECO:0000313|Proteomes:UP000237426};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POX47027.1}.
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DR   EMBL; PQSR01000059; POX47027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4YDL9; -.
DR   OrthoDB; 9803306at2; -.
DR   Proteomes; UP000237426; Unassembled WGS sequence.
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:POX47027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237426};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:POX47027.1}.
FT   DOMAIN          10..274
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   300 AA;  32939 MW;  F3194C1E1A2E95CE CRC64;
     MTQSHARITK AVIPAAGLGT RFLPATKATP KEMLPVVDKP AIQYVVEEAV SAGLDDVLMV
     TGRNKRPLED HFDRNYELES ALEKKGDAER LAKVQESSDL ATMHYVRQGD PKGLGHAVLC
     AAPHVGREPF AVLLGDDLID PRDPLLKRMI EVQEQHGGSV VALMEVAPEQ IHLYGCAAVE
     ATEDGDVVQV TGLIEKPDPA DAPSNYAVIG RYVLDPRIFD ILRKTEPGRS NEIQLTDALQ
     QLAEDEKAGG PVHGVVFKGR RYDTGDRGDY LRAIVRLACE REDLGPGFRT WLRSFVAEEM
//
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