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Database: UniProt
Entry: D5X226_THIK1
LinkDB: D5X226_THIK1
Original site: D5X226_THIK1 
ID   D5X226_THIK1            Unreviewed;       295 AA.
AC   D5X226;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00019048, 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   OrderedLocusNames=Tint_1803 {ECO:0000313|EMBL:ADG31172.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31172.1};
RN   [1] {ECO:0000313|EMBL:ADG31172.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG31172.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) 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}.
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DR   EMBL; CP002021; ADG31172.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5X226; -.
DR   STRING; 75379.Tint_1803; -.
DR   KEGG; tin:Tint_1803; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_4; -.
DR   BioCyc; TINT75379:TINT_RS09050-MONOMER; -.
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:ADG31172.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361259}.
FT   DOMAIN          12..269
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   295 AA;  31896 MW;  9B57BC360254B3F4 CRC64;
     MPPTITKAVF PVAGLGTRFL PATKATPKEM MPVVDKPLIQ YAVEEAYAAG ITEMIFVTGR
     HKRAIEDHFD TAYELEHQLE EAGKQAMLDV VRSVKPDNVQ CVFVRQPVAN GLGAAVLCAE
     RLVGDEPFAV ILADDLLVGE PPVMAQMVDI HSRHGRSVLA TEEVPREHTK RYGIVSGQEI
     TPGLTSLSGI VEKPAPDVAP STQAVVGRYI LSPRVFHHLR NGKPGAGGEI QLTDGISALL
     HEEAVYAYRY SGRRFDCGSK LGYLEATVQL GMSHPETGPE FSAYINNLCT GHAAS
//
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