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Database: UniProt
Entry: Q11EQ9_CHESB
LinkDB: Q11EQ9_CHESB
Original site: Q11EQ9_CHESB 
ID   Q11EQ9_CHESB            Unreviewed;       294 AA.
AC   Q11EQ9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=Meso_2739 {ECO:0000313|EMBL:ABG64116.1};
OS   Chelativorans sp. (strain BNC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Chelativorans.
OX   NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG64116.1};
RN   [1] {ECO:0000313|EMBL:ABG64116.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BNC1 {ECO:0000313|EMBL:ABG64116.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL   Submitted (JUN-2006) 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; CP000390; ABG64116.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q11EQ9; -.
DR   STRING; 266779.Meso_2739; -.
DR   KEGG; mes:Meso_2739; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_5; -.
DR   OrthoDB; 9803306at2; -.
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:ABG64116.1};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:ABG64116.1}.
FT   DOMAIN          11..268
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   294 AA;  32788 MW;  B163F3804CA6E2C5 CRC64;
     MKKIRKAVFP VAGLGTRFLP ATKALPKEML TVVDKPVIQY VVDEAREAGI EHFIFVTGRN
     KTAIEDHFDV AVELYETLSR RGKTEILERL KAMQPEPGQT GYTRQQVPLG LGHAVWCARE
     LVGNEPFALL LPDMIMQSEP GCMKQMVELY METGGNILAV EECDPAETQK YGIVGRGKET
     HGGFEITSMV EKPKPKDAPS NFYINGRYIL QPEIFSLLED QETGAGGEIQ ITDAMLRLHA
     KEPFYAHIFR GRTFDCGSPE GFIKANIALA LQQETLKPQV LGFLKDFLEE EGLA
//
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