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Database: UniProt
Entry: B8DN77_DESVM
LinkDB: B8DN77_DESVM
Original site: B8DN77_DESVM 
ID   B8DN77_DESVM            Unreviewed;       291 AA.
AC   B8DN77;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   OrderedLocusNames=DvMF_0060 {ECO:0000313|EMBL:ACL07021.1};
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=883 {ECO:0000313|EMBL:ACL07021.1};
RN   [1] {ECO:0000313|EMBL:ACL07021.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL07021.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) 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; CP001197; ACL07021.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8DN77; -.
DR   STRING; 883.DvMF_0060; -.
DR   KEGG; dvm:DvMF_0060; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_7; -.
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:ACL07021.1};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:ACL07021.1}.
FT   DOMAIN          6..264
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   291 AA;  32535 MW;  634D5D6F23535F27 CRC64;
     MNIRKVVIPV AGWGTRSLPA TKNIPKEMLP VYNKPVVQYV VEEAMRSGIG DVVFVTNRDK
     KIIEDHFDYN LQLEGVLERA GKTEMLRQVR EVAEMVNIIS IRQKQQLGLG HAVLCARDVV
     RDESFAVMVG DDLMFGMTPG IKQLIDVAAS ERLPVIGVME VPADKVNRYG IISGEEFAPG
     IFKVNKLVEK PKLGEAPSRL AIVGRYVLTP DIFRCLEQMK PGHGGEIQLT DALQMLADDR
     GLLAVKIRGM RFDAGDWAEY LTANIYFALQ DEELRDELVR QLKPLLPYSG T
//
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