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Database: UniProt
Entry: Q6LNS4_PHOPR
LinkDB: Q6LNS4_PHOPR
Original site: Q6LNS4_PHOPR 
ID   Q6LNS4_PHOPR            Unreviewed;       316 AA.
AC   Q6LNS4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
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   Name=SO1665 {ECO:0000313|EMBL:CAG21052.1};
GN   OrderedLocusNames=PBPRA2674 {ECO:0000313|EMBL:CAG21052.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21052.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
CC   -!- FUNCTION: May play a role in stationary phase survival.
CC       {ECO:0000256|ARBA:ARBA00037294}.
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; CR378671; CAG21052.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LNS4; -.
DR   STRING; 298386.PBPRA2674; -.
DR   KEGG; ppr:PBPRA2674; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_2_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   Transferase {ECO:0000256|RuleBase:RU361259}.
FT   DOMAIN          10..279
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   316 AA;  34284 MW;  D2B73DAB8EAFF3E3 CRC64;
     MDNKMNKITK AVIPVAGLGT RMLPATKAIP KEMLPIVDKP LIQYIVNECV AAGIKEIVLV
     THSSKNAIEN HFDTSYELEA TLEKRVKRQL LDAVQSICPK DVTIMHVRQG HAKGLGHAVL
     CAKPLIGDAP FVVVLPDVIL DEYTADQSRE NLAAMLARYE STQASQIMVE PVPMHDVSKY
     GVVDCNGAAL KGGESHPMTA MVEKPAMEEA PSNLAVVGRY VLSAKIWEKL AKTPPGAGDE
     IQLTDAIDML MADETVEAFH MTGKSHDCGD KLGYLKAFVE YGIRHESLGD DFKDYLVSSL
     LVSSAEVASI EVASVE
//
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