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Database: UniProt
Entry: Q6LNV6_PHOPR
LinkDB: Q6LNV6_PHOPR
Original site: Q6LNV6_PHOPR 
ID   Q6LNV6_PHOPR            Unreviewed;       306 AA.
AC   Q6LNV6;
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=Y2631 {ECO:0000313|EMBL:CAG21020.1};
GN   OrderedLocusNames=PBPRA2642 {ECO:0000313|EMBL:CAG21020.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG21020.1, 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; CAG21020.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LNV6; -.
DR   STRING; 298386.PBPRA2642; -.
DR   KEGG; ppr:PBPRA2642; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_1_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   ECO:0000313|EMBL:CAG21020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   Transferase {ECO:0000256|RuleBase:RU361259}.
FT   DOMAIN          13..283
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   306 AA;  33323 MW;  64CCB39C16BA033E CRC64;
     MEFIMTKTSL VRKAVIPVAG LGTRMLPATK AIPKEMLPIV DRPLIQYVVN ECVAAGIKEI
     ILVTHSSKNS IENHFDTSFE LEATLEKRVK RQLLEEVQSI CPKDVTIMHV RQGQAKGLGH
     AVLSARPLVG DEPFAVVLPD VVLDDAASDL RTENMAAMIA AFNETKISQV MVEPVPMADV
     SSYGVADVNG VGLKPGETAA MTKVVEKPAL EDAPSNLAIV GRYVLPAEIW GMLERTPVGA
     GDEIQLTDAI DMLMESQQVN AFHMSGKSHD CGTKLGYMQA FVEYGMRHNS LGDDFKAYLK
     DMVKTL
//
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