ID F6AD55_PSEF1 Unreviewed; 278 AA.
AC F6AD55;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Psefu_2399 {ECO:0000313|EMBL:AEF22365.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22365.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF22365.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002727; AEF22365.1; -; Genomic_DNA.
DR RefSeq; WP_013791493.1; NC_015556.1.
DR AlphaFoldDB; F6AD55; -.
DR STRING; 743720.Psefu_2399; -.
DR KEGG; pfv:Psefu_2399; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_2_6; -.
DR OrthoDB; 9803306at2; -.
DR Proteomes; UP000000686; Chromosome.
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:AEF22365.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AEF22365.1}.
FT DOMAIN 9..266
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 278 AA; 31008 MW; 17E72863E367E651 CRC64;
MIKKCLFPAA GYGTRFLPAT KAMPKEMLPV VNTPLIQYGV EEALDAGLNE IAMVTGRGKR
SLEDHFDISY ELEHQIRNTD KEKYLVGIRR LIDNCTFSYT RQVEMKGLGH AILSGRPLIG
DEPFAVVLAD DLCLNVGGDG VLTQMVKLYN QFRCSIVAVQ EVPMDEIHKY GVIAGETIRD
DIFRVSHMVE KPKAEEAPSN LAIIGRYILT PDIFDLIKNT EPGKGGEIQI TDALMQQAQE
GCVLAYKFKG RRFDCGGAEG YIEATNYCFE NLYREGRG
//
