ID I3UH89_ADVKW Unreviewed; 278 AA.
AC I3UH89;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=TKWG_24000 {ECO:0000313|EMBL:AFK64377.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK64377.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK64377.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
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; CP003555; AFK64377.1; -; Genomic_DNA.
DR RefSeq; WP_014752468.1; NC_017964.1.
DR AlphaFoldDB; I3UH89; -.
DR STRING; 1036672.TKWG_24000; -.
DR KEGG; aka:TKWG_24000; -.
DR HOGENOM; CLU_029499_1_2_4; -.
DR OrthoDB; 9803306at2; -.
DR Proteomes; UP000005267; 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:AFK64377.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361259}.
FT DOMAIN 11..269
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 278 AA; 30093 MW; 1587ADE6ABCEC611 CRC64;
MNPIRKAVFP VAGLGTRFLP ATKAMPKEML PVVDKPLIQY AVEEAVKAGI TDLIFITGRH
KRAIEDHFDS MPELESELEE KGKQEMLEQV RQVIPSNVNC IYIRQPAPLG LGHAVLCAEP
VVGNEPFAVL LADDLIDSNV PVTQQLIQAA HANNGSVLGI QTIAREDSNK YGIIAGKSVS
SNTIQVNQIV EKPAPADAPS DKAVVGRYIL EPEIFEYLRH IGKGAGGEIQ LTDGIAALLK
SRNVFGFAYE GTRYDCGSKA GFFAATVALG QKYHGFKL
//
