ID K0I2Y0_9BURK Unreviewed; 295 AA.
AC K0I2Y0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-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 ORFNames=C380_18390 {ECO:0000313|EMBL:AFU47372.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU47372.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU47372.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU47372.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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; CP003872; AFU47372.1; -; Genomic_DNA.
DR RefSeq; WP_015015338.1; NC_018708.1.
DR AlphaFoldDB; K0I2Y0; -.
DR STRING; 358220.C380_18390; -.
DR KEGG; ack:C380_18390; -.
DR PATRIC; fig|358220.3.peg.3745; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_2_4; -.
DR OrthoDB; 9803306at2; -.
DR Proteomes; UP000006306; 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:AFU47372.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361259}.
FT DOMAIN 14..275
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 295 AA; 32052 MW; DF408CBA410715A6 CRC64;
MTVATTVRKA VFPVAGLGTR FLPATKASPK EMLPVVDKPL IQYAVEEAYA AGIRHMIFVT
GRSKRAIEDH FDTAYELEAE LEAAGKKELL ELVRSIQPSD MDCAFVRQPR SLGLGHAVLC
AEPLVGKEPF AVLLADDLMV GPQGGQPVLA QMATAFRQQG RSVIAVQEVP EDHVHKYGIV
AGEPAGGPLI RIQRIVEKPK AAEAPSRMGV AGRYILTPGV FDEIRNQPRG VGGEIQLTDG
IARLMHSEAV YAFQYEGKRY DCGSKEGFLE ATVELALQHP QVGAHFRGYL KNLAL
//
