ID L8M2K1_9CYAN Unreviewed; 387 AA.
AC L8M2K1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_02085};
DE EC=2.7.7.9 {ECO:0000256|HAMAP-Rule:MF_02085};
DE AltName: Full=Cyanobacterial UDP-glucose pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_02085};
DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_02085};
DE Short=UDP-Glc PPase {ECO:0000256|HAMAP-Rule:MF_02085};
GN Name=cugP {ECO:0000256|HAMAP-Rule:MF_02085};
GN ORFNames=Xen7305DRAFT_00023010 {ECO:0000313|EMBL:ELS02586.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS02586.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS02586.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS02586.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: Catalyzes the formation of UDP-glucose, from UTP and glucose
CC 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_02085}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02085};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02085};
CC -!- SIMILARITY: Belongs to the CugP-type UDP-glucose pyrophosphorylase
CC family. {ECO:0000256|HAMAP-Rule:MF_02085}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS02586.1}.
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DR EMBL; ALVZ01000190; ELS02586.1; -; Genomic_DNA.
DR RefSeq; WP_006510305.1; NZ_ALVZ01000190.1.
DR AlphaFoldDB; L8M2K1; -.
DR STRING; 102125.Xen7305DRAFT_00023010; -.
DR PATRIC; fig|102125.3.peg.3131; -.
DR eggNOG; COG1208; Bacteria.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
DR GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:UniProt.
DR GO; GO:0002134; F:UTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04181; NTP_transferase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR HAMAP; MF_02085; CugP_cyano; 1.
DR InterPro; IPR037538; CugP_cyano.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR22572; SUGAR-1-PHOSPHATE GUANYL TRANSFERASE; 1.
DR PANTHER; PTHR22572:SF137; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02085};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02085};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02085};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02085}.
FT DOMAIN 2..246
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02085"
SQ SEQUENCE 387 AA; 42838 MW; DB78BE8C6C3897BF CRC64;
MKAMILAAGK GTRVRPITYT IPKPLIPILQ KPVMEFLLEL LRQHGFDQVM VNVSHLAHEI
EGYFRDGQRF GVNIGYSFEG RIVDGELVGE ALGSAGGLKK IQEFKTFFDD TFIVLCGDAL
IDLDLSEAIQ WHKDKGAIAT IVTKSVPKED VSSYGVVVTD EDGRIQSFQE KPTVQEALST
NINTGIYIFE PEIFDYIPPN QEYDIGGELF PQLVAKQAPF YAVAMDFQWV DIGKVPDYWR
AIRGVLQGEI KNVRIPGIEV KPGIYTGLNV SVNWDKVNIQ GPVYIGGMTK IEDGATIIGP
SMIGPNCWIC RDATVDNSVI FEYSRLGEGI RLVDKLVFGR YCVDKTGAAI DVRAAALDWL
ITDSRHAPPE AKAEHETAIR NLLNSDG
//
