CUGP_SYNY3
ID CUGP_SYNY3 Reviewed; 388 AA.
AC P74285;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000305|PubMed:24727225};
DE EC=2.7.7.9 {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000269|PubMed:24727225};
DE AltName: Full=Cyanobacterial UDP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000303|PubMed:24727225};
DE AltName: Full=UDP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000303|PubMed:24727225};
DE Short=UDP-Glc PPase {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000303|PubMed:24727225};
GN Name=cugP {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000303|PubMed:24727225};
GN OrderedLocusNames=sll1558 {ECO:0000312|EMBL:BAA18379.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ALA-8.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=24727225; DOI=10.1128/jb.01591-14;
RA Maeda K., Narikawa R., Ikeuchi M.;
RT "CugP is a novel ubiquitous non-GalU-type bacterial UDP-glucose
RT pyrophosphorylase found in cyanobacteria.";
RL J. Bacteriol. 196:2348-2354(2014).
CC -!- FUNCTION: Catalyzes the formation of UDP-glucose, from UTP and glucose
CC 1-phosphate. Is highly specific since it cannot use other NTPs such as
CC dTTP, CTP, ATP, and GTP, and other sugar-1P such as GlcNAc-1P, Gal-1P,
CC and Man-1P, as substrates. Has probably a central and essential role as
CC the substrate supplier for galactolipid synthesis; galactolipids are
CC major constituents of the photosynthetic thylakoid membrane and
CC important for photosynthetic activity. {ECO:0000269|PubMed:24727225}.
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:0000255|HAMAP-
CC Rule:MF_02085, ECO:0000269|PubMed:24727225};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02085,
CC ECO:0000305|PubMed:24727225};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.18 mM for UTP (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24727225};
CC KM=0.085 mM for alpha-D-glucose 1-phosphate (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:24727225};
CC Vmax=0.63 umol/min/mg enzyme (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:24727225};
CC Note=kcat is 28 sec(-1) (at pH 7.5 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:24727225};
CC -!- DISRUPTION PHENOTYPE: Complete disruption of this gene could not be
CC achieved, suggesting that the CugP-type UDP-Glc PPase is essential for
CC growth and survival of Synechocystis. {ECO:0000269|PubMed:24727225}.
CC -!- MISCELLANEOUS: The CugP-type UDP-Glc PPase appears to be present in all
CC cyanobacteria, whereas the GalU-type UDP-Glc PPase is present in only
CC certain cyanobacterial species. Moreover, the GalU-type PPase is found
CC to be widely distributed throughout the bacterial kingdom, whereas the
CC CugP-type can be found in only very limited species other than
CC cyanobacteria. {ECO:0000305|PubMed:24727225}.
CC -!- SIMILARITY: Belongs to the CugP-type UDP-glucose pyrophosphorylase
CC family. {ECO:0000255|HAMAP-Rule:MF_02085, ECO:0000305|PubMed:24727225}.
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DR EMBL; BA000022; BAA18379.1; -; Genomic_DNA.
DR PIR; S75920; S75920.
DR AlphaFoldDB; P74285; -.
DR SMR; P74285; -.
DR IntAct; P74285; 2.
DR STRING; 1148.1653465; -.
DR PaxDb; P74285; -.
DR EnsemblBacteria; BAA18379; BAA18379; BAA18379.
DR KEGG; syn:sll1558; -.
DR eggNOG; COG1208; Bacteria.
DR InParanoid; P74285; -.
DR OMA; PFLTHQL; -.
DR PhylomeDB; P74285; -.
DR BRENDA; 2.7.7.9; 382.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0002134; F:UTP binding; IDA:UniProtKB.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..388
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000438891"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8Z5I4, ECO:0000255|HAMAP-
FT Rule:MF_02085"
FT MUTAGEN 8
FT /note="A->G: Two-fold decrease in affinity for UTP. No
FT effect on affinity for Glc-1P and on catalytic activity
FT rate."
FT /evidence="ECO:0000269|PubMed:24727225"
SQ SEQUENCE 388 AA; 42768 MW; 0CD3E7B6828E0402 CRC64;
MKAMILAAGK GTRVRPITHT IPKPMIPILQ KPVMEFLLEL LRQHGFDQIM VNVSHLAEEI
ESYFRDGQRF GVQIAYSFEG NIVDGDLVGK ALGSAGGLKK IQEFNPFFDD TFVVLCGDAL
IDLDLTTAVK LHREKGAIAT IITKTVPQEL VSSYGVVVTD DNGKILTFQE KPAVEEALST
EINTGIYIFE PEVIDYIPSG QEYDLGGDLF PKLVDSGLPF YAVNMDFEWV DIGKVPDYWQ
AIRGVLSREI KNVQIPGIEV RPGVYTGINV AANWDNIEIE GPVYIGGMTR IEDGVKIIGP
SMIGPSCLIC QGAVVDNSVI FEYSRLGPGA RLVDKLVFGR YCVDKTGAAI DVQAAALDWL
ITDARHAAVQ YRQEYPSQRE ISKLLQPE
