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Database: UniProt
Entry: A0A0C1NDZ4_9CYAN
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Original site: A0A0C1NDZ4_9CYAN 
ID   A0A0C1NDZ4_9CYAN        Unreviewed;       390 AA.
AC   A0A0C1NDZ4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=DA73_0221335 {ECO:0000313|EMBL:KIE10976.1}, DA73_0400017160
GN   {ECO:0000313|EMBL:KAF3887020.1};
OS   Tolypothrix bouteillei VB521301.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10976.1};
RN   [1] {ECO:0000313|EMBL:KIE10976.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KIE10976.1};
RX   PubMed=25700407;
RA   Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA   Adhikary S.P., Tripathy S.;
RT   "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL   Genome Announc. 3:e00001-15(2015).
RN   [2] {ECO:0000313|EMBL:KAF3887020.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VB521301 {ECO:0000313|EMBL:KAF3887020.1};
RA   Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA   Tripathy S.;
RT   "Improved Assembly of Tolypothrix boutellei genome.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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:KIE10976.1}.
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DR   EMBL; JHEG04000001; KAF3887020.1; -; Genomic_DNA.
DR   EMBL; JHEG02000048; KIE10976.1; -; Genomic_DNA.
DR   RefSeq; WP_038083836.1; NZ_JHEG04000001.1.
DR   AlphaFoldDB; A0A0C1NDZ4; -.
DR   STRING; 1479485.DA73_0221335; -.
DR   OrthoDB; 9803871at2; -.
DR   Proteomes; UP000029738; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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   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.
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:UP000029738};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02085, ECO:0000313|EMBL:KIE10976.1}.
FT   DOMAIN          2..245
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   390 AA;  42922 MW;  01B2CAC739937570 CRC64;
     MKAMILAAGK GTRVRPITYT IPKPMIPILQ KPVMEFLLEL LRQHGFDQIM VNVSHLADEI
     ESYFRDGQRF GVQIAYSFEG RIVDGTLVGE AVGSAGGMRK IQDFYPFFDD TFVVLCGDAL
     IDLDLTAAVK WHREKGSIAT IIMKSVPQEE VSSYGVVVTD EEGRVKAFQE KPKVEEALST
     NINTGIYIFE PEIFNYIPSG VEYDIGSQLF PKLVEVGAPF YAIPMNFEWV DIGKVPDYWR
     AVRGVLSGEI KNVQIPGHQV APGIYTGMNV AVNWDKVDIT GPVYIGGMTR IEDGAKIVGP
     TMIGPNCWVC SGATVENSVI FDWSRLGPGV RLVDKLVYGR YCVDKTGATI DVQAAALDWL
     ITDARQEPPS HTPAERQAIA ELLGTNAPVT
//
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