(data stored in ACNUC29543 zone)

SWISSPROT: A5GQH2_SYNR3

ID   A5GQH2_SYNR3            Unreviewed;       395 AA.
AC   A5GQH2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 55.
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   OrderedLocusNames=SynRCC307_0228 {ECO:0000313|EMBL:CAK27131.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27131.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of UDP-glucose, from UTP and
CC       glucose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_02085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate +
CC         UDP-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02085};
CC   -!- SIMILARITY: Belongs to the CugP-type UDP-glucose pyrophosphorylase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02085}.
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DR   EMBL; CT978603; CAK27131.1; -; Genomic_DNA.
DR   RefSeq; WP_011934646.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0228; -.
DR   EnsemblBacteria; CAK27131; CAK27131; SynRCC307_0228.
DR   KEGG; syr:SynRCC307_0228; -.
DR   eggNOG; ENOG4107S2F; Bacteria.
DR   eggNOG; COG1208; LUCA.
DR   HOGENOM; HOG000283479; -.
DR   KO; K00966; -.
DR   OMA; KVPDYWQ; -.
DR   OrthoDB; 1557977at2; -.
DR   BioCyc; SSP316278:G1GJL-224-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
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   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_02085; CugP_cyano; 1.
DR   InterPro; IPR037538; CugP_cyano.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQH2.
DR   SWISS-2DPAGE; A5GQH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
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:UP000001115};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02085,
KW   ECO:0000313|EMBL:CAK27131.1}.
FT   DOMAIN        2    246       NTP_transferase. {ECO:0000259|Pfam:
FT                                PF00483}.
FT   METAL       118    118       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_02085}.
SQ   SEQUENCE   395 AA;  43434 MW;  1D33164451748D22 CRC64;
     MKAMILAAGK GTRVQPITHT IPKPMIPILQ KPVMEFLLEL LRQHGFTEVM VNVSHLAEEI
     ENYFRDGQRF GVEIAYSFEG RIEDGELIGD ALGSAGGLKK IQNFQKFFDD TFVVLCGDAL
     IDLNLSEAVR KHRQSGALAT IITKRVPKEK VSSYGVVVTD DDGRVKAFQE KPGVEEALSD
     EINTGIYLFE PEIFEHIPDG VSYDIGSQLF PKLVEKGLPF YALPMDFEWV DIGKVPDYWH
     AIRSVLQGDI RQVSIPGKQV RPGIYTGLNV AANWDKIEVE GPVYVGGMTK IEDGARIIGP
     AMIGPSCHIC AGATIDNSII FDYSRIGAGV TLAEKLVFGR YCVDKTGDHL DVQEASLDWL
     ITDARRLDLV EPSPEQKALA ELLGSDLGNN LGEAS
//

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