ID A1AXE3_RUTMC Unreviewed; 276 AA.
AC A1AXE3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Rmag_0885 {ECO:0000313|EMBL:ABL02600.1};
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL02600.1, ECO:0000313|Proteomes:UP000002587};
RN [1] {ECO:0000313|EMBL:ABL02600.1, ECO:0000313|Proteomes:UP000002587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm {ECO:0000313|EMBL:ABL02600.1};
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
CC -!- FUNCTION: May play a role in stationary phase survival.
CC {ECO:0000256|ARBA:ARBA00037294}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000488; ABL02600.1; -; Genomic_DNA.
DR RefSeq; WP_011738225.1; NC_008610.1.
DR AlphaFoldDB; A1AXE3; -.
DR STRING; 413404.Rmag_0885; -.
DR KEGG; rma:Rmag_0885; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_2_6; -.
DR OrthoDB; 9803306at2; -.
DR Proteomes; UP000002587; 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:ABL02600.1};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:ABL02600.1}.
FT DOMAIN 9..270
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 276 AA; 30711 MW; C2ADCD7F62EBB43B CRC64;
MIKKCLFPAA GFGTRFLPAT KAVPKEMLPI LTKPLLQYAV KEALDAGMSN MAIVTGKGKR
AIEDHFDRSL ELEMQIQGTQ KEVLLKEINA VCNNSTFTYV RQKQMLGLGH AILTGEPLIG
NEPFAVHLAD DLCTSENDNV LTQMIQMYNK YQCSIVAIEQ VPMDQTHKYG VITGDLVNNT
NDTYRVTSMI EKPNPKDAPT NMAIIGRYIL TPDIFNILKQ NKPGKDGEIQ ITDALLTQAK
QGRVIAYKFK GKRFDCGSIQ GYVEATNYFA KQQGII
//
