ID Q9X364_BACAN Unreviewed; 295 AA.
AC Q9X364;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase {ECO:0000256|ARBA:ARBA00012415, 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=GBAA_pXO1_0129 {ECO:0000313|EMBL:AAT28870.2};
OS Bacillus anthracis.
OG Plasmid pX01 {ECO:0000313|EMBL:AAD32398.1}, and
OG Plasmid pXO1 {ECO:0000313|EMBL:AAT28870.2,
OG ECO:0000313|Proteomes:UP000000594}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392 {ECO:0000313|EMBL:AAD32398.1};
RN [1] {ECO:0000313|EMBL:AAD32398.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sterne {ECO:0000313|EMBL:AAD32398.1};
RC PLASMID=pX01 {ECO:0000313|EMBL:AAD32398.1};
RX PubMed=10515943;
RA Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P.,
RA Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y.,
RA Ricke D., Svensson R., Jackson P.J.;
RT "Sequence and organization of pXO1, the large Bacillus anthracis plasmid
RT harboring the anthrax toxin genes.";
RL J. Bacteriol. 181:6509-6515(1999).
RN [2] {ECO:0000313|EMBL:AAT28870.2, ECO:0000313|Proteomes:UP000000594}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames Ancestor {ECO:0000313|EMBL:AAT28870.2}, and Ames ancestor
RC {ECO:0000313|Proteomes:UP000000594};
RC PLASMID=pXO1 {ECO:0000313|Proteomes:UP000000594};
RX PubMed=18952800; DOI=10.1128/JB.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
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}.
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DR EMBL; AF065404; AAD32398.1; -; Genomic_DNA.
DR EMBL; AE017336; AAT28870.2; -; Genomic_DNA.
DR PIR; F59102; F59102.
DR RefSeq; NP_052790.1; NC_001496.1.
DR RefSeq; WP_000702222.1; NZ_VLYO01000010.1.
DR AlphaFoldDB; Q9X364; -.
DR GeneID; 45025493; -.
DR KEGG; bar:GBAA_pXO1_0129; -.
DR PATRIC; fig|1392.233.peg.5847; -.
DR HOGENOM; CLU_029499_1_2_9; -.
DR OMA; YGHAVFC; -.
DR Proteomes; UP000000594; Plasmid pXO1.
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:AAT28870.2}; Plasmid {ECO:0000313|EMBL:AAD32398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000594};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AAT28870.2}.
FT DOMAIN 5..266
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 295 AA; 33153 MW; 097ECF36D0DEE1DA CRC64;
MKIRKAIIPA AGLGTRFLPA TKAQPKEMLP IVDKPTIQYI VEEAVSSGIE DIIIVSGRGK
HVIEDHFDKS YELEQTLFKK NKIKTLEDIE CISNLANIHY IRQKEPKGLG HAIYCARRFI
GEEPFAVLLG DDIVSSTYPC LKQLIDVYEE HHCSVVGVQR VLETEVSKYG IVKSANQNVN
QSIIPISMLV EKPPLETAPS NLAIMGRYIL KPDIFEVLKN LPVGSGGEIQ LTDAINVLNK
QQKVLAFEFD GKRYDVGDKF GFIKATIDFA LQRESLKEDV LSYLRNITRD KLINK
//
