ID A0A372LDZ5_9BACI Unreviewed; 301 AA.
AC A0A372LDZ5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 Name=galU {ECO:0000313|EMBL:RFU64427.1};
GN ORFNames=D0469_18840 {ECO:0000313|EMBL:RFU64427.1};
OS Peribacillus saganii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=2303992 {ECO:0000313|EMBL:RFU64427.1, ECO:0000313|Proteomes:UP000264541};
RN [1] {ECO:0000313|EMBL:RFU64427.1, ECO:0000313|Proteomes:UP000264541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V47-23a {ECO:0000313|EMBL:RFU64427.1,
RC ECO:0000313|Proteomes:UP000264541};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RFU64427.1}.
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DR EMBL; QVTE01000056; RFU64427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372LDZ5; -.
DR OrthoDB; 9803871at2; -.
DR Proteomes; UP000264541; Unassembled WGS sequence.
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:RFU64427.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000264541};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:RFU64427.1}.
FT DOMAIN 5..266
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 301 AA; 33908 MW; 92D874ED3F3572A1 CRC64;
MKIRKAIIPA AGLGTRFLPA TKAQPKEMLP IVDKPTIQYI VEEAVASGIE EIIIIIGRGK
RSIEDHFDKS YELEDTLMKK NKLEILKDVQ KISNLVNIVY VRQKEPKGLG NAILCAKSVI
GDEPFAVLLG DDIVMSETPC LKQMIRLFEN HNSPVVAVQP VPYNDVSKYG IIKPKEPVNE
VNFFHIESLV EKPSIEEAPS RYAIMGRYVL TPEIFDILEK IPVGQGDELQ LTDAINTLNK
QQAVLASKFE GRRYDIGDNI GFIKATIDFA LERDDTKQEV LAYLQDVIKK YKSHNSKRVM
D
//
