ID Q84BL0_AERHY Unreviewed; 297 AA.
AC Q84BL0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 Name=galU {ECO:0000313|EMBL:AAN10297.1};
OS Aeromonas hydrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644 {ECO:0000313|EMBL:AAN10297.1};
RN [1] {ECO:0000313|EMBL:AAN10297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PPD11/90 {ECO:0000313|EMBL:AAN10297.1};
RA Zhang Y., Lau Y.L., Leung K.Y.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAN10297.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PPD11/90 {ECO:0000313|EMBL:AAN10297.1};
RX PubMed=12686647; DOI=10.1099/mic.0.26144-0;
RA Zhang Y.L., Lau Y.L., Arakawa E., Leung K.Y.;
RT "Detection and genetic analysis of group II capsules in Aeromonas
RT hydrophila.";
RL Microbiology 149:1051-1060(2003).
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}.
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DR EMBL; AY144595; AAN10297.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84BL0; -.
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:AAN10297.1};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AAN10297.1}.
FT DOMAIN 7..276
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 297 AA; 32843 MW; D56D1C3AA95466B0 CRC64;
MIRDKMKAVI PVAGLGTRML PATKAIPKEM LPIVDKPLIQ YVVNECIAAG LKEIILVTHS
SKNAIENHFD KSFELEATLE SRVKRQLLEE IQSICPKDVT IMHVRQGEAK GLGHAVLSAY
PLVGNNPFVV VLPDVIIDDA ASDLKKDNLA KMVRNYKESG HSQIMVEPVA IQDVSKYGIV
DCHSVDISAG ESATIFNVVE KPEKDEAPSN LAIVGRYVLT PEIWPYLRTT KPGAGDEIQL
TDAISELLKD GQVDAFCMQG KSHDCGDKLG YMKAFVEYGL RHKDHQHNFR NFIVSLV
//
