ID K0G420_ACTSU Unreviewed; 295 AA.
AC K0G420;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=ASU2_03800 {ECO:0000313|EMBL:AFU18898.1};
OS Actinobacillus suis H91-0380.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=696748 {ECO:0000313|EMBL:AFU18898.1, ECO:0000313|Proteomes:UP000006303};
RN [1] {ECO:0000313|EMBL:AFU18898.1, ECO:0000313|Proteomes:UP000006303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H91-0380 {ECO:0000313|EMBL:AFU18898.1,
RC ECO:0000313|Proteomes:UP000006303};
RX PubMed=23144422; DOI=10.1128/JB.01633-12;
RA Macinnes J.I., Mackinnon J., Bujold A.R., Ziebell K., Kropinski A.M.,
RA Nash J.H.;
RT "Complete Genome Sequence of Actinobacillus suis H91-0380, a Virulent
RT Serotype O2 Strain.";
RL J. Bacteriol. 194:6686-6687(2012).
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; CP003875; AFU18898.1; -; Genomic_DNA.
DR RefSeq; WP_014991495.1; NC_018690.1.
DR AlphaFoldDB; K0G420; -.
DR GeneID; 34290780; -.
DR KEGG; asi:ASU2_03800; -.
DR PATRIC; fig|696748.4.peg.768; -.
DR eggNOG; COG1210; Bacteria.
DR HOGENOM; CLU_029499_1_1_6; -.
DR OrthoDB; 9803306at2; -.
DR Proteomes; UP000006303; 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:AFU18898.1};
KW Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AFU18898.1}.
FT DOMAIN 3..272
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 295 AA; 32558 MW; BB90B4C8C9EB7B27 CRC64;
MKVIIPVAGL GTRMLPATKA IPKEMLTIAD KPLIQYIVNE CVAAGIKEIV LVTHSSKNAI
ENHFDTSFEL ETMLEKRVKR QLLDEVRSIV PKDVTLMHVR QGQAKGLGHA VLCGRAVVGN
EPFAVVLPDV ILADFTANQK TENLAAMIKR FNETKHSQIM VAPVPKEDVS SYGVADCAGV
EIPAGETAKI VKMVEKPSVE EAPSNLAVVG RYVFSENIWD LLEKTPVGVG DEIQLTDAID
MLIEQETVEA FHMTGRTFDC GDKLGYMQAF TEYSLRHDKF GDDFKDFIKK LAKTL
//
