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Database: UniProt
Entry: A0A097QZ66_HAFAL
LinkDB: A0A097QZ66_HAFAL
Original site: A0A097QZ66_HAFAL 
ID   A0A097QZ66_HAFAL        Unreviewed;       302 AA.
AC   A0A097QZ66;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AT03_04545 {ECO:0000313|EMBL:AIU71740.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU71740.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU71740.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU71740.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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; CP009706; AIU71740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097QZ66; -.
DR   KEGG; hav:AT03_04545; -.
DR   PATRIC; fig|1453496.5.peg.906; -.
DR   eggNOG; COG1210; Bacteria.
DR   HOGENOM; CLU_029499_1_1_6; -.
DR   Proteomes; UP000029986; 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:AIU71740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986};
KW   Transferase {ECO:0000256|RuleBase:RU361259, ECO:0000313|EMBL:AIU71740.1}.
FT   DOMAIN          11..275
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   302 AA;  32556 MW;  9BC699E00A4B71F1 CRC64;
     MRYTVSVIKK VIIPVAGLGT RMLPATKAIP KEMLPLVDRP LIQLIVDECV AAGIKEIILV
     THSSKNAIEN HFDKNFELES TLDSKNKHQL LDEVRAICPA DVSIVSVRQG AAQGLGHAVL
     CAQSLVGEQP FAVLLPDVIM DNLHGVENKS NNLASMIQHY ESTSISQVMV SPVPEEDVSN
     YGIVDCQGVE ANPGESVLIK RVIEKPARDS APSNLSIVGR YILPPEIWPI LASTPCGAGG
     EIQLTDAIST LMESQPVAAY AMVGSYYDCG NKLGYAQTFV ESAMAHPDIG PLFHAWLTSK
     FA
//
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