ID A0A149VZF7_9PROT Unreviewed; 289 AA.
AC A0A149VZF7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=gtaB {ECO:0000313|EMBL:KXW58586.1};
GN ORFNames=FEMY_09850 {ECO:0000313|EMBL:KXW58586.1};
OS Ferrovum myxofaciens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Ferrovales; Ferrovaceae;
OC Ferrovum.
OX NCBI_TaxID=416213 {ECO:0000313|EMBL:KXW58586.1, ECO:0000313|Proteomes:UP000075653};
RN [1] {ECO:0000313|EMBL:KXW58586.1, ECO:0000313|Proteomes:UP000075653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-31 {ECO:0000313|EMBL:KXW58586.1,
RC ECO:0000313|Proteomes:UP000075653};
RA Poehlein A., Ullrich S.R., Schloemann M., Muehling M., Daniel R.;
RT "Genome sequence of the acidophilic iron oxidising Ferrovum strain Z-31.";
RL Submitted (JAN-2016) 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:KXW58586.1}.
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DR EMBL; LRRD01000013; KXW58586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A149VZF7; -.
DR STRING; 1789004.FEMY_09850; -.
DR PATRIC; fig|1789004.3.peg.1000; -.
DR Proteomes; UP000075653; 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:KXW58586.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361259}.
FT DOMAIN 12..268
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 289 AA; 31497 MW; A8CC99E7D75DF0E2 CRC64;
MIKKIRKAVF PVAGMGSRFL PATKASPKEM LPVVDKPLIQ YAVEEAVAAG ITEMIFVTGR
GKRAIEDHFD KAYELEAELA QRGKDRMLEI VRNLPPSGVS CAYVRQPEAL GLGHAILCAA
PLVGDEPFAV VLADDLIDSK VPVLRQMMEW YEKSGSSVLG VQQVPRAQTG QYGIVQTEHG
MGEYLRVTGI VEKPAPDRAP STLAVVGRYI LTPSVFDTLR EVAPGAGGEI QLTDGIARLL
EREMVLACPF EGVRYDCGSK LGYLKATVTY GLRHEETGTA FAHWLAERT
//