ID A0A1F7BFK1_9BACT Unreviewed; 430 AA.
AC A0A1F7BFK1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN ORFNames=A2706_04030 {ECO:0000313|EMBL:OGJ56372.1};
OS Candidatus Peribacteria bacterium RIFCSPHIGHO2_01_FULL_51_35.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria.
OX NCBI_TaxID=1801914 {ECO:0000313|EMBL:OGJ56372.1, ECO:0000313|Proteomes:UP000179226};
RN [1] {ECO:0000313|EMBL:OGJ56372.1, ECO:0000313|Proteomes:UP000179226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP;
CC Xref=Rhea:RHEA:31319, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58885, ChEBI:CHEBI:62600;
CC EC=2.4.1.266; Evidence={ECO:0000256|ARBA:ARBA00036914};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320;
CC Evidence={ECO:0000256|ARBA:ARBA00036914};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-
CC (alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-
CC diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600,
CC ChEBI:CHEBI:76533; EC=2.4.1.266;
CC Evidence={ECO:0000256|ARBA:ARBA00035799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245;
CC Evidence={ECO:0000256|ARBA:ARBA00035799};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:OGJ56372.1}.
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DR EMBL; MFXP01000004; OGJ56372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7BFK1; -.
DR Proteomes; UP000179226; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd04179; DPM_DPG-synthase_like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR016965; Pase_PHOSPHO-typ.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR48090:SF9; GLUCOSYL-3-PHOSPHOGLYCERATE SYNTHASE; 1.
DR PANTHER; PTHR48090; UNDECAPRENYL-PHOSPHATE 4-DEOXY-4-FORMAMIDO-L-ARABINOSE TRANSFERASE-RELATED; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..122
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 430 AA; 48113 MW; D4065FED842F5F94 CRC64;
MDKVTCVLPA LNEKKTIGTL IRILKNVKEI GEIVVVDDGS TDGTGIIAKR CGARVIRHLR
NQGKGAAVKT GASHATHDLL LFLDADLQNL TSAKVRKVIR PLLKNTADFV KASFTNSSGR
VTKLVAKPLL SIVHPFVKLE QPLSGQFAFN RKKIDMDAIE DGWGVDIQLV FQAMRKKLRI
QEVFIGALKH KHQSTEALSA MSEQVMRTIL SELNLICNKK KVIFFDLDET LIQESSIAVL
AKEWGFSEEL KKLQRRVRAG EVPDKVITKA LAKHFKGRTR EEVSALCERL LHINPFAAKV
IDSLRRQRYR VRIVSSAFSP VVRHFAAALN VYDFFAPRLA RDSTGRFTGT LKRSRFEDQT
CACCGRYVCK AKAVRYMLRR FKIAKDEAIA VGDGKSDACM FKTCGTSLGF RANATDKRID
QLSEVLMYAD
//