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Database: UniProt
Entry: E3GWV0_METFV
LinkDB: E3GWV0_METFV
Original site: E3GWV0_METFV 
ID   E3GWV0_METFV            Unreviewed;       570 AA.
AC   E3GWV0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE            EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN   OrderedLocusNames=Mfer_1233 {ECO:0000313|EMBL:ADP78019.1};
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP78019.1, ECO:0000313|Proteomes:UP000002315};
RN   [1] {ECO:0000313|EMBL:ADP78019.1, ECO:0000313|Proteomes:UP000002315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC   {ECO:0000313|Proteomes:UP000002315};
RX   PubMed=21304736;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
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};
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DR   EMBL; CP002278; ADP78019.1; -; Genomic_DNA.
DR   RefSeq; WP_013414297.1; NC_014658.1.
DR   AlphaFoldDB; E3GWV0; -.
DR   STRING; 523846.Mfer_1233; -.
DR   CAZy; GT81; Glycosyltransferase Family 81.
DR   GeneID; 9962983; -.
DR   KEGG; mfv:Mfer_1233; -.
DR   HOGENOM; CLU_478695_0_0_2; -.
DR   OrthoDB; 11098at2157; -.
DR   Proteomes; UP000002315; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd04179; DPM_DPG-synthase_like; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
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   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADP78019.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        274..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..157
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   570 AA;  64059 MW;  6301CCF482A1B8C2 CRC64;
     MYSMILIFII FLFLVVKRYK PRVSAVIPAY NEEETVADVV NAVKKSKYVD EIIVVDDGST
     DKTYEKALNA GAKVIKHEKN KGKGAALKTG FKESSGDIIL FLDADLKNIN PKKVDRIVEP
     IIRGEADITK SKFKRKAGRV TELTAKPLLN FFFPELNFKQ PLSGQFAAKR SVLEKVKFEE
     DYGVDIGIIL DADAHGFRIK EVDIGTLNHK MSDLSDLNLM ANEVVRTIVN RAVEYGRVAM
     MDTIGNSIRM CVLGLSLTSF GIFSIFFTRI IPLYVGIALS ILGFIVAMYY LVILLMKSCK
     IILTSKNPIS TIKSFIYMHF PVLVSALILF AILSALFGSI HVEKDKISIQ PVSGNLVIWK
     KAHENRTIAI KGPYTIDSAL ENESNIIRMP ADAIDTLGIN YGDKIYIYNL SYEVREPLPG
     ENNVIRMPQE IRSVLNVNIG DVIQDNNLRK IFKNVYVLRN IYTSEGLTVK EGVLIQTQSN
     ESKSVNIYFD NKFLVSTSGI MKEGYYSVYV NGIKVDTIYF DGNAPANYTI YWNGHIINIY
     IKENGQSDMM FANSLRGRFL DFNITNSSSL
//
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