ID Q2NEA2_METST Unreviewed; 606 AA.
AC Q2NEA2;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN OrderedLocusNames=Msp_1481 {ECO:0000313|EMBL:ABC57851.1};
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860 {ECO:0000313|EMBL:ABC57851.1, ECO:0000313|Proteomes:UP000001931};
RN [1] {ECO:0000313|EMBL:ABC57851.1, ECO:0000313|Proteomes:UP000001931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3
RC {ECO:0000313|Proteomes:UP000001931};
RX PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57851.1; -; Genomic_DNA.
DR RefSeq; WP_011407050.1; NC_007681.1.
DR AlphaFoldDB; Q2NEA2; -.
DR STRING; 339860.Msp_1481; -.
DR CAZy; GT81; Glycosyltransferase Family 81.
DR GeneID; 41326055; -.
DR KEGG; mst:Msp_1481; -.
DR eggNOG; arCOG00894; Archaea.
DR HOGENOM; CLU_478695_0_0_2; -.
DR OrthoDB; 11098at2157; -.
DR Proteomes; UP000001931; 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:UP000001931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..152
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 606 AA; 67800 MW; D9350CB8E3B933AF CRC64;
MLQVIPIILI IIVSLLYFGD KSSKVNDTVS VVIPAFNEEK SIKHVIDTVK QVKSITEIIV
VDDGSTDKTY DIVSKEDVVL IKHKINKGKG SAMKTGLKKV TNNIILFLDA DLSEINKKQV
ESIIRPIIKG NADITKTKFK REAGRVTELT AKPLLQFFFP ELSFEQPLSG QFAATKNFLD
TIDLEKDYGV DIGIVLDADA RGMRIHEVDI GNIVHEMSSL KELNLMANEV VRTIVDRAIN
YGRLTMVDDL GSSIRMEIMG LSLITLGIFG LFFIRFMTTW MSSFIIIIGL IISILYIIKI
IKMSLRIYGQ SKVSKKQIFK SFIHMHFPIV ISIIILLLLT VSLVGSVTIS SNQISIEPAS
KNLIISTSPE PHKGVDVRGP YTIENALENE EQLIRLPTSA LSTLQSQYGD NIYINHEKYQ
LEQSLEGEND LIRMPELARS NLEVNPGDVI RDSDFKTKFE NTQQVKNIKV DENTLDKNLN
NTTINVDINH TNASVGTEIK SQQLPEKILT VYVNDTEIGK VLASVTNTSY SIYLNEGYSD
TIDLNSNTHG VIYNQTYKNS TIEVVLEDSG ANTTTEFAND DSYVKFLNIN IDNVTINNTT
TTTQKD
//
