ID F6D5G1_METPW Unreviewed; 574 AA.
AC F6D5G1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN OrderedLocusNames=MSWAN_2308 {ECO:0000313|EMBL:AEG19313.1};
OS Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=868131 {ECO:0000313|EMBL:AEG19313.1, ECO:0000313|Proteomes:UP000009231};
RN [1] {ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. SWAN-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG19313.1, ECO:0000313|Proteomes:UP000009231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25820 / JCM 18151 / SWAN1
RC {ECO:0000313|Proteomes:UP000009231};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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; CP002772; AEG19313.1; -; Genomic_DNA.
DR RefSeq; WP_013826812.1; NC_015574.1.
DR AlphaFoldDB; F6D5G1; -.
DR STRING; 868131.MSWAN_2308; -.
DR GeneID; 10669837; -.
DR KEGG; mew:MSWAN_2308; -.
DR eggNOG; arCOG00894; Archaea.
DR HOGENOM; CLU_478695_0_0_2; -.
DR Proteomes; UP000009231; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEG19313.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..140
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 574 AA; 63316 MW; D387DD6C4D93047C CRC64;
MSWTILMLFL LLASFRTIKK PKDMTVSVII PAYNEAKTVK HVVSVAKSLS YILEIIVVDD
GSTDGTARIA EEAGARVIRH LENKGKGAAI KTGFTNSKGD IAVFLDADLH NLTADQVERI
IKPILNGEAD ITKTKFKREA GRVTQLTAKP LLDFFFPEVK FDQPLSGQFA AKRSFLSSIK
LEDDYGVDVG IVLDADVRGM RVKEVDIGKI DHVLSSLGDL NLMATEVVRT IVDRAMEYGR
VTMMDSLGKS IRMGILGLSL TILGVFCIFF ITFVPLNFGL VISVVGMIIA IFYIAKIIKM
SFHIIRRSEA KLRTLKSFFY MHSPIIVSGL ILIAMLTTLL GSVHIYDGKI SVEPSSRNLI
YWIEPAHNQS VDVRGPYTVD SALENEYTIM RMTPESIATL ELGYGDAVYI NNQQYILNQS
LPGEGNTIRI PYNARNFLGI NVGDVISDSN LRNVFKNVYA AKNLQLQNTN SNITVKEGVL
IKTDSENGRA VNISINGTPV TMTSGIFKNG AYSIYVDGSR YKTIEINDDT SSTSYYVKVG
EYTIKIDIGA LGTAQSDMEF APSSEGKFLN FTSS
//
