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Database: UniProt
Entry: Q8TVK8_METKA
LinkDB: Q8TVK8_METKA
Original site: Q8TVK8_METKA 
ID   Q8TVK8_METKA            Unreviewed;       555 AA.
AC   Q8TVK8;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Glucosyl-3-phosphoglycerate synthase {ECO:0000256|ARBA:ARBA00040894};
DE            EC=2.4.1.266 {ECO:0000256|ARBA:ARBA00039022};
GN   OrderedLocusNames=MK1381 {ECO:0000313|EMBL:AAM02594.1};
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales;
OC   Methanopyraceae; Methanopyrus.
OX   NCBI_TaxID=190192 {ECO:0000313|EMBL:AAM02594.1, ECO:0000313|Proteomes:UP000001826};
RN   [1] {ECO:0000313|EMBL:AAM02594.1, ECO:0000313|Proteomes:UP000001826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938
RC   {ECO:0000313|Proteomes:UP000001826};
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02594.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TVK8; -.
DR   STRING; 190192.MK1381; -.
DR   CAZy; GT81; Glycosyltransferase Family 81.
DR   PaxDb; 190192-MK1381; -.
DR   EnsemblBacteria; AAM02594; AAM02594; MK1381.
DR   KEGG; mka:MK1381; -.
DR   HOGENOM; CLU_478695_0_0_2; -.
DR   InParanoid; Q8TVK8; -.
DR   OrthoDB; 11098at2157; -.
DR   Proteomes; UP000001826; 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; 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; 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:UP000001826};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        278..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..145
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
SQ   SEQUENCE   555 AA;  61531 MW;  94FF4BCE33CBA6EA CRC64;
     MLDGGLTLLV LTALALFRER KKRPQKVSVV IPAYNEEKTV ARVVRAAKEC DLVNEVIVVD
     DGSEDRTAEE AEAAGAIVIS HSVNRGKGEA MKTGLKHASG EIVAFVDADI KNIRPEMIEK
     MIRPVLEGEA DLVKTKFKRK AGRVTLLTAK PLLRFFFPEV AHLEQPLSGQ ICARRKLLER
     VDFEPDYGVD IGIILDAVAL GARIEEVDIG EIKHEMQPLE RLHRMALQVV RTILDRAHKY
     GRVVLRWNVG KALNRMNLGV SLLALALATL FYTELPLASV LALGILGLGI ALFSLAQLVY
     ELLRVEGKKR RILRPFLHMH ASVIMSLAVV AVLVGAMFSS IQIAHDRVEV NPLPRKVVWG
     EREVKAEGPY VVQYGRELKM GRNVLKVLDL KPDDVLVYQR GEYRVESAGR DNLLMVPTEL
     ARQLGIKPGN ATDSEIRLAF RNITVKRKVE GPDVNIRVTA VLSATPDRAE ALTVYVDGKK
     EAWIPVATRG GSVYVYVSGY GLIKLEDRSV VYVGNREILL KLEDTDIETL LLAPAEPTPF
     AVIELKMPSV RAVVE
//
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