ID Q2J1N2_RHOP2 Unreviewed; 494 AA.
AC Q2J1N2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000256|ARBA:ARBA00018539, ECO:0000256|RuleBase:RU362045};
DE EC=2.4.1.15 {ECO:0000256|ARBA:ARBA00012538, ECO:0000256|RuleBase:RU362045};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000256|RuleBase:RU362045};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000256|RuleBase:RU362045};
GN OrderedLocusNames=RPB_0917 {ECO:0000313|EMBL:ABD05628.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD05628.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD05628.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD05628.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in the osmoprotection via the biosynthesis
CC of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-
CC glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-
CC 6-phosphate. Acts with retention of the anomeric configuration of the
CC UDP-sugar donor. {ECO:0000256|RuleBase:RU362045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001516,
CC ECO:0000256|RuleBase:RU362045};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|RuleBase:RU362045}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU362045}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000256|ARBA:ARBA00008799, ECO:0000256|RuleBase:RU362045}.
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DR EMBL; CP000250; ABD05628.1; -; Genomic_DNA.
DR RefSeq; WP_011439817.1; NC_007778.1.
DR AlphaFoldDB; Q2J1N2; -.
DR STRING; 316058.RPB_0917; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR KEGG; rpb:RPB_0917; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_5; -.
DR OrthoDB; 9815690at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000008809; Chromosome.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362045};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
SQ SEQUENCE 494 AA; 53493 MW; 046B805B055A33D7 CRC64;
MNLVVVSNRV ARASSNEPMT GGLAAALLPV VEKSGAIWVG SSGRVRDGAQ REPFAEIEQL
GAGALAMLDL PAAHYGGYYE GFANSALWPA LHSRADLIRV SQDDYRSYRE VNSFMARALL
RFRKPDTAFW IQDYHFLALG AELRALGVTQ PIGFFLHTPW ASPATMGCVP HNRELVEAML
AYDLIGFQTE EDRSNFLAYG KAELGFAIAD GVVTTPYGTS RCEVFPIGID ADLFAQQAQK
ATAHPDVSRL RKSLNGEKLV IGVDRLDYSK GLINRVNAFD RMLTMRPSLQ RTVSLLQIAT
PSRGTIEAYG NLQGELAKLV SDVNGRLGEA DWTPIRYLNK GFRQGVLAGL YRTAQVGLVT
PLQDGMNLVA KEYVAAQNPI DPGVLVLSKF AGAANELDTA LLVNPHDVEG MARAIATALS
MPLTERRLRW EAMMAKLRRG SVQSWFADFV ASLEDAHTAN SDAAGALASQ PPALKMAGGW
SRGGPLAFGG ARLQ
//
