ID A2SMF4_METPP Unreviewed; 463 AA.
AC A2SMF4;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Mpe_A3790 {ECO:0000313|EMBL:ABM96743.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM96743.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM96743.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96743.1; -; Genomic_DNA.
DR RefSeq; WP_011831363.1; NC_008825.1.
DR AlphaFoldDB; A2SMF4; -.
DR STRING; 420662.Mpe_A3790; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR KEGG; mpt:Mpe_A3790; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_4; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000000366; 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 Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
SQ SEQUENCE 463 AA; 51602 MW; 2CD831F8D54F484C CRC64;
MTSRLVVVSN RIGDPRKAAA GGLAVALGDA LSESGGLWFG WSGKVVAGGA RGEGDLHLQP
SGKVTLATLD LGSDDHAAYY AGYSNRVLWP VFHYRLDLAQ FDDGYFEGYQ RVNRLFARKL
STLLKPDDII WVHDYHLIPL AAELRALGCR QRIGFFLHIP MPPPLVMAAI PAHDMLMRSL
FAYDLIGLQS EADVAHFARY VEMEAGAERL GRDQYRAFGQ QVCARAFPIG IDVDEFQALA
QTPESIETRE TLRSQYPLRQ LLIGVDRLDY SKGLPQRLRA FHRLLADYPE NRNSATLIQV
ATPTREGVES YEDIRRELEG LSGQINGEYG ELDWMPVRYI HRTLARRRLP GLYRAGRVAL
VTPLRDGMNL VAKEFVAAQD AADPGVLVLS RFAGAAEQMR AALLVNPYDI GATAGAVQRA
LRMPLSERVE RHQALLAGVR EHDVHRWRRE FLQALQAAER APG
//
