ID   C0ZRC6_RHOE4            Unreviewed;       487 AA.
AC   C0ZRC6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   10-JUN-2026, entry version 72.
DE   RecName: Full=alpha,alpha-trehalose-phosphate synthase (ADP-forming) {ECO:0000256|ARBA:ARBA00012842};
DE            EC=2.4.1.347 {ECO:0000256|ARBA:ARBA00012842};
GN   Name=otsA {ECO:0000313|EMBL:BAH31676.1};
GN   OrderedLocusNames=RER_09680 {ECO:0000313|EMBL:BAH31676.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31676.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|EMBL:BAH31676.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT   strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-
CC         trehalose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:53880,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.4.1.347;
CC         Evidence={ECO:0000256|ARBA:ARBA00048311};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-
CC         trehalose 6-phosphate + CDP + H(+); Xref=Rhea:RHEA:53884,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58069, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:61548, ChEBI:CHEBI:137927;
CC         Evidence={ECO:0000256|ARBA:ARBA00001525};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-glucose + D-glucose 6-phosphate = alpha,alpha-
CC         trehalose 6-phosphate + GDP + H(+); Xref=Rhea:RHEA:14605,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58189, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:61548, ChEBI:CHEBI:62230;
CC         Evidence={ECO:0000256|ARBA:ARBA00047452};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=TDP-alpha-D-glucose + D-glucose 6-phosphate = 5-methyl-UDP +
CC         alpha,alpha-trehalose 6-phosphate + H(+); Xref=Rhea:RHEA:53888,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58429, ChEBI:CHEBI:61417,
CC         ChEBI:CHEBI:61548, ChEBI:CHEBI:137931;
CC         Evidence={ECO:0000256|ARBA:ARBA00093268};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|ARBA:ARBA00008799}.
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DR   EMBL; AP008957; BAH31676.1; -; Genomic_DNA.
DR   RefSeq; WP_020906320.1; NC_012490.1.
DR   AlphaFoldDB; C0ZRC6; -.
DR   GeneID; 57488890; -.
DR   KEGG; rer:RER_09680; -.
DR   eggNOG; COG0380; Bacteria.
DR   HOGENOM; CLU_002351_7_1_11; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0047260; F:alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity; IEA:RHEA.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:TreeGrafter.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IEA:TreeGrafter.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
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:0000313|EMBL:BAH31676.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002204};
KW   Transferase {ECO:0000313|EMBL:BAH31676.1}.
SQ   SEQUENCE   487 AA;  54570 MW;  3F0F824966D3B244 CRC64;
     MSGQAEFVVV ANRLPVDLER LPDGTTRWKR SPGGLVTALE PILRSNQGAW VGWAGVPDAD
     LDPIVEDGLE LYPVPLSAEE INEYYEGFSN ATLWPLYHDV IVKPEYHREW WNAYVEVNRR
     FAEATSKAAA QGATVWIQDY QLQLVPKMLR MLRPDLTIGF FLHIPFPPVE LFMQMPWRTE
     IVEGLLGADL IGFHLPGGAQ NFLYLARRLA GQQTSRGTVG VRSKLGVVQV GFRSVRVGAF
     PISIDSGKLD ELSRTKAIRD RAKQIRKELG NPKHIMLGVD RLDYTKGIDV RLAALHELLM
     EKRIDPADTV MVQLATPSRE RVESYVQMRG DIEQKVSRIN GEFSEVGRPV VHYIHRPIPR
     DELVAFFVAA DLMLVTPLRD GMNLVAKEYV ACRSDLGGAL LLSEFTGAAA ELRQAFLCNP
     HDLDDVKDSM EKALNQPRED GRRHMRALRR QVLTHDVDRW ARSFLDALAH GGAAGPALIA
     PAEAQDH
//