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Database: UniProt
Entry: C1ASL2_RHOOB
LinkDB: C1ASL2_RHOOB
Original site: C1ASL2_RHOOB 
ID   C1ASL2_RHOOB            Unreviewed;       480 AA.
AC   C1ASL2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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:BAH48461.1};
GN   OrderedLocusNames=ROP_02140 {ECO:0000313|EMBL:BAH48461.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48461.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48461.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48461.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP +
CC         alpha,alpha-trehalose 6-phosphate + 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:ARBA00001801};
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=D-glucose 6-phosphate + GDP-alpha-D-glucose = 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:ARBA00000839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + TDP-alpha-D-glucose = alpha,alpha-
CC         trehalose 6-phosphate + H(+) + TDP; 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:ARBA00000159};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|ARBA:ARBA00008799}.
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DR   EMBL; AP011115; BAH48461.1; -; Genomic_DNA.
DR   RefSeq; WP_012687470.1; NC_012522.1.
DR   AlphaFoldDB; C1ASL2; -.
DR   STRING; 632772.ROP_02140; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   KEGG; rop:ROP_02140; -.
DR   PATRIC; fig|632772.20.peg.247; -.
DR   HOGENOM; CLU_002351_7_1_11; -.
DR   OrthoDB; 9761633at2; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0047260; F:alpha,alpha-trehalose-phosphate synthase (GDP-forming) activity; IEA:RHEA.
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:BAH48461.1};
KW   Transferase {ECO:0000313|EMBL:BAH48461.1}.
SQ   SEQUENCE   480 AA;  53307 MW;  54147F8E3F6DA61C CRC64;
     MNDSAPHGTS DFVVVANRLP VDMETLDDGT TRWKRSPGGL VTALEPILLG RERGSWVGWP
     GVPDTKVEPI VSGGVDLFPV ELSSDEVARY YEGFSNATLW PLYHDVLVAP VFDRDWWHTY
     LEVNRHFAEE TARTAAEGAT VWVQDYQLQL VPRLLREMRP DLTIGFFLHI PFPPVELFMQ
     LPWRKEIVEG LLGADLIGFH LPGGAHNFLF LARRLLGLDA TTAGVGVRGA LGTVTLDDRV
     VHVGAFPISV DARKLVEQAT EPAVVERAAE IRRELGNPRK ILLGVDRLDY TKGIDLRLSA
     LGELLDEGRL DPSDTVMVQL ATPSRERVEH YMKMRSSIEE QVSHINGDHG QIGRPVVHYL
     YQPVDRSELI ALFLAADVML VTPMRDGMNL VAKEYVACRA DLGGALVLSE FAGAAAELRG
     AYLVNPHDLD GVKNTIVAAL GQEREQGRRR MSRLHRQVLD HDVHRWAQSF LGALDPNAAD
//
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