ID Q6NFC8_CORDI Unreviewed; 479 AA.
AC Q6NFC8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 OrderedLocusNames=DIP1966 {ECO:0000313|EMBL:CAE50497.1};
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE50497.1, ECO:0000313|Proteomes:UP000002198};
RN [1] {ECO:0000313|EMBL:CAE50497.1, ECO:0000313|Proteomes:UP000002198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC {ECO:0000313|Proteomes:UP000002198};
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248359; CAE50497.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6NFC8; -.
DR STRING; 257309.DIP1966; -.
DR KEGG; cdi:DIP1966; -.
DR HOGENOM; CLU_002351_7_1_11; -.
DR Proteomes; UP000002198; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000002198}.
SQ SEQUENCE 479 AA; 52831 MW; 2D61064EE537E92A CRC64;
MSAIESNEGE QLFDFVVVAN RLPVDLSTSA DGSPRWVASP GGLVTALTPV LAGNRGCWVG
WHGGTGPAPD PFRTDTNIWV HPVALSDHDF EGFYEGFSNA TLWPLYHDLI VSPVYNRDWW
TAYREVNLKF ASAVAEVAAE GAVVWIQDYQ LQLVPGILRQ IRPDLTIGFF LHIPFPHSDL
FRQLPWREEI VRGLLGADLV GFHLTSSANN FLDLAAALGL EAQGRAKVRE VSATVTAGDG
HVVSVAAYPI SIDVEPLIAS HSNRDEIRAE FGYPETLILG VDRLDYTKGI LQRLLAFEEL
LESGAIDPNT TVFAQVATPS RERIEHYKQA RSEVEEAVGR INGRFGSIGR SVVHYHHRHM
DRSELNKLYR AADVMLVTPF KDGMNLVAKE YVSCHSDGSG AMVLSEFAGA AVELEQAFLC
NPFDLESIKR QIAGAVTTLK NHPEAARDRM LAMHQQVVDH DVNVWASAFL RDLSSAHTS
//
