OTSA_MYCBO
ID OTSA_MYCBO Reviewed; 500 AA.
AC Q7TWE1; A0A1R3Y4A1; X2BP60;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000250|UniProtKB:P9WN11};
DE Short=TPS {ECO:0000250|UniProtKB:P9WN11};
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:P9WN11};
DE EC=2.4.1.347 {ECO:0000250|UniProtKB:P9WN11};
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000250|UniProtKB:P9WN11};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000250|UniProtKB:P31677};
DE Short=OtsA {ECO:0000250|UniProtKB:P31677};
GN Name=otsA {ECO:0000250|UniProtKB:P9WN11}; OrderedLocusNames=BQ2027_MB3520;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Probably involved in the osmoprotection via the biosynthesis
CC of trehalose and in the production of glycogen and alpha-glucan via the
CC TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate
CC (M1P). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to
CC D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Probably
CC also able to use ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc as glucosyl
CC donors. {ECO:0000250|UniProtKB:P9WN11}.
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:0000250|UniProtKB:P9WN11};
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:0000250|UniProtKB:P9WN11};
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:0000250|UniProtKB:P9WN11};
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:0000250|UniProtKB:P9WN11};
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:0000250|UniProtKB:P9WN11};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000250|UniProtKB:P9WN11}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P9WN11}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000250|UniProtKB:P9WN11}.
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DR EMBL; LT708304; SIU02147.1; -; Genomic_DNA.
DR RefSeq; NP_857159.1; NC_002945.3.
DR RefSeq; WP_003418951.1; NC_002945.4.
DR AlphaFoldDB; Q7TWE1; -.
DR SMR; Q7TWE1; -.
DR EnsemblBacteria; SIU02147; SIU02147; BQ2027_MB3520.
DR GeneID; 45427476; -.
DR PATRIC; fig|233413.5.peg.3859; -.
DR OMA; YYGFSNR; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001419; Chromosome.
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:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..500
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000348904"
FT BINDING 28
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 48..49
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 108
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 162
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 304
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 309
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 342
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 407..411
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 117
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 187
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
SQ SEQUENCE 500 AA; 55877 MW; B79269D3A64B30DC CRC64;
MAPSGGQEAQ ICDSETFGDS DFVVVANRLP VDLERLPDGS TTWKRSPGGL VTALEPVLRR
RRGAWVGWPG VNDDGAEPDL HVLDGPIIQD ELELHPVRLS TTDIAQYYEG FSNATLWPLY
HDVIVKPLYH REWWDRYVDV NQRFAEAASR AAAHGATVWV QDYQLQLVPK MLRMLRPDLT
IGFFLHIPFP PVELFMQMPW RTEIIQGLLG ADLVGFHLPG GAQNFLILSR RLVGTDTSRG
TVGVRSRFGA AVLGSRTIRV GAFPISVDSG ALDHAARDRN IRRRAREIRT ELGNPRKILL
GVDRLDYTKG IDVRLKAFSE LLAEGRVKRD DTVLVQLATP SRERVESYQT LRNDIERQVG
HINGEYGEVG HPVVHYLHRP APRDELIAFF VASDVMLVTP LRDGMNLVAK EYVACRSDLG
GALVLSEFTG AAAELRHAYL VNPHDLEGVK DGIEEALNQT EEAGRRRMRS LRRQVLAHDV
DRWAQSFLDA LAGAHPRGQG
