OTSA_MYCTA
ID OTSA_MYCTA Reviewed; 500 AA.
AC A5U8G5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=MRA_3530;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ75315.1; -; Genomic_DNA.
DR RefSeq; WP_003900868.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U8G5; -.
DR SMR; A5U8G5; -.
DR STRING; 419947.MRA_3530; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; ABQ75315; ABQ75315; MRA_3530.
DR KEGG; mra:MRA_3530; -.
DR eggNOG; COG0380; Bacteria.
DR HOGENOM; CLU_002351_7_1_11; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 556566at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001988; 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_0000348923"
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; 55862 MW; 5200FA01BB77CA8D 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 DTVVVQLATP SRERVESYQT LRNDIERQVG
HINGEYGEVG HPVVHYLHRP APRDELIAFF VASDVMLVTP LRDGMNLVAK EYVACRSDLG
GALVLSEFTG AAAELRHAYL VNPHDLEGVK DGIEEALNQT EEAGRRRMRS LRRQVLAHDV
DRWAQSFLDA LAGAHPRGQG
