ID   TREY_MYCTO              Reviewed;         765 AA.
AC   P9WQ20; L0T775; Q10768;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Putative maltooligosyl trehalose synthase;
DE            EC=5.4.99.15;
DE   AltName: Full=(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase;
GN   Name=treY; OrderedLocusNames=MT1614;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the conversion of maltooligosaccharide into the
CC       non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl
CC       alpha-D-glucoside) by intramolecular transglycosylation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha-
CC         D-glucosyl](n-1)-alpha-D-glucose; Xref=Rhea:RHEA:13621, Rhea:RHEA-
CC         COMP:14708, Rhea:RHEA-COMP:14709, ChEBI:CHEBI:140774,
CC         ChEBI:CHEBI:140775; EC=5.4.99.15;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45881.1; -; Genomic_DNA.
DR   PIR; H70763; H70763.
DR   RefSeq; WP_003407790.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ20; -.
DR   SMR; P9WQ20; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAK45881; AAK45881; MT1614.
DR   KEGG; mtc:MT1614; -.
DR   PATRIC; fig|83331.31.peg.1736; -.
DR   HOGENOM; CLU_005045_1_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0047470; F:(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11336; AmyAc_MTSase; 1.
DR   Gene3D; 1.10.10.470; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013797; Maltooligo_trehalose_synth_4.
DR   InterPro; IPR012767; Trehalose_TreY.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR02401; trehalose_TreY; 1.
PE   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..765
FT                   /note="Putative maltooligosyl trehalose synthase"
FT                   /id="PRO_0000426852"
SQ   SEQUENCE   765 AA;  82707 MW;  34E9A5CB53624D6A CRC64;
     MAFPVISTYR VQMRGRSNGF GFTFADAENL LDYLDDLGVS HLYLSPILTA VGGSTHGYDV
     TDPTTVSPEL GGSDGLARLS AAARSRGMGL IVDIVPSHVG VGKPEQNAWW WDVLKFGRSS
     AYAEFFDIDW ELGDGRIILP LLGSDSDVAN LRVDGDLLRL GDLALPVAPG SGDGTGPAVH
     DRQHYRLVGW RHGLCGYRRF FSITSLAGLR QEDRAVFDAS HAEVARWFTE GLVDGVRVDH
     LDGLSDPSGY LAQLRELLGP NAWIVVEKIL AVDEALEPTL PVDGSTGYDV LREIGGVLVD
     PQGESPLTAL VESAGVDYQE MPAMLADLKV HAAVHTLASE LRRLRRCIAA AAGADHPLLP
     AAVAALLRHI GRYRCDYPGQ AAVLPCALAE THSTTPQLAP GLQLIAAAVA RGGEPAVRLQ
     QLCGAVSAKA VEDCMFYRDA RLVSLNEVGG EPRRFGVGAA EFHHRAATRA RLWPRSMTTL
     STHDTKRGED VRARIGVLSQ VPWLWAKFIG HAQAIAPAPD AVTGQFLWQN VFGVWPVSGE
     VSAALRGRLH TYAEKAIREA AWHTSWHNPN RAFEDDVHGW LDLVLDGPLA SELTGLVAHL
     NSHAESDALA AKLLALTVPG VPDVYQGSEL WDDSLVDPDN RRPVDYGTRR VALKALQHPK
     IRVLAAALRL RRTHPESFLG GAYHPVFAAG PAADHVVAFR RGDDILVAVT RWTVRLQQTG
     WDHTVLPLPD GSWTDALTGF TASGHTPAVE LFADLPVVLL VRDNA