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TREH_MYCTU
ID   TREH_MYCTU              Reviewed;         680 AA.
AC   P71741; L0TB43;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Trehalase;
DE            EC=3.2.1.28;
DE   AltName: Full=Alpha,alpha-trehalase;
DE   AltName: Full=Alpha,alpha-trehalose glucohydrolase;
GN   OrderedLocusNames=Rv2402;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-16 AND 20-48, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17319935; DOI=10.1111/j.1742-4658.2007.05715.x;
RA   Carroll J.D., Pastuszak I., Edavana V.K., Pan Y.T., Elbein A.D.;
RT   "A novel trehalase from Mycobacterium smegmatis - purification, properties,
RT   requirements.";
RL   FEBS J. 274:1701-1714(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of alpha,alpha-trehalose into two
CC       molecules of D-glucose. {ECO:0000269|PubMed:17319935}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-
CC         glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28;
CC         Evidence={ECO:0000269|PubMed:17319935};
CC   -!- COFACTOR:
CC       Name=phosphate; Xref=ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:17319935};
CC       Note=Shows an absolute requirement for inorganic phosphate for
CC       activity. The function of the phosphate may involve stabilizing the
CC       protein conformation and/or initiating protein aggregation. Unlike the
CC       threhalase ortholog in M.smegmatis, does not require Mg(2+) for
CC       activity. {ECO:0000269|PubMed:17319935};
CC   -!- PATHWAY: Glycan degradation; trehalose degradation; D-glucose from
CC       alpha,alpha-trehalose: step 1/1.
CC   -!- SUBUNIT: Homomultimer. {ECO:0000269|PubMed:17319935}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP45193.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP45193.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70683; E70683.
DR   RefSeq; NP_216918.3; NC_000962.3.
DR   AlphaFoldDB; P71741; -.
DR   SMR; P71741; -.
DR   STRING; 83332.Rv2402; -.
DR   CAZy; GH15; Glycoside Hydrolase Family 15.
DR   PaxDb; P71741; -.
DR   DNASU; 885661; -.
DR   GeneID; 885661; -.
DR   KEGG; mtu:Rv2402; -.
DR   PATRIC; fig|83332.12.peg.2688; -.
DR   TubercuList; Rv2402; -.
DR   eggNOG; COG3387; Bacteria.
DR   InParanoid; P71741; -.
DR   UniPathway; UPA00300; UER00535.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004555; F:alpha,alpha-trehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0015927; F:trehalase activity; IDA:MTBBASE.
DR   GO; GO:0005993; P:trehalose catabolic process; IDA:MTBBASE.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045582; Trehalase-like_N.
DR   Pfam; PF19291; DUF5911; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..680
FT                   /note="Trehalase"
FT                   /id="PRO_0000413980"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   680 AA;  76518 MW;  0217C57C76280BA1 CRC64;
     MVLHAQPPDQ STETAREAKA LAGATDGATA TSADLHAPMA LSSSSPLRNP FPPIADYAFL
     SDWETTCLIS PAGSVEWLCV PRPDSPSVFG AILDRSAGHF RLGPYGVSVP SARRYLPGSL
     IMETTWQTHT GWLIVRDALV MGKWHDIERR SRTHRRTPMD WDAEHILLRT VRCVSGTVEL
     MMSCEPAFDY HRLGATWEYS AEAYGEAIAR ANTEPDAHPT LRLTTNLRIG LEGREARART
     RMKEGDDVFV ALSWTKHPPP QTYDEAADKM WQTTECWRQW INIGNFPDHP WRAYLQRSAL
     TLKGLTYSPT GALLAASTTS LPETPRGERN WDYRYAWIRD STFALWGLYT LGLDREADDF
     FAFIADVSGA NNNERHPLQV MYGVGGERSL VEAELHHLSG YDHARPVRIG NGAYNQRQHD
     IWGSILDSFY LHAKSREQVP ENLWPVLKRQ VEEAIKHWRE PDRGIWEVRG EPQHFTSSKV
     MCWVALDRGA KLAERQGEKS YAQQWRAIAD EIKADILEHG VDSRGVFTQR YGDEALDASL
     LLVVLTRFLP PDDPRVRNTV LAIADELTED GLVLRYRVHE TDDGLSGEEG TFTICSFWLV
     SALVEIGEVG RAKRLCERLL SFASPLLLYA EEIEPRSGRH LGNFPQAFTH LALINAVVHV
     IRAEEEADSS GMFQPANAPM
 
 
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