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Database: UniProt
Entry: Q8NNR1_CORGL
LinkDB: Q8NNR1_CORGL
Original site: Q8NNR1_CORGL 
ID   Q8NNR1_CORGL            Unreviewed;       595 AA.
AC   Q8NNR1;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   12-SEP-2018, entry version 105.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
GN   OrderedLocusNames=Cgl2125 {ECO:0000313|EMBL:BAB99519.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS   LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB99519.1, ECO:0000313|Proteomes:UP000000582};
RN   [1] {ECO:0000313|Proteomes:UP000000582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
RC   {ECO:0000313|Proteomes:UP000000582};
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-alpha-D-glucosidic
CC       linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to
CC       yield trehalose and (1->4)-alpha-D-glucan.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|PIRNR:PIRNR006337, ECO:0000256|SAAS:SAAS00964676}.
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DR   EMBL; BA000036; BAB99519.1; -; Genomic_DNA.
DR   RefSeq; NP_601327.2; NC_003450.3.
DR   RefSeq; WP_011014899.1; NC_006958.1.
DR   ProteinModelPortal; Q8NNR1; -.
DR   STRING; 196627.NCgl2045; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   World-2DPAGE; 0001:Q8NNR1; -.
DR   EnsemblBacteria; BAB99519; BAB99519; BAB99519.
DR   GeneID; 1020077; -.
DR   KEGG; cgl:NCgl2045; -.
DR   PATRIC; fig|196627.13.peg.2064; -.
DR   eggNOG; ENOG4105C9C; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   KO; K01236; -.
DR   OMA; FTPMLFM; -.
DR   BioCyc; CORYNE:G18NG-11718-MONOMER; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012768; Trehalose_TreZ.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF11941; DUF3459; 1.
DR   PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000582};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000582}.
FT   DOMAIN      125    476       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    270    270       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    307    307       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        403    403       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   595 AA;  65737 MW;  501C18E977D616EA CRC64;
     MCHSISHLSS PTGSIFTSLV AMLTSQSFSV WAPLPHDVHL ILNGETLPMH KTEGSWWRAE
     IAPKAGDRYG FSLFDGSSWS KTLPDPRSTS QPDGVHGLSE VSDDSYLWGD QQWTGRILPG
     SVLYELHVGT FSEDGTFEGV VDKLPYLRDL GVTAIELLPV QPFGGNRNWG YDGVLWHAVH
     AGYGGPAGLK KLIDASHQAG IAVYLDVVYN HFGPDGNYNG QFGPYTSGGS TGWGDVVNIN
     GHDSDEVRNY ILDAARQWFE DFHVDGLRLD AVHSLDDRGA YSLLAQLTMV AEDVSAQTGI
     PRSLIAESEL NDPKFVTSRE AGGFGLDAQW VDDIHHALHA LVSGERNGYY SDFGSVDTLA
     KTLREVFEHT GNYSTYRGRN HGRPVHPDIT PASRFVTYTT THDQTGNRAI GDRPSTTLTP
     EQQVLKAAII YSSPYTPMLF MGEEFGATTP FAFFCSHTDP ELNRLTSEGR KREFARLGWN
     ADDIPSPELE STFTSSKLDW EFTAEQRRIN DAYKQLLHLR HTLGFSQPNL LTLEVEHGEN
     WLSMANGRGR ILANFSDDTI TVPLGGELIY SFTSPTVTDT STTLQPWGFA ILTRN
//
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