ID I0IN86_LEPFC Unreviewed; 640 AA.
AC I0IN86;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938, ECO:0000256|PIRNR:PIRNR006337};
DE Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268, ECO:0000256|PIRNR:PIRNR006337};
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284, ECO:0000256|PIRNR:PIRNR006337};
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057, ECO:0000256|PIRNR:PIRNR006337};
GN OrderedLocusNames=LFE_1032 {ECO:0000313|EMBL:BAM06735.1};
OS Leptospirillum ferrooxidans (strain C2-3).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM06735.1, ECO:0000313|Proteomes:UP000007382};
RN [1] {ECO:0000313|EMBL:BAM06735.1, ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|EMBL:BAM06735.1,
RC ECO:0000313|Proteomes:UP000007382};
RX PubMed=22815442; DOI=10.1128/JB.00696-12;
RA Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA Kamijo T., Ohta H.;
RT "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT Japan.";
RL J. Bacteriol. 194:4122-4123(2012).
RN [2] {ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA Kamijo T., Ohta H.;
RT "The complete genome sequence of the pioneer microbe on fresh volcanic
RT deposit, Leptospirillum ferrooxidans strain C2-3.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC alpha-D-glucan.; EC=3.2.1.141;
CC Evidence={ECO:0000256|ARBA:ARBA00034013,
CC ECO:0000256|PIRNR:PIRNR006337};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|PIRNR:PIRNR006337}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRSR:PIRSR006337-1}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR006337}.
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DR EMBL; AP012342; BAM06735.1; -; Genomic_DNA.
DR AlphaFoldDB; I0IN86; -.
DR STRING; 1162668.LFE_1032; -.
DR KEGG; lfc:LFE_1032; -.
DR PATRIC; fig|1162668.3.peg.1200; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_020726_2_0_0; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000007382; 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 CDD; cd11325; AmyAc_GTHase; 1.
DR CDD; cd02853; E_set_MTHase_like_N; 1.
DR Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR006337};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006337};
KW Reference proteome {ECO:0000313|Proteomes:UP000007382}.
FT DOMAIN 137..481
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 320
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 281..286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 345..349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 413..418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 414
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 640 AA; 71330 MW; 18A83AF36D6F7EAB CRC64;
MDCSGHHLIS RNDIDSVALD HALGPIGAVL QKDGSVLFRV WAPQFFHVHL VLPDQKKSPL
LMVSEGNGYH HLSLSGIGVG TRYLFQLEGV GIYPDPASRW QPDGVHKASA VWFPEESFPS
PLPAWQGHRL DSLIIYELHV GTFTAEGTFD GLIQHLGHLQ ELGVTAIEVM PVASFPGERN
WGYDGVYLFA VQQSYGGPDG FGRFVRGCHE HGISVLLDVV YNHLGPEGNY LGKFAPYFSK
VSRTPWGDAI NFDGPESDHV RHFFLENLRT YLEVFDVDGF RFDAIHAIID QSPVPFLTDV
SRLCRQISEK RGRPVHLIGE SHQNDRRAVL PEDQNGIGFD SQWSDDFHHA LHVFLTGERE
GYYQDFSGAS DLPRIFSEGF LYQGEYAPSF RRRRGSSPEG LSGSSFVVFS QNHDQVGNRP
AADRLTARIP DAGLRLAASL TLLSPFLPLL FMGEEFGETN PFHYFTSHGD EDLINAVREG
RKREFQDFPG WTDHLDPQGL EVFENSRLSM LDPGSRIGSS LKLYAFYREL IRIRKSYPAL
VPPNTLPGPD CRLLPSNPPL LLVRREGGGE VVLIVGNLSE LPQRLGNILS NAPGRWSKVL
DSEEERWGGG GSLFPERLES SSDENVCAPY QVALYRGVAS
//
