ID T0ZSL2_9ZZZZ Unreviewed; 170 AA.
AC T0ZSL2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00012560};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
DE Flags: Fragment;
GN ORFNames=B2A_06951 {ECO:0000313|EMBL:EQD51271.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD51271.1};
RN [1] {ECO:0000313|EMBL:EQD51271.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD51271.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQD51271.1}.
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DR EMBL; AUZZ01004964; EQD51271.1; -; Genomic_DNA.
DR AlphaFoldDB; T0ZSL2; -.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EQD51271.1};
KW Hydrolase {ECO:0000313|EMBL:EQD51271.1};
KW Transferase {ECO:0000313|EMBL:EQD51271.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EQD51271.1"
FT NON_TER 170
FT /evidence="ECO:0000313|EMBL:EQD51271.1"
SQ SEQUENCE 170 AA; 19721 MW; BB7FA4B5E66C357E CRC64;
WWSWPEPLRE REPAALRRLR HERVARIEQV RAEQFAFFVQ WRRLQDYAHA HGVRLFGDLP
FYIGPMSAET WTDREQFQLT PEGRPAAVAG VPPDYFCEGG QVWGNPLYDW TAMGRDGFAF
WRARVRAQLG RVDLLRVDHF RAFAAHWAIP AGAPDARGGR WCPTPGHEVL
//
