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Database: UniProt
Entry: A0A0L6U2T6_9FIRM
LinkDB: A0A0L6U2T6_9FIRM
Original site: A0A0L6U2T6_9FIRM 
ID   A0A0L6U2T6_9FIRM        Unreviewed;       511 AA.
AC   A0A0L6U2T6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN   ORFNames=AKG39_08015 {ECO:0000313|EMBL:KNZ42105.1};
OS   Acetobacterium bakii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ42105.1, ECO:0000313|Proteomes:UP000036873};
RN   [1] {ECO:0000313|Proteomes:UP000036873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA   Song Y., Hwang S., Cho B.-K.;
RT   "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT   psychrophilic chemical producer through syngas fermentation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU361207};
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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:KNZ42105.1}.
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DR   EMBL; LGYO01000019; KNZ42105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6U2T6; -.
DR   STRING; 52689.AKG39_08015; -.
DR   PATRIC; fig|52689.4.peg.731; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000036873; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR00217; malQ; 1.
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   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036873};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:KNZ42105.1}.
SQ   SEQUENCE   511 AA;  58522 MW;  E2317FBFDC8B2BD8 CRC64;
     MPLTERASGV LMHISSLPGD YGIGTLGREA KDFVDLLALM DCAYWQILPL GPTDNCHSPY
     KSTSAFAGNT EFIDLEILSE WGLLTKDELV SNRSPNPLYW VNFQELLKNQ EPVFKLAFQR
     LTPELKKSIR EFEEANRSWL PDFALYTTLT QDFSEMNWTK WKNKELVHRK PAALSQAIKK
     HSEEIDYHNF LQYAFYRQWS DLKTYANTKG IKIIGDIPIY VALESADVWS HSELFQLDAD
     GTPLFVAGVP PDYFSPDGQL WGNPLYHWAT MKADGYSWWM DRIKAALKAF DLVRIDHFRG
     FSAYWSVPAS ETTAKKGQWV PGPGMDFFNR VFEKHPKPGI IAEDLGVQDE ALAQLLSDTG
     LPGMRLMEFA FIDKNNNIHL PHNYTPNMVT YTGTHDNNTL LGTLFNYTPE QRNYALKYCG
     YLDTWPDQWQ VGGPQSPSCR SFIRSLWQSA ANLVIIPIQD VCGYGDDTRM NQPGTARGNW
     SFRMTKEGLS SVDILWMKDL NRLYHRTSKI K
//
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