ID B1R7P6_CLOPF Unreviewed; 497 AA.
AC B1R7P6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=malQ {ECO:0000313|EMBL:EDT23723.1};
GN ORFNames=AC1_2905 {ECO:0000313|EMBL:EDT23723.1};
OS Clostridium perfringens B str. ATCC 3626.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT23723.1, ECO:0000313|Proteomes:UP000004342};
RN [1] {ECO:0000313|EMBL:EDT23723.1, ECO:0000313|Proteomes:UP000004342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens B str. ATCC 3626.";
RL Submitted (JUL-2007) 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:EDT23723.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABDV01000013; EDT23723.1; -; Genomic_DNA.
DR RefSeq; WP_003457856.1; NZ_ABDV01000013.1.
DR AlphaFoldDB; B1R7P6; -.
DR Proteomes; UP000004342; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW ECO:0000313|EMBL:EDT23723.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EDT23723.1}.
FT COILED 112..139
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 497 AA; 58035 MW; 7DB6C6DBF23B8884 CRC64;
MRRASGIIMH IASLPGKYGI GTFGKEAFEF VDFLKKAGQG CWQILPLGPT SYGDSPYQSF
SAFAGNPYFI DFDILNKEGL LDKKDYQGIN FGNDPEKIDY ALLFDKKMRV LRVAYEKSLD
ENKEEIEKFR EENKLWLEDY ALYMAIKNEN ELVSWQEWDE KLRLRDKKTL EEYKVKLEKE
INYWVFLQYH FFKQWNKLKE YANSFGIKII GDMPIYVAED SADVWANPKA FLLDENNIPK
KVAGCPPDAF SETGQLWGNP IYDWSYMDDT GYSWWIDRVR ESFKLYDILR IDHFRGFEAY
WQIPYGDETA VNGEWVKGPG IKLFNAIKEE LGGVNVIAED LGYLTQEVID FRNETGFPGM
KVLQFAFDSR EESDYLPHNY PVNSIAYTGT HDNDTFRGWF EVTGNREDVE YSKKYLKLTE
EEGYNWGFIR GVWSSVSHTA IALMQDFLNL GNEARINYPS TLGGNWQWRV KYDALTDELA
EKIYDITKLY GRVNINE
//
