ID B1BQJ5_CLOPF Unreviewed; 497 AA.
AC B1BQJ5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:EDT16047.1};
GN ORFNames=AC3_2961 {ECO:0000313|EMBL:EDT16047.1};
OS Clostridium perfringens E str. JGS1987.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT16047.1, ECO:0000313|Proteomes:UP000005337};
RN [1] {ECO:0000313|EMBL:EDT16047.1, ECO:0000313|Proteomes:UP000005337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E str. JGS1987 {ECO:0000313|Proteomes:UP000005337};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens E str. JGS1987.";
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:EDT16047.1}.
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DR EMBL; ABDW01000005; EDT16047.1; -; Genomic_DNA.
DR RefSeq; WP_003462355.1; NZ_ABDW01000005.1.
DR AlphaFoldDB; B1BQJ5; -.
DR Proteomes; UP000005337; 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:EDT16047.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EDT16047.1}.
FT COILED 112..139
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 497 AA; 58181 MW; CC93C313A66508F7 CRC64;
MRRASGIIMH IASLPGKYGI GTFGKEAFEF VDFLKKAGQG YWQILPLGPT SYGDSPYQSF
SAFAGNPYFI DFDILNKEGL LDKKDYQGIN FGNDPEKIDY ALLFDKKMRV LRIAYEKSLD
KNKEEIEKFR EENKLWLEDY ALYMAIKNEN ELVSWQEWDE KLRLRDKKTL EEYKVKLEKE
INYWVFLQYH FFKQWNKLKE YANSFGIKII GDMPIYVAED SADVWANPKA FLLDENNIPK
KVAGCPPDAF SETGQLWGNP IYDWSYMDDT GYSWWIDRVR ESFKIYDILR IDHFRGFEAY
WQIPYGDETA VNGEWVKGPG IKLFNAIKEE LGEVNVIAED LGYLTQEVID FRNETGFPGM
KVLQFAFDSR EESDYLPHNY PVNSIAYTGT HDNDTFRGWF EVTGNREDVE YSKKYLKLTE
EEGYNWGFIR GVWSSVSHTA IALMQDFLNL GNEARINYPS TLGGNWQWRV KYDALTDELA
EKIYDITKLY GRVNINE
//