ID A1QYW1_BORT9 Unreviewed; 493 AA.
AC A1QYW1;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=BT0166 {ECO:0000313|EMBL:AAX17503.1};
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=314724 {ECO:0000313|EMBL:AAX17503.1, ECO:0000313|Proteomes:UP000001205};
RN [1] {ECO:0000313|Proteomes:UP000001205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135 {ECO:0000313|Proteomes:UP000001205};
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) 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}.
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DR EMBL; CP000049; AAX17503.1; -; Genomic_DNA.
DR RefSeq; WP_011772122.1; NZ_CP073176.1.
DR AlphaFoldDB; A1QYW1; -.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR KEGG; btu:BT0166; -.
DR eggNOG; COG1640; Bacteria.
DR HOGENOM; CLU_014132_1_0_12; -.
DR Proteomes; UP000001205; Chromosome.
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 ECO:0000313|EMBL:AAX17503.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AAX17503.1}.
SQ SEQUENCE 493 AA; 57361 MW; 18558B9A1C616F79 CRC64;
MKRKSGILLN ISSLPSKYGI GDLGRGAYKF IDFLADSSQG YWQILPYSPP SFLEFPYSSY
SAFAGNINYI DLNAIDRFID IDLGTFECLE DRYVDYDKLK AKEVILRNAA LNFLHRATID
EIHAFEKFKK SAAYWLLDFS SFVAFKEYYS KFQSSQAFNL LFSREILKRD AKALAKLRET
LEVEINIQQV LQYFFFSQFK ALKKYANNAG IKIVSDIPIF VSYDSADVWA HQKYFKLRFD
ASKDKVTGVP PDCLFSKKYL WGNAAYNWKA LRKDDYVWWI NRIDFLRKYV DIVRIDYFRG
FVSTWEVSAE ESLLFGGQWV KCPGKDFFKQ ILNEINDLEI WVEDLVKDRG DTFRLRDYFG
FPGTKMMQCA FDFDSANIYL PHNYIRNCVV YTGTHESNTI RGFINSVDNE HKKYIFDYFN
TSENAIVWDM IRGAMASVAN SVIIPMKDYL DLVADFSMNI SDAMLNNFRI LSGDLSDDLS
KKISDITKLY GRT
//
