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Database: UniProt
Entry: G0IR10_BORAP
LinkDB: G0IR10_BORAP
Original site: G0IR10_BORAP 
ID   G0IR10_BORAP            Unreviewed;       506 AA.
AC   G0IR10;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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:AEL69396.1};
GN   OrderedLocusNames=BafPKo_0163 {ECO:0000313|EMBL:AEL69396.1};
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=390236 {ECO:0000313|EMBL:AEL69396.1, ECO:0000313|Proteomes:UP000005216};
RN   [1] {ECO:0000313|EMBL:AEL69396.1, ECO:0000313|Proteomes:UP000005216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo {ECO:0000313|EMBL:AEL69396.1,
RC   ECO:0000313|Proteomes:UP000005216};
RX   PubMed=22123755; DOI=10.1128/JB.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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; CP002933; AEL69396.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0IR10; -.
DR   STRING; 29518.BLA32_03480; -.
DR   KEGG; bafz:BafPKo_0163; -.
DR   PATRIC; fig|390236.22.peg.161; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_014132_1_0_12; -.
DR   Proteomes; UP000005216; 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   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AEL69396.1}.
SQ   SEQUENCE   506 AA;  59590 MW;  EB8C74D24690197F CRC64;
     MKYEKIRINL NLKRKSGILL NISSLPSKYG IGDLGKGAYK FIDFLFASSQ SYWQMFAYSP
     IDFTRSPPYS IFSAFAGNVY YIDLEALDKF IDSDLNILKE NESRHSDFKK LSFKDKFLKE
     AALNFINRAS VDEVRSFEKF KKKSYYWLLD FASFVAFKEY SLKESKDAFN VLFDRGILKR
     NEQDLFKLRN ILSKEIKVQE VLQYFFFSQF QALKRYANGK GIELVMNVPL FIAYDSADVW
     AHQKYFKLRF DASKDKVAGI SPDYFLEQEQ AWDSPAYSWN VLKKVNYEWW AKRIEILKKY
     VDVIKIDHFR GFVSTWEVSA GETYAFNGLW VKSPGRDFFN FILNEIKDLK IWVEDFENDL
     EDVSRLRDFF NFPGMRIMKL AFDFDSGNQN LPHNYIKNCI VYTGISDNDT ILEFINSLDD
     LHKKYIFDYL NTNEDFVVWD MIRSAMSSVS DNVIIPMQDY ISLGDKFRAN VPKNTLDNWI
     FRLLESDLDT TLSKNISFIT RLYGRA
//
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