ID O51188_BORBU Unreviewed; 506 AA. AC O51188; DT 01-JUN-1998, integrated into UniProtKB/TrEMBL. DT 01-JUN-1998, sequence version 1. DT 02-SEP-2026, entry version 134. 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:AAC66547.1}; GN OrderedLocusNames=BB_0166 {ECO:0000313|EMBL:AAC66547.1}; OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OS (Borrelia burgdorferi). OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales; OC Borreliaceae; Borreliella. OX NCBI_TaxID=224326 {ECO:0000313|EMBL:AAC66547.1, ECO:0000313|Proteomes:UP000001807}; RN [1] {ECO:0000313|EMBL:AAC66547.1, ECO:0000313|Proteomes:UP000001807} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31 RC {ECO:0000313|Proteomes:UP000001807}; RX PubMed=9403685; DOI=10.1038/37551; RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R., RA White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B., RA Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R., RA Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D., RA Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P., RA Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K., RA Hatch B., Smith H.O., Venter J.C.; RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi."; RL Nature 390:580-586(1997). 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 --------------------------------------------------------------------------- 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; AE000783; AAC66547.1; -; Genomic_DNA. DR PIR; F70120; F70120. DR RefSeq; WP_010889696.1; NC_001318.1. DR AlphaFoldDB; O51188; -. DR STRING; 224326.BB_0166; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR PaxDb; 224326-BB_0166; -. DR EnsemblBacteria; AAC66547; AAC66547; BB_0166. DR GeneID; 46847402; -. DR KEGG; bbu:BB_0166; -. DR PATRIC; fig|224326.49.peg.563; -. DR HOGENOM; CLU_014132_1_0_12; -. DR OrthoDB; 9811841at2; -. DR BRENDA; 2.4.1.25; 902. DR Proteomes; UP000001807; Chromosome. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR003385; Glyco_hydro_77. DR NCBIfam; TIGR00217; malQ; 1. DR NCBIfam; NF011080; PRK14508.1-3; 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|ARBA:ARBA00023277, KW ECO:0000256|RuleBase:RU361207}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|RuleBase:RU361207}; KW Reference proteome {ECO:0000313|Proteomes:UP000001807}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361207}. SQ SEQUENCE 506 AA; 59392 MW; ECD83CCAFBF66135 CRC64; MKYKKTRINL NLKRKSGILL NISSLPSKYG IGDLGKGAYK FIDFLFASSQ SYWQMFAYSP IDFTRSPPYS IFSAFAGNVY YIDLEALDKF IDSDLSLLKE NETRYSDLKK ISFKDKFLKE AALNFINRAS ADEVRSFEKF KKKSSYWLLD FASFVAFKEY FFKESKNAFN VLFDRGILKR NEKDLFKLRN ILSKEIKVQE VLQYFFFSQF QALKRYANDK GIELIMNVPF FIAYDSADVW AYQKYFKLRF DASKDKIAGI SPDYFLEQEQ AWDSAAYSWN VLKKFKYEWW AKRIGVLRKY ADIIKIDHFR GFVSTWEVSA GESYAFNGLW VKSPGRDFFN FILNEIKDLK IWVEDFQNDL EDVSRLRDFF NFPGMKIMNL AFDFDSSNQN LPHNYIKNCI VYTGSGDNDT IREFINSLDD LHKKYIFDYL NTNENFVVWD MIRSAMGSVS DNVIVSMQDY INLGDKFSAN IPKSTLDNCI FRLLESDLDA TLSQNISFIT RLYGRA //