ID A0AAN0ULE9_CORUL Unreviewed; 732 AA. AC A0AAN0ULE9; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685}; DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685}; DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685}; DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685}; GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685, GN ECO:0000313|EMBL:AEG81439.1}; GN ORFNames=CULC809_00903 {ECO:0000313|EMBL:AEG81439.1}; OS Corynebacterium ulcerans 809. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=945711 {ECO:0000313|EMBL:AEG81439.1, ECO:0000313|Proteomes:UP000008886}; RN [1] {ECO:0000313|EMBL:AEG81439.1, ECO:0000313|Proteomes:UP000008886} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=809 {ECO:0000313|EMBL:AEG81439.1, RC ECO:0000313|Proteomes:UP000008886}; RX PubMed=21801446; DOI=10.1186/1471-2164-12-383; RA Trost E., Al-Dilaimi A., Papavasiliou P., Schneider J., Viehoever P., RA Burkovski A., Soares S.C., Almeida S.S., Dorella F.A., Miyoshi A., RA Azevedo V., Schneider M.P., Silva A., Santos C.S., Santos L.S., RA Sabbadini P., Dias A.A., Hirata R.Jr., Mattos-Guaraldi A.L., Tauch A.; RT "Comparative analysis of two complete Corynebacterium ulcerans genomes and RT detection of candidate virulence factors."; RL BMC Genomics 12:383-383(2011). CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from CC growing alpha-1,4-glucan chains and the subsequent attachment of the CC oligosaccharide to the alpha-1,6 position. {ECO:0000256|HAMAP- CC Rule:MF_00685}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; CC Evidence={ECO:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP- CC Rule:MF_00685}; CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP- CC Rule:MF_00685}. 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; CP002790; AEG81439.1; -; Genomic_DNA. DR RefSeq; WP_014525627.1; NC_017317.1. DR GeneID; 75260096; -. DR Proteomes; UP000008886; Chromosome. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW. DR CDD; cd11322; AmyAc_Glg_BE; 1. DR CDD; cd02855; E_set_GBE_prok_N; 1. DR FunFam; 2.60.40.10:FF:000169; 1,4-alpha-glucan branching enzyme GlgB; 1. DR FunFam; 3.20.20.80:FF:000003; 1,4-alpha-glucan branching enzyme GlgB; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR HAMAP; MF_00685; GlgB; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR037439; Branching_enzy. DR InterPro; IPR006407; GlgB. DR InterPro; IPR054169; GlgB_N. DR InterPro; IPR044143; GlgB_N_E_set_prok. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR004193; Glyco_hydro_13_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR NCBIfam; TIGR01515; branching_enzym; 1. DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR Pfam; PF02922; CBM_48; 1. DR Pfam; PF22019; GlgB_N; 1. DR PIRSF; PIRSF000463; GlgB; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF81296; E set domains; 2. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_00685}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00685}. FT DOMAIN 225..611 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 409 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685" FT ACT_SITE 462 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685" SQ SEQUENCE 732 AA; 82624 MW; C3B75C02EE7EDC8B CRC64; MISSSDPVRI DDDILGRLRY CQFHDPHAVY GCHHIDDSHA VIRTRQLGAE AVTVTLTDGS THVLSPIGDD IFAASVDASL ATDYRLNVSW AGDTTLTTAD PYHFLPTLGE LDIHLIREGR HERLWDVLGA HVRTVSTELG DVTGTSFAVW APNATGVAVV GDFCGWNPNQ YPMRSLGDSG VWELFIPGIQ AGEVYKYAIH TREGHRIDKA DPLARHAEVA PATGSIVADS SYEWQDADWI AKRATRDHAA QPMSIYECHL GSWRENRTYK ELASELVDYV SSLGYTHVEF LPVAEHPFGG SWGYQVSGYY APTSRWGNPD ELRMLIDAFH RAGIGVIMDW VPAHFPKDSF ALGRFDGQPL YEHPDWRRGE QKDWGTYVFD FGRNEVRNFL VANALYWIDE FHVDGLRVDA VASMLYLDYS REAGEWLPNI YGGRENLEAV QFLQEMNATV HKTFPGVLTI AEESTSWPGV TTPTDHNGLG FSMKWNMGWM NDTLEYFSLD PIHRSYHHNE ITFSMVYAYS ERFVLPFSHD EVVHGKGSLW TRMPGDAWNK ASGLRTLYAY MYAHPGKKLL FQGQEFGQVM EWSEGRSLDW DNLVGWEGEY HEGIIKLIRD LNVVYQDNPA LYTQDNGPEG FSWSKSNDAD NNVLSFIRYG SAGEKILAVF NFGGSSQPHY KLGVPEGGRW ECILNTDAGV YEGANNLLEH TITAWDTEWD GYEHSLTVHI PAMSGQFYRW IG //