GLGB_BURCM
ID GLGB_BURCM Reviewed; 733 AA.
AC Q0B3Y4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=Bamb_5592;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000255|HAMAP-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; CP000442; ABI91139.1; -; Genomic_DNA.
DR RefSeq; WP_011660498.1; NZ_CP009800.1.
DR AlphaFoldDB; Q0B3Y4; -.
DR SMR; Q0B3Y4; -.
DR STRING; 339670.Bamb_5592; -.
DR EnsemblBacteria; ABI91139; ABI91139; Bamb_5592.
DR GeneID; 44696145; -.
DR KEGG; bam:Bamb_5592; -.
DR PATRIC; fig|339670.21.peg.6517; -.
DR eggNOG; COG0296; Bacteria.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000662; Chromosome 3.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
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 PANTHER; PTHR43651; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..733
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000044970"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 467
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 733 AA; 81191 MW; 9A0C19F09869CEC2 CRC64;
MTDMLFDRTD IDALLAGRHP DPFACLGPHT DAGRVVVRAL LPGAQRVRAV TPDGDELGAL
ACVDDAGCFA GTLAHDGRYR LAIDWPDTRQ ITDDAYAFGT LLDEAALARF AAGDPAAVLD
CLGATPTRVD GVDGVRFAVW APNAQRVSVV GDFNMWDGRR HPMRLRRPWG VWELFVPGIG
AGEHYKYELR AADGHVLPHK ADPCARATEA PPRTASVVAD TAALDAFAWH DDGWLHARPP
ADQRFRMPWS IYEVHAESWQ RVPEDMDRSA NWDELAERLI PYVRGMGFTH VEFMPISEYP
FGGSWGYQPL AQFAPSARFG PVDGFARFVD RAHAAGIGVI VDWVPAHFPN DAHGLAQFDG
SALYEHADPR EGMHPDWNTC VFNLGRNEVS AFLIASALAW ARRYHVDGIR VDAVASMLYR
DYSRNEGEWV PNIHGGRENL ESVAFLRALN DTLHGTLAPP GVVTFAEEST AWPGVTASTG
DGGLGFDFKW NMGWMHDTLS YVREDPIHRR YHHDRMTFGL VYAFSERFVL PLSHDEVVHG
KGSLAVKMPG DAWQRLATLR AYFGFMWAHP GKKLLFMGSE FAQWAEFAHD ATPHWDLLDA
PAHRGVQRLV RDLNRTYAAE PALHALDCHA SGFFWLIGDD RDNSVFAFAR RDDSGRLVVA
ICNFTPVPRP GYRIGLPAPG HWRELMNTDA AVYGGTNAGN DGAVWTEDVP SHGQSWSATL
RLPPLATLWL SPA
