GLGB_BIFLO
ID GLGB_BIFLO Reviewed; 737 AA.
AC Q8G5L0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=BL0999;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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}.
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DR EMBL; AE014295; AAN24807.1; -; Genomic_DNA.
DR RefSeq; NP_696171.1; NC_004307.2.
DR AlphaFoldDB; Q8G5L0; -.
DR SMR; Q8G5L0; -.
DR STRING; 206672.BL0999; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q8G5L0; -.
DR EnsemblBacteria; AAN24807; AAN24807; BL0999.
DR KEGG; blo:BL0999; -.
DR PATRIC; fig|206672.9.peg.702; -.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; Q8G5L0; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000439; Chromosome.
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; -; 2.
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; Reference proteome; Transferase.
FT CHAIN 1..737
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188684"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 471
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 737 AA; 83051 MW; 035A1580871A21F9 CRC64;
MPVAQGDLDA TSNAEFYNPH GVLGGHLGIG KHADTATIRV LRPLAKSVTI LTQDGEYPMT
HEYNGVFVVT VPASGTKKQP TIPDYRVRTE WESGAVLIED DPYRYMPTVG DMDTYLFGEG
RHEKLWETLG AHVLRYDDPM GGADGTPGEQ VVGTAFSVWA PNAHAVRVVG NFNAWDGRRH
AMRELGSSGV WEIFIPGIGA GETYKFQILN ANYTWEMKAD PMERQHEVPP STASIVTEST
YKWNDDAWMQ HRRTTNPHDG PVSIYEVHAG SWKQGLTYRD LAKQLVDYVK QEGFTHVEFM
PLAQHPFSGS WGYQVTGYYA VDSRLGSPDD FRYLVDQFHQ AGIGVIMDWV PAHFPKDAFA
LGRFDGTPLY EDPDPLRGEH PEWGTYVFNF GRREVRNFLV ANALFWLEDL HVDALRVDAV
SSMLYLDYSR EPGHWRPNIY GGRENLEAID FLKEATATAY KNNPGVMVIA EESTAWPGIT
APTSAGGIGF GMKWNMGWMH DTLEYLHEEP INRKWHHNEI TFSMVYAYSE HYVLPISHDE
VVYGKGSLYG KMPGDDWQKL AGVRSMFAYQ WAHPGKKLSF MGNELAQWGE WDHDASIDWD
CLNWQEHRQV QTMVADLNAF YKAHPALWSQ DFDPAGFQWL TSDDADHNTL SFLRIGTKGE
TLAVVVNFSG EAWSDYQVAL PTGGKWTEVF TTDDAKYGGS DIHNGTFEAV EGEYHSRPFS
AKITVPALGV VFLKPED
