GLGB_THIDA
ID GLGB_THIDA Reviewed; 740 AA.
AC Q3SH78;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 118.
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=Tbd_2058;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98011.1; -; Genomic_DNA.
DR RefSeq; WP_011312570.1; NC_007404.1.
DR AlphaFoldDB; Q3SH78; -.
DR SMR; Q3SH78; -.
DR STRING; 292415.Tbd_2058; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAZ98011; AAZ98011; Tbd_2058.
DR KEGG; tbd:Tbd_2058; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_4; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008291; 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; -; 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; 1.
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..740
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260711"
FT ACT_SITE 419
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 472
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 740 AA; 84263 MW; 0DACE2E56940ABF5 CRC64;
MRKLVEATQA GSEASVALAP SAPIQRLQAG LHHDPFEVLG VHVQPDGSKL VRAFLPAAEA
VEVAGVRMTR VPGTDCFERL LPPGTALEAH PLLTWQDKRS GAWQRLRSPY SFAPQLGEMD
LYLFGEGRHF EIWKVLGARV KTVDGVTGCL FAVWAPAVLR VSVVGDFNDW DGRRHPMRCR
GVSGVWELFI PGLEAGHAYK YEILGRHGER VTKTDPYARQ MFLRPETTSR VPDERPYAWG
DAEWLAARTR FDWQHRPMSV YEVHPGSWRR RADGSFYSWR ELTAELIPYV RDLGYTHIEL
LPVAEHPFDA SWGYQVSGYY AATARFGSPD DLRAFVDACH QAGLGVLLDW VPGHFPKDDF
ALARFTGEPL YEHADPRRGE HQDWGTLVFD FGRNEVRNFL VANALYWLEE FHIDGLRVDA
VASMLYLDYS RRHGEWLPNQ HGGRENLEAI HFLHEVNAEV HARFPGAITI AEESTAWPAV
SRPIELGGLG FSMKWNMGWM NDTLDYIEKE PVYRKYQHNQ LTFSQMYAWS ENFVLPLSHD
EVVHLKKSLL DKMPGDRWQR FANLRLLYAW QYAHPGKKLL FMGGEFGQWN EWREAGQLDW
VLLGFPEHDG IRALLRDLNR LYRDEAALHF WDFDPRGFRW IDCHDADQSV LSLVREGPDG
APPIVVLLNF TPVPRHGYRI GVPRAGAWCE VLNSDSMYYG GSNLGNGKPL YPAAVPWMGF
GQSIEVTLPP LGAIFLKPCP
