GLGB_HYDCU
ID GLGB_HYDCU Reviewed; 726 AA.
AC Q31IB6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=Tcr_0511;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(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; CP000109; ABB41107.1; -; Genomic_DNA.
DR RefSeq; WP_011369932.1; NC_007520.2.
DR AlphaFoldDB; Q31IB6; -.
DR SMR; Q31IB6; -.
DR STRING; 317025.Tcr_0511; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q31IB6; -.
DR EnsemblBacteria; ABB41107; ABB41107; Tcr_0511.
DR KEGG; tcx:Tcr_0511; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
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; Transferase.
FT CHAIN 1..726
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000260712"
FT ACT_SITE 407
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 460
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 726 AA; 84006 MW; C935A8F3EF9889BC CRC64;
MMNQTVTEEA VRRLAEGTHH DPFQILGCHA VGKKWEVRVW LPTAESASVE GWHALTRVEG
TSLFIASLTE KQKKALPLHF KVNWVEANGS EHTVVSPYTF LPQLGELDLH LYAEGRHWHV
YDVLGAQVKE VDNISGVQFS VWAPAASRVS VVGDFNGWNG LRHPMRTNGQ SGVWELFIPG
MVSGDIYKFE IRNYQTDQLL VKTDPYAKAM EFRPQTGSIV YDSTFQWQDR DWLAARAHFD
WQASPINIYE VHLGSWQRDH DGFFLNYKEI AQRLVEYVKW MGYTHIELLP ISEHPLDESW
GYQTTGYFSP TSRFGSPDDF RYFVNYCHEN GIGVFLDWVP AHFPKDEFAL ARFDGTALYE
HEDPRRGEHQ DWGTYIFNYG RNEVRNFLIA NALYWLKELH IDGLRVDAVA SMLYLDYSRK
DGDWLPNQYG GRENIEAIEF LKTLNAEVHA QCPGALMMAE ESTSWPMVSR PTWMGGLGFS
MKWNMGWMND TLDFFQQDPI YRPYHHNQLT FSQMYAYSEN FILPLSHDEV VHMKHALVSK
MPGDTWQKMA NMRLLMGYQT LNPGKKLLFM GGEFAQWQEW SESRGLDWYL CEQPANRGVQ
MLVRDLNLLY QTSPALYCHD FDQEGFEWID CHDYEQSVLS FVRISEKESL ICVFNFTPVP
RYDYRIGLPE TGIYEEVLNS DSELYGGGNV GNSGQLTTED QRWMNRPCST TLVLPPLAVV
VLRKKS
