GLGB_RHIRD
ID GLGB_RHIRD Reviewed; 734 AA.
AC P52979;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB;
DE EC=2.4.1.18;
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase;
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme;
DE AltName: Full=Glycogen branching enzyme;
DE Short=BE;
GN Name=glgB;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A348;
RX PubMed=9851999; DOI=10.1128/jb.180.24.6557-6564.1998;
RA Ugalde J.E., Lepek V., Uttaro A.D., Estrella J., Iglesias A., Ugalde R.A.;
RT "Gene organization and transcription analysis of the Agrobacterium
RT tumefaciens glycogen (glg) operon: two transcripts for the single
RT phosphoglucomutase gene.";
RL J. Bacteriol. 180:6557-6564(1998).
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:0000250}.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AF033856; AAD03472.1; -; Genomic_DNA.
DR AlphaFoldDB; P52979; -.
DR SMR; P52979; -.
DR STRING; 1082932.ATCR1_20073; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR eggNOG; COG0296; Bacteria.
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; -; 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..734
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188671"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 470
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 734 AA; 83623 MW; 70A3CD35A77F31E6 CRC64;
MKKPLNSAEE KKTGDITKAE IEAIKSGLHS NPFQIIPLHE TPEGFSARCF IPGAEEVSVL
TLDGNFVGEL KQIDPDGFFE GRIDLSKRQP VRYRACRDDA EWAVTDPYSF GPVLGPMDDY
FVREGSICGY STGWARIPLK LEGVEGFHFA VWAPNGRRVS VVGDFNNWDG RRHVMRFRKD
TGIWEIFAPD VYACAYKFEI LGANGELLPL KADPYARRGE LRPKNASVTA PELTQKWEDQ
AHREHWAQVD QRRQPISIYE VHAGSWQRSE DGTFLSWDEL EAQLIPYCTD MGFTHIEFLP
ITEHPYDPSW GYQTTGLYAP TARFGDPEGF ARFVNGAHKV GIGVLLDWVP AHFPTDEHGL
RWFDGTALYE HADPRQGFHP DWNTAIYNFG RIEVMSYLIN NALYWAEKFH LDGLRVDAVA
SMLYLDYSRK EGEWIPNEYG GRENLESVRF LQKMNSLVYG THPGVMTIAE ESTSWPKVSQ
PVHEGGLGFG FKWNMGFMHD TLSYFSREPV HRKFHHQELT FGLLYAFTEN FVLPLSHDEV
VHGKGSLIAK MSGDDWQKFA NLRSYYGFMW GYPGKKLLFM GQEFAQWSEW SEKGSLDWNL
RQYPMHEGMR RLVRDLNLTY RSKAALHARD CEPDGFRWLV VDDHENSVFA WLRTAPGEKP
VAVICNLTPV YRENYYVPLG VAGRWREILN TDAEIYGGSG KGNGGRVQAV DAGGEIGAML
VLPPLATIML EPEN