GLGB_YERP3
ID GLGB_YERP3 Reviewed; 727 AA.
AC A7FNX5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 97.
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};
GN OrderedLocusNames=YpsIP31758_4006;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS46943.1; -; Genomic_DNA.
DR RefSeq; WP_012105901.1; NC_009708.1.
DR AlphaFoldDB; A7FNX5; -.
DR SMR; A7FNX5; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABS46943; ABS46943; YpsIP31758_4006.
DR KEGG; ypi:YpsIP31758_4006; -.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; DKRRQPI; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002412; 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; Transferase.
FT CHAIN 1..727
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000061994"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 458
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 727 AA; 84168 MW; 7F9CF14D78012789 CRC64;
MPVLPDRQVI NQLISGHYGD PFSILGMHET SQGLQVCALL PDAQEVWLVE TENGRRIAQL
TLEDPRGFFI AQLTRRKKSF RYQFAVTWQE NPQIIDDPYR FGPLLQDIDS WLLAEGTHLR
PYERLGAHLM RLDGVPGVSF AVWAPNAQRV SVVGDFNFWD GRRHPMRLRR ENGIWELFLP
GIEAGQLYKF EIIDCHGQVR LKADPYAFEA QMRPETASLI SPLPDVVKSS AARQKANDLC
SPVSIYEVHL GSWRRHTDNN FWLSYRELAD QLVEYVKYMG FTHVELLPIN EHPFDGSWGY
QPLGLYAPTR RYGTPEDFKA FVAKFHQAGI NVILDWVPGH FPSDEHGLST FDGTALYEYA
DPREGYHQDW NTLIYNYGRN EVRNYLAGNA FYWMERFGID ALRIDAVASM IYRDYSRAEG
QWVPNYYGGR ENLEAIAFLR YTNKTIGVER PGSVTMAEES TDFPGVTLPP DIGGLGFNYK
WNMGWMHDTL NYMQCDPVHR KYHHNLMTFG MLYAYTENFI LPLSHDEVVH GKRSILDRMP
GDAWQKFANL RAYYAFMWAH PGKKLLFMGC EFAQGREWNF ETSLDWHLLD DENGWHSGVQ
RLVRDLNHCY RQYAPLYEWD YQPAGFEWLV VDDHENSVFA FLRRDAEGHE LIAISNFTPV
PRYHYRVGIP QGGHYREVLN SDSAFYCGSN LGNQGGIDSH HVRSHNHEHS LLLTLPPLAT
IYLLREN
