GLGB_PROM4
ID GLGB_PROM4 Reviewed; 759 AA.
AC A9BAY7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=P9211_10681;
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=93059;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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; CP000878; ABX08999.1; -; Genomic_DNA.
DR RefSeq; WP_012195620.1; NC_009976.1.
DR AlphaFoldDB; A9BAY7; -.
DR SMR; A9BAY7; -.
DR STRING; 93059.P9211_10681; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABX08999; ABX08999; P9211_10681.
DR KEGG; pmj:P9211_10681; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000788; 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..759
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000147760"
FT ACT_SITE 431
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 484
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 759 AA; 87953 MW; 6DD5F46C9793B497 CRC64;
MTTSFVSDWM AQEGQKLSDC KHDDPFSVLG IQPFQGKWIA RIWMPEAEEV ELLINGSLIP
LTPPNHPWIF EALLDENPGS NYQVKVHRGG IKHQQYDPWS FRDEWMGEID THLFAEGNHH
HIWRRMGAHL SEMNGVCGVM FCLWAPNARS VSVIGEVNSW DGRHHPMQKR MGGIWELFIP
GLKEGALYKY EIRTQNGHCY EKSDPYGFEH EVRPAQSSKV SRIDNFKWSD QEWITKRDSS
NPLDQPISVY EMHLGSWLHA PSDEPFIEPN GNKRTAVPAA DLKPGTRLLT YPELKQKLIK
YVKERGFTHI ELMPISEHPF DGSWGYQATG WYAPTSRYGT PNEFRAFVDA CHSEGIGVIL
DWVPGHFPKD SHGLAFFDGS HLYEHSDPRI GEHKEWGTLI FNYSRNEVRN FLVANLVFWF
EQFHIDGIRV DAVASMLYKD YLRPEGQWIP NEDGGNENTE AVKFLQQANH VLFEHFPGAL
SIAEESTTWP GVTNPTDVGG LGFNLKWNMG WMHDMLDYFE VDPWFRQFHQ NNVTFSITYN
YTENFMLALS HDEVVHGKSH LLHKMPGDDW RKYANTRALL AYMWTHPGKK TIFMGMEFGQ
RKEWNVWDDL EWDLLGYQPH QGIQRLVDDL NVLYKSNPAL WRDDFNQYGF QWIDCKDNKN
SVISFMRRET LNNEWLIVVA NFTPESHPNY RVGVPLEGFY EEIFNTDSDK YGGSNTGNMG
GKASEKWSIH EYEDSIDLSL PPLSVLVFKY AQKKSPNEN