GLGB_PROM1
ID GLGB_PROM1 Reviewed; 755 AA.
AC A2C142;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, 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=NATL1_06401;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
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; CP000553; ABM75202.1; -; Genomic_DNA.
DR RefSeq; WP_011823366.1; NC_008819.1.
DR AlphaFoldDB; A2C142; -.
DR SMR; A2C142; -.
DR STRING; 167555.NATL1_06401; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABM75202; ABM75202; NATL1_06401.
DR KEGG; pme:NATL1_06401; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_3; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002592; 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..755
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000044989"
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 755 AA; 87953 MW; 260074A43CB53AF5 CRC64;
MTVSILLDSL KDDGQRLSEC RHESPFSILG PQPFKDKWII RIWMPEASEV ELITQQTKIK
LQNPNHEWIF EGVLEKDPGN DYQIKVNRGG IEHVQHDPWS FRKEWMGEID RHLFAEGNHH
HIWRKMGAHL TEINKKQGVM FCLWAPHAKS VSVIGDLNSW DGRHHPMQKR LGGIWELFIP
GLSEGDLYKY EIRTEKGHCY EKADPYGFQH EVRPAKSSVI SKIDSFQWND QSWISNRDNR
DPLEQPISVY EMHLGSWMHA SSDDPFINSN GEHRAPVPAA DMKPGSRLLT YKELANKVIP
YVKERGFTHI ELMPISEHPF DGSWGYQVTG WYAPTSRFGS PDEFRAFVDS CHKEGIGIIL
DWVPGHFPKD QHGLAYFDGS HLYEHSDPRV GEHKEWGTLI FNYSRNEVRN FLVANLIFWF
DQFHIDGIRV DAVASMLYKD YLRPEGEWIP NEDGGNENFE AVRFLQQANH VLFQHFPGAL
SIAEESTTWS GVTKPTDMDG LGFNLKWNMG WMHDMLDYFE IDPWFRQFNQ NNITFSICYN
FTENFMLALS HDEVVHGKSH LLHKMPGDDW QKYANTRALL AYMWTHPGKK TIFMGMEFGQ
RQEWNVWDDL QWDLLNYEPH KGIQKLVDDL NNLYKREPAL WRNDFDEYGF QWIDCDDNKN
SVISFMRREK TDGEWLVIVA NFTPQNHSNY RIGVPVDGFY EEIFNTDASQ YGGSNLGNMG
GKSTDLYNIH GYENSIDLCL PPLSVLVLKH KSKKN
