GLGB_ACTP2
ID GLGB_ACTP2 Reviewed; 777 AA.
AC A3MZ64;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=APL_0346;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73450.1; -; Genomic_DNA.
DR RefSeq; WP_009874649.1; NC_009053.1.
DR AlphaFoldDB; A3MZ64; -.
DR SMR; A3MZ64; -.
DR STRING; 416269.APL_0346; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; A3MZ64; -.
DR EnsemblBacteria; ABN73450; ABN73450; APL_0346.
DR KEGG; apl:APL_0346; -.
DR PATRIC; fig|416269.6.peg.355; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001432; 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; -; 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; Reference proteome; Transferase.
FT CHAIN 1..777
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_1000131804"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 461
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 777 AA; 89300 MW; 8420D9345EBD9E02 CRC64;
MKTYTYSKQD LSFIEQLSQA YCKDPFSYLG LHQAGDVSVI RVFLPEATTV KILSAVGQIL
SEALKIDDSG LFVAQLAQQY SSLNYRLRVG YSLAEIDLED PYRFTSSLLP MDNWLLAEGT
HLRPYEILGA HLKTQEGVSG VHFSVWAPNA RRVSVVGDFN YWDGRVNPMR FHAESGIWDI
FLPNVEKGAL YKFEILDSNG NIRLKSDPYA FASQFRPDTA SVVTGLPEKI EVDAKLRHAN
DPDQPISIYE VHLGSWRRHL ENNYWLNYEE IANELIPYVK DMGFTHIELL PITEYPFDGS
WGYQPTGLYS PTSRFGSPED LRTLIRKAHE AGINVILDWV VGHFPTDSHG LTEFDGSHLY
EHQDPREGYH QDWNTLIFNY GRHEVFNYLS SNALYWTERF GIDGLRVDAV SSMIYRDYSR
KDGEWIPNQY GGRENLEALD FLRRTNRMLK KEGHGAVVIA EESTSFAGIT HSPEENGVGF
DYKWNMGWMN DTLRYMSLDP IYRQYHHDWM TFGMMYQYSE KFVLPLSHDE VVHGKCSILG
KMSGDCWQKF ANLRAYYGYM WGYPGKKLLF MGNEFAQGRE WNYNESLDWF LLGEQGGGWH
KGVLNWVRDL NRTYQKYPAL YQLDYDPAGF EWLVVDDWQQ SVFAFERKAK NGESVIVVSN
FTPVVRHNYR IGVRQDGTYT EILNSDAAYY EGSNVGNYGE IECEAIESHG KPFSIELSIP
PLSTIFIACQ PKPKEAVEAE QDIVKMAEVA MQKALKPTKK TVSVKAKAHK KAHKNKK
