GLGB_LACAC
ID GLGB_LACAC Reviewed; 638 AA.
AC Q5FL68;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=LBA0680;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42556.1; -; Genomic_DNA.
DR RefSeq; WP_011254224.1; NC_006814.3.
DR RefSeq; YP_193587.1; NC_006814.3.
DR AlphaFoldDB; Q5FL68; -.
DR SMR; Q5FL68; -.
DR STRING; 272621.LBA0680; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q5FL68; -.
DR EnsemblBacteria; AAV42556; AAV42556; LBA0680.
DR GeneID; 56942312; -.
DR KEGG; lac:LBA0680; -.
DR PATRIC; fig|272621.13.peg.650; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_9; -.
DR OMA; FGMKWMM; -.
DR BioCyc; LACI272621:G1G49-702-MON; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000006381; 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; 2.
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; 1.
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..638
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188711"
FT ACT_SITE 303
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 638 AA; 74582 MW; F66FC75355225AAC CRC64;
MVTIVEVKQH IKKFAAGNEL YLQEVLGCHY ENDIYTFRVW APNAQKVWLV GDFNDWDKSL
EMSQTLDGVW EIKTSLPKEG QLYKFLVKQA DGREVMKIDP MAFELEPRPG SAAVIVKLPN
KKWLDGAWMG RNKRSNHFAR PINIYEVHAS SWKRHTDGSL YTLKDLQKEL IPYVKEQGFN
YIEFLPLTAH PLDASWGYQT IGYYALERTY GTPRELQDFV EACHKENIGV LADWVPGHFC
INDDALAYYD GTPCYEFSEK WRAENKGWGA LNFDLGKPEV QSFLLSSALF WLEFYHLDGL
RVDAVSNMIY RDYDRSDGEW KTDKFGGNRN LEGIEFLQKL NRTIKGKHPE CLMIAEESSA
QVKITGRIED GGLGFDFKWN MGWMNDILRF YEMDPLFRKF NFNLATFSFM YRMSENFILP
LSHDEVVHGK RSLMNKMFGD RDKQFAQLRN LLTLQMTYPG KKLLFMGSEF GQYLEWRYND
GLDWAELKDE LNAKMKHFDQ DLNSFYLNEP ALWQLEQRED SVQIIDADNK DESVLSFIRQ
GKTRHDFLIV ILNFTPVDRK KITIGVPYAG KYCEVFNSAR KEYGGSWNQE KQNLKTQNNS
FKNFNYQVQL DIPGFSAVIL KPVDVHIKRR INRKTKTK
