GLGB_STRMU
ID GLGB_STRMU Reviewed; 628 AA.
AC Q8DT52;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=SMU_1539;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59189.1; -; Genomic_DNA.
DR RefSeq; NP_721883.1; NC_004350.2.
DR RefSeq; WP_002262951.1; NC_004350.2.
DR AlphaFoldDB; Q8DT52; -.
DR SMR; Q8DT52; -.
DR STRING; 210007.SMU_1539; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q8DT52; -.
DR EnsemblBacteria; AAN59189; AAN59189; SMU_1539.
DR KEGG; smu:SMU_1539; -.
DR PATRIC; fig|210007.7.peg.1371; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_4_0_9; -.
DR OMA; FGMKWMM; -.
DR PhylomeDB; Q8DT52; -.
DR BRENDA; 2.4.1.18; 5941.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000002512; 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; 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..628
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188751"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 355
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 628 AA; 73968 MW; 795A2B117F5461F6 CRC64;
MNEREALRTF GTGENFHAQH YFGFHETEKN GVKGYIFRVW APNAEDLHLI GDFTGWFDNP
LQMDKNEAGV WEVFTDLPKE GHIYKYLVKR QGGQIVEKMD PFAIYLEERP GTGSLIRTIP
EKKWKDGLWL GRRKRWGFFK RPVNIYEVHA GSWKQNEDGS PYSFEQLKDE LVPYLVKMNY
THVEFMPLMA HPLGMSWGYQ LMGFFAFEHT YGTPEQFQDF VEACHLNNIG VIVDWVPGHF
TQNDDALAYF DGTPTFEYQD HDRAHNYRWG ALNFDLGKNQ VQSFLISSAK FWIDFYHIDG
IRVDAVSNML YLDYDEGPWQ PNIEGNNRNL EGYYFLQRLN TVLKLAHPDV MMIAEESTAT
TKITGRREEG GLGFDYKWNM GWMNDILKFY EEDPIYRKYD FNLVTFSFMY LFSENFILPF
SHDEVVHGKK SLMHKMWGDR YNQFAGLRNL YTYQICHPGK KLLFMGSEFG QFLEWKYDHA
LEWTNLEEED GLNLKMQDFT SQLNQFYKDH KVLWQLDTSY DGLEIIDADN VDESVLSFIR
KNEKGDLLVC VFNMVPVERK GFTIGVPVAG IYEEVWNTEL EEFGGVWKEH NMTVKTQKNL
WKEYENTLSF TLPALGASIW KIKRRLRK
