GLGB_OCEIH
ID GLGB_OCEIH Reviewed; 637 AA.
AC Q8CZE8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=OB0406;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(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; BA000028; BAC12362.1; -; Genomic_DNA.
DR RefSeq; WP_011064812.1; NC_004193.1.
DR AlphaFoldDB; Q8CZE8; -.
DR SMR; Q8CZE8; -.
DR STRING; 221109.22776085; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; BAC12362; BAC12362; BAC12362.
DR KEGG; oih:OB0406; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_9; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR PhylomeDB; Q8CZE8; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000822; 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..637
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188722"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 361
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 637 AA; 74651 MW; 2A3165A2556A269D CRC64;
MYHISAEDIY LFHQGTNFES HQFLGCHEIN WKGKRGYRFA VWAPNALKVC VVGDFNNWEE
NSHPLEKFTD EGLWGGFIAD IPPATSYKYH ICSSEDTSIL KADPFATQAE RRPKTASVIP
AANGYQWSDD QWIEQRNTYD PYSSPISIYE VHLGTWKKTL KKQFLSYREL ATQLIPYVKS
LGYTHIELLP INEHPFDRSW GYQITGYFAV TSRYGNPSDF KYFIDQCHQH QIGVILDWVP
GHFCKDDFGL RQFDGAPLYE YRDPKKSEKK SWGTLAFDYG RPEVQSFLIS NAIYWLKEFH
IDGLRVDAVA SMLYLNFDRY DEEEKIYNTY GGEENLEAFA FLRKLNKVVF SYIPGALMMA
EDSSDLPLVT APVNKGGLGF NYKWNMGWMN DLLSFMEKES IHRKWHHNRL TFSFMYTYSE
NYLLPLSHDE VVHGKKSLLD KMPGDQWQQF ANLRLLYGYM YTHPGKKLVF MGGELAQYAE
WKDTEELDWH LLEYPLHKGI YHYIKNLNEL YQQHPELYEL DHLSEGFEWI DPHNIDQSVI
AFRRKANKPN QELIIICNFT PQVHFDYKIG VPESGRYKEI FNSDSVRFGG SGQINEGEHF
SFPEKWHGLS QHIKIKVPPL AISVFQIEVE RERLPRE