GLGB2_STRAW
ID GLGB2_STRAW Reviewed; 592 AA.
AC Q825Q8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE 2 {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB2 {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=SAV_7399;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC75110.1; -; Genomic_DNA.
DR AlphaFoldDB; Q825Q8; -.
DR SMR; Q825Q8; -.
DR STRING; 227882.SAV_7399; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q825Q8; -.
DR EnsemblBacteria; BAC75110; BAC75110; SAVERM_7399.
DR KEGG; sma:SAVERM_7399; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_11; -.
DR OMA; DKRRQPI; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000428; 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 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 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..592
FT /note="1,4-alpha-glucan branching enzyme GlgB 2"
FT /id="PRO_0000188748"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 327
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 592 AA; 66806 MW; 3A7355E0360BCC51 CRC64;
MMTHAGVLGT RFTVWAPNAR GVRVCGNFCR WDGAAFPMRS LGSSGVWELF VPGIGEGELY
KFEITRPDGT HTVRADPMAR RAEVPPATAS IVTESSYAWA DGAWMAARGE RPVHESPFSV
YEVHLPSWRP GLTYRQLAEQ LPAYVADLGF THVELLPVAE HPFGGSWGYQ VTGFYAPTAR
LGTPDDFKYL VDALHRAGVG VLMDWVPAHF PRDDWALAEF DGRPLYEPED PQRAAHPDWG
TLEFDYGRKE VRNFLVANAV YWCEEFHIDG LRVDAVASML YLDYSREEGQ WSPNEFGGRD
NPDAVAFLQE MNATLYRRVP GVITIAEEST AWDGVTRATH DNGLGFGLKW NMGWMHDSLG
YVQHEPVHRK YHHHEMTFSM VYAYSENYVL PISHDEVVHG KQALVSKMPG DWWQRRANHR
AYLGFMWAHP GKQLLFMGQE FAQGAEWSPE HGPEWWLLDD EYHSAGDHRG MRDLVRDLNT
LYRAEPALWE RDTDPSGFAW VVGDAAEDNV FAFLRHAADG TPLLAVSNFS PVVRHDYRLG
VPDDIPAWQE ALNTDAARYG GSDLICPDPV KPESGEIRLT LPPLATVWLR PA
