ID H0TEB1_9BRAD Unreviewed; 633 AA.
AC H0TEB1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=BRAS3843_1150017 {ECO:0000313|EMBL:CCE04799.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE04799.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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.
CC {ECO:0000256|ARBA:ARBA00002953}.
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:0000256|ARBA:ARBA00000826};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCE04799.1}.
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DR EMBL; CAFK01000019; CCE04799.1; -; Genomic_DNA.
DR RefSeq; WP_008967323.1; NZ_CAFK01000019.1.
DR AlphaFoldDB; H0TEB1; -.
DR OrthoDB; 9800174at2; -.
DR Proteomes; UP000002686; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
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:InterPro.
DR CDD; cd11325; AmyAc_GTHase; 1.
DR CDD; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR PIRSF; PIRSF000463; GlgB; 3.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000313|EMBL:CCE04799.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002686};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCE04799.1}.
FT DOMAIN 131..523
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 633 AA; 69676 MW; 54A3D9CF6DA9CB72 CRC64;
MSLRQLHLLQ APMGGTLVPG GATFRVFAPH AKAVYVSGDF NNWVQDDSCR LSPIGAGYWA
VFIPGLKDGD PYMYFIEGAG SSGYKRDPHA RLLTVEPPFP SCHSVLRNPH AFPWHEVDFK
PPAFNELVVY QLHVGTFDMK AGNPDGCFFD VIERVPHLAS LGVNAIELLP IQEFPTTFSM
GYNGTDLFSP ETEYGEADAA KLAAYVNRTN EILVKAGQAP YESAELLRHC DDQLRALVDV
CHVHGIGVLF DVVYNHAGGG FDENSIWFFD RQPYGNANDS LYFTDQGWAG GQVFAYWNAD
IRQFLVDNAL SFYRDYRVDG LRFDEVSVMD RFGGWATCQQ LTSALRAEKP EAIQVAEYWP
VNPWVVKDHA EGGAGFDATW SDRLRESVRA AVGAAAAGRN APVPMQAIAA AIADDSLGRR
ARAVHSIENH DIVYAGREPR IARLADSLDS RSWYARSRSR VATGLLLTAP GIPMLFMGQE
LLEEKPWSDT PHPETSIGWA RLDGGDTVTL DFLRFTRELI DLRHKLKALS GEGSGIVHVH
DGNRVLAFER WAAGSDDAVM VVVSLNETAW TDYAIGFPAG GAWHLAFSSE DYEEGAHPAE
HREVMADGPP MHGRPCSAHL TIPANGLLVF ARG
//
