ID A0A0D7PHB8_9BRAD Unreviewed; 715 AA.
AC A0A0D7PHB8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN ORFNames=UP09_06130 {ECO:0000313|EMBL:KJC49679.1};
OS Bradyrhizobium sp. LTSP885.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1619232 {ECO:0000313|EMBL:KJC49679.1, ECO:0000313|Proteomes:UP000032343};
RN [1] {ECO:0000313|Proteomes:UP000032343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LTSP885 {ECO:0000313|Proteomes:UP000032343};
RX PubMed=25909973; DOI=10.1038/ismej.2015.54;
RA VanInsberghe D.S., Maas K.R., Cardenas E., Strachan C.R., Hallam S.J.,
RA Mohn W.;
RT "Non-symbiotic Bradyrhizobium ecotypes dominate North American forest
RT soils.";
RL ISME J. 9:2435-2441(2015).
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, ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00000826, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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:KJC49679.1}.
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DR EMBL; JYMT01000008; KJC49679.1; -; Genomic_DNA.
DR RefSeq; WP_044537192.1; NZ_JYMT01000008.1.
DR AlphaFoldDB; A0A0D7PHB8; -.
DR STRING; 1619232.UP09_06130; -.
DR PATRIC; fig|1619232.5.peg.7590; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000032343; Unassembled WGS sequence.
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; cd11322; AmyAc_Glg_BE; 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; 2.
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 NCBIfam; TIGR01515; branching_enzym; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000032343};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 241..595
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 398
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 451
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 715 AA; 80885 MW; 1E856591F7DDADBD CRC64;
MTKLPAEAYA IIEGRHADPF HYLGLHTEGD RSVVRAFLPD ASNVEAIGEH GETAPLTRIH
DAGLFAGPLP NGSTRYQLRA RFGDTIVELE DAYRFLPILS DFDLYLLGEG THQRIYDTLG
AHPMTLDGVD GVGFVVLAPN ARRVSVVGDF NFWDPRRHPM RVRGAGYWEL FIPRARVGDH
YKFDIVGSNG QHLALKSDPM AFATEVRPKT ASIVYDERTI PHPRPAPDGI NALRAPMSIY
EVHLGSWRRK GRNEWLTYRE LAEQLPAYAR DMGFTHVEFL PVSEHPFDGS WGYQPTGMFA
PTSRFGSPDD FSALVDACHR EGLAVLLDWV PGHFPDDPHA LGRFDGTALY EHANPLQGRH
LDWGTLIYNY GRTEVTNFLV SNALFWLERY GIDGLRVDAV ASMLYLDYSR PAGGWIPNKY
GGRENIEAID FLRRFNTELF ARFPQATTAA EESTAWPQVS RPVEFGGLGF GYKWNMGWMH
DTLKYIGKDP IHRKHHHGDI LFGLQYAFSE NFILPLSHDE VVHGKRSILG RMPGDEWQRF
ANLRAYYSFM FAHPGKKLLF MGCEFGQVRE WDHDHSLDWH LTEQPKHAGV QNLIRDLNRL
YRALPALHEL DCDQAGFEWV VTNDANHNLF AWIRKGSDAR ARCLVVVNFS PNVYRNYRVR
VPFAGKWHEV LNSDSAHYGG SNVGNIGEVR ASEGATPELS LTIPPLAAIF LVPES
//