ID A0A1Q5Q1F7_9ACTO Unreviewed; 1192 AA.
AC A0A1Q5Q1F7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BSZ39_08665 {ECO:0000313|EMBL:OKL53586.1};
OS Bowdeniella nasicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Bowdeniella.
OX NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL53586.1, ECO:0000313|Proteomes:UP000185628};
RN [1] {ECO:0000313|Proteomes:UP000185628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA Meng X.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_00685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC EC=2.7.1.175; Evidence={ECO:0000256|ARBA:ARBA00001537};
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|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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:OKL53586.1}.
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DR EMBL; MQVR01000051; OKL53586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5Q1F7; -.
DR STRING; 208480.SAMN02910418_00218; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000185628; 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; 3.90.1200.10; -; 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; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040999; Mak_N_cap.
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 Pfam; PF18085; Mak_N_cap; 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.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685};
KW Reference proteome {ECO:0000313|Proteomes:UP000185628};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 718..1099
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 870
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 923
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1192 AA; 131916 MW; C1132507BD7A85F4 CRC64;
MMTDIPHLSA DLFAPYLARR RWYQGKDHDP QLAHCATGMS LRSKDKNATI HVLVLADIAA
DRPTHYQVPV VVRRRPLADL TDALIAEVAP PPGAGADTGP RYVYDAVYDP AFAPALLAEL
VGAPTGDVTA ARVMSAEQSN TSLVVDMSDG ERLIVKLFRV LNPGENPDVV VQGALGEAGC
PYVPAPKGYL AGGWQQLNVD GSAGERVSGH LAVAQEFLPD VTDAWSEALA SLTDGRDFTE
AARDLGTATA EVHRVLADVM PTHRATDDVR TALTDSWRER LAQAIDAVPE LAEHEAAAEE
IFAAAASGRW PRLQRIHGDY HLGQVLNVPG RGWVLLDFEG EPLRPLTERT QPDLPLRDIA
GMLRSFDYAA GSVPNANDDA WAAAARVAFL AGYCEHSECD PDDYPELLRA LELDKALYEA
VYEARNRPDW LALPVAGISR LCAGDATANQ DAAGRPRPDK RWETNTMNAE PLPVSHDYLA
AVARGLHHDP HSILGAHEHD GAITIRTLRH LASSVEIVTE DASYPARHEH DGIWVAVLPV
AEVPDYRVRV SYGGESHLLD DPYRFWPTFG ELDGHLLAAG RHEDLWRVLG AHVRRFPSAL
GDVEGVSFTV WAPSARAVRV KGDMNSWDGT QHAMRSLGSS GVWELFIPGA RTGQCYKFEI
WSEGGGWLEK ADPMARGTQI PPATASVVVE SAYEWNDDAW LARRAETDPH SGPMSIYEVH
LGSWRAGLSY RALAHELTEY VTSLGFTHVE FMPIAEHPFG GSWGYQVTSY YAPTARLGSP
DDFKYLVDCL HQAGIGVIVD WVPAHFPKDS WALARFDGTP LYEDPNPLRG EHPDWGTLVF
NFGRNEVRNF LVANALYWLE EFHIDALRVD AVASMLYLDY SREDGAWQPN IYGGRENLEA
IQFLQEANAT AYRRNPGIAM IAEESTSWPG VTAPTDAGGL GFGLKWNMGW MNDTLRYMAE
APINRRYHHG MLTFSLVYAF SEQFVLPFSH DEVVHGKGSL KRKMPGDWWQ QLAGVRALLA
YQWSHPGKQL LFMGQEFAQD SEWTESQSLD WWLLDNPTHA GVAELVRTMN ELYREHPALY
SEDFSHRGFE WIQADDADHN VLSFLRRSAD GEDVIACIIN FAGTPHENYR IGLPQGGDWL
ELLNTDSELY GGSGVGNLGR VSAEEIPWDG REHSVRLRIP PLGALWLSPA KD
//
