ID A0A1M5PM82_BUTFI Unreviewed; 855 AA.
AC A0A1M5PM82;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN02745229_00033 {ECO:0000313|EMBL:SHH02806.1};
OS Butyrivibrio fibrisolvens DSM 3071.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1121131 {ECO:0000313|EMBL:SHH02806.1, ECO:0000313|Proteomes:UP000184278};
RN [1] {ECO:0000313|EMBL:SHH02806.1, ECO:0000313|Proteomes:UP000184278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3071 {ECO:0000313|EMBL:SHH02806.1,
RC ECO:0000313|Proteomes:UP000184278};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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.
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; FQXK01000003; SHH02806.1; -; Genomic_DNA.
DR RefSeq; WP_073384518.1; NZ_FQXK01000003.1.
DR AlphaFoldDB; A0A1M5PM82; -.
DR STRING; 1121131.SAMN02745229_00033; -.
DR GeneID; 40455670; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000184278; 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:UniProtKB-UniPathway.
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 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; 2.
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};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 253..589
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 800..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 717..783
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 819..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 97752 MW; 3ACC49A0B93A1B53 CRC64;
MSNRLYKLMN WPEIEEIIYS DGHDPHRILG AHKVGNQILI QTFRPDYAEI KVVSSDGKTY
KMELEDDAGF YAALLPYKAN FSYHYVLVDQ SGQETVLHDP YIYEPVITRE DCIKFSSGMH
DTIYEKLGAH VMERDGVKGV NFAVWAPDAA RVSVIGDFNS WDGRIHQMRR VDESGVYELF
IPDVAEGEEY QFECKTRGGE IFLRPDPYAL RTKDYKAEVS VVSAPASYKW SDKAWMTQRK
TYDKTGSALS ICELSLDGFA QTAFEDDETV TYAALASRVI HYVKANGFNA IELLPVCEHD
EVHKFDVNSF YAIKGEYGTA AEFMGFIDAC HKEGIRVILD WTATYFPRRD YGLSYFDGHA
LYEYEDPGKG TQPGTHRLIF DYGRKQVTNF LYANALYLLK EFHIDGLRIT DISKVLYLDY
DRKPGEWTPN IYGGYENLEA VEFMRELTQK INQFDQGVLL ITKETACWPH LTDTVEEGGL
GFDYKWNNGW SHDCLEYMKY DPLFRGQHHN ELTFSMMYSY TEKFILALSH EDVGGYPALK
EMMPGDDDQK ESNVRLTIAY LMVHPGKKML YHGRNAVSME RGLQMENFIY KLNMMYFEHP
ALYELDDVTD GFEWINSMAA DLCMLAFVRK SSKDEEELLV VMNMAGVERE LRVGVNHDGR
YEEILNTDAK DFGGSGVIND RKIEADLIEA DGRKYSVPVR LAPLSLAVFS YIPYTDKEKK
IRKIREEAHE KKIAEQEKSR SLLLSKHEKE EAKMLAELKA KYEKELAQQQ KAIEEKYDKI
EEERIFAIVS DAAIEKLSET SKDAAKKPAK AASKKSSITK FPEGKEVKKA APKKTSAKGK
SSAKGGKKKP TGDKS
//
