ID B6W6U0_9FIRM Unreviewed; 663 AA.
AC B6W6U0;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=ANHYDRO_00274 {ECO:0000313|EMBL:EEB36880.1};
OS Anaerococcus hydrogenalis DSM 7454.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=561177 {ECO:0000313|EMBL:EEB36880.1, ECO:0000313|Proteomes:UP000005451};
RN [1] {ECO:0000313|EMBL:EEB36880.1, ECO:0000313|Proteomes:UP000005451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36880.1,
RC ECO:0000313|Proteomes:UP000005451};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB36880.1, ECO:0000313|Proteomes:UP000005451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36880.1,
RC ECO:0000313|Proteomes:UP000005451};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454).";
RL Submitted (OCT-2008) 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 -!- 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:EEB36880.1}.
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DR EMBL; ABXA01000004; EEB36880.1; -; Genomic_DNA.
DR RefSeq; WP_004812631.1; NZ_ABXA01000004.1.
DR AlphaFoldDB; B6W6U0; -.
DR STRING; 561177.ANHYDRO_00274; -.
DR eggNOG; COG0296; Bacteria.
DR Proteomes; UP000005451; 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; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_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; 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: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; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 172..564
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 380
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 663 AA; 78771 MW; E0ED650A4A7EBD8B CRC64;
MKDWKILEID PWIKDYKNDI DLRMEEYKKQ KNRLLKKGEK LKDFANAHNY YGFHKTKTGW
IYREWAPNAK GLYLVGDFNN WDRHSHPLKK INDSDWEIFI KGIRTIPHKS RLKVMVDYGD
SFQDRIPLFA RRVERDENHD FSAILENPRK KFEWTDDKFK IKKDDLLIYE AHIGMACERE
GVGTYKEFEK NILPRIKKEG YNTIQLMAIA EHPYYGSFGY QVSNFFAPSS WYGENDELKS
LINTAHEMGL NVIMDLVHSH SVKNTNEGIN LFDGTEYQFF HEGDEGNHPD WDSKLFDYHK
PGVCHFLLSN IKYWLEEFHF DGFRFDGVTS MIYKNHGRGE SFDNYSKYFS MNTDIEAINY
LQLANELIRE VKKDAITIAE DMSAMPGMCL PIKDGGIGFD YRLSMGMPDF WEKVLEKRDE
DWDMGRMWYE LSTYRPEEKR ISYVESHDQA LVGSKTTIFR LADSAMYWDM EKKTHNIIID
RAIALHKMIR WITISMGAEG YLNFMGNEFG HPEWIDFPRE GNNYSFHYAR RLWSLADNDL
LKYDWLLKWD EKMLDQIKEY DQLGNDIFRL WLDNDRKVIA YRNKDIVYIF NFHPQNSYDS
FQVPIHDKGK FKVILDTDDE EFGGLDRISK DIIYESKNLE NTDYDGIEIY IPSRTALALK
KVE
//
