ID R5MIK2_9BACE Unreviewed; 669 AA.
AC R5MIK2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=BN461_02081 {ECO:0000313|EMBL:CCY91535.1};
OS Bacteroides sp. CAG:1076.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262735 {ECO:0000313|EMBL:CCY91535.1, ECO:0000313|Proteomes:UP000018060};
RN [1] {ECO:0000313|EMBL:CCY91535.1, ECO:0000313|Proteomes:UP000018060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1076 {ECO:0000313|Proteomes:UP000018060};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCY91535.1}.
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DR EMBL; CAZB010000100; CCY91535.1; -; Genomic_DNA.
DR AlphaFoldDB; R5MIK2; -.
DR Proteomes; UP000018060; 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 179..537
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 382
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 669 AA; 77758 MW; 8E339DD9870227B5 CRC64;
MDEVLNIIKN DPWLEPYKEA ITGRHQHAID KEKELIGKKT LSDFATGHLY FGLHRTEKGW
TFREWAPNAT EIYLIGDFNG WQEQAKYKLK RVKNTGNWEI NLRENAMKHG DLYKLKVYWE
GGCGERIPAW ATRVVQDDQT KIFSAQVWNP GKPYKFKKKV FVPNVSPLMI YECHIGMAQD
AEKVGTYNEF RENILPRVAK DGYNCIQIMA IQEHPYYGSF GYHVSSFFAP SSRFGTPEEL
KQLIDTAHQM GIAVIMDIVH SHAVKNEIEG LGNFAGDPCQ YFYQGERREH PAWDSLCFDY
GKNEVIHFLL SNCKYWLEEF HFDGFRFDGV TSMLYYSHGL GEAFCNYGDY FNGHEDDNAI
CYLTLANKLI HQVNPRAITI AEEVSGMPGL AAPFNDGGYG FDYRMAMNIP DYWIKIIKER
RDEDWKPSSM FWEVTNRRKD EKTISYCESH DQALVGDKTI IFRLIDADMY WHFKKGDENG
VVQRGIALHK MIRLLTASTI NGGYLNFMGN EFGHPEWIDF PREGNGWSYK YARRQWHLVD
DKDLCYHYLG DFDNAMVHLI EGVKNIQKTD VVEIWHNDGD QVLAYRRKDL IFVFNFSPTR
SFTDYGFLVP RGEYRVVLNT DNKAFGGFGF ADDTIAHFTC ADPLYAKEKK EWLKLYIPAR
SAVVLKRQK
//
