ID R7AFL0_9BACE Unreviewed; 670 AA.
AC R7AFL0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=BN800_00493 {ECO:0000313|EMBL:CDD52191.1};
OS Bacteroides sp. CAG:875.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262752 {ECO:0000313|EMBL:CDD52191.1, ECO:0000313|Proteomes:UP000018287};
RN [1] {ECO:0000313|EMBL:CDD52191.1, ECO:0000313|Proteomes:UP000018287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:875 {ECO:0000313|Proteomes:UP000018287};
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:CDD52191.1}.
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DR EMBL; CBHD010000213; CDD52191.1; -; Genomic_DNA.
DR AlphaFoldDB; R7AFL0; -.
DR Proteomes; UP000018287; 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 670 AA; 77954 MW; CA3D8C5C5D98B302 CRC64;
MDKVLNIIKN DPWLEPYANA INGRHQHAIE KEKELVGKKT LSDFATGHMY FGLHRTEKGW
TFREWAPNAT EIYLVGDFNG WQEKPSFRLK RVRKTGNWEI NLPEKALKHG DLYKLKVYWE
GGCGERIPAW ATRVVQDEQT KIFSAQVWNP EKPYKFKKKS FTPNVSPLMI YECHIGMAQD
AEKVGTYNEF RENVLPRIAK DGYNCIQIMA IQEHPYYGSF GYHVSSFFAP SSRFGTPEEL
KQLIDTAHQM NIAVIMDIVH SHAVKNEVEG LGNFAGDPYQ YFYPGDRREH PAWDSLCFDY
GKNEVVHFLL SNCKYWLEEF HFDGFRFDGV TSMLYYSHGL GEAFCNYGDY FNGHQDDNAI
CYLTLANRLI HEVNPKAITI AEEVSGMPGL AAPFEDGGYG FDYRMAMNIP DYWIKIIKER
KDEDWKPSSL FWEVTNRRKD EKTISYCESH DQALVGDKTI IFRLIDADMY WHFKIGDENG
VVERGIALHK MIRLLTASTI NGGYLNFMGN EFGHPEWIDF PREGNGWSYK YARRQWHLVD
DPTLYYHYLG DFDECMVKLM RSVKNIQKSD VIEVWHNDGD QILAFRRKDL VFVFNFNPTR
SFTDYGFLVP RGAYDVVLNT DSKQFGGFGF SDDSLRHFTC ADPLYAKDKK EWLKLYVPAR
SAVVLKRVKD
//
