ID R5CG54_9BACT Unreviewed; 687 AA.
AC R5CG54;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BN458_00219 {ECO:0000313|EMBL:CCX66668.1};
OS Prevotella sp. CAG:1058.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262918 {ECO:0000313|EMBL:CCX66668.1, ECO:0000313|Proteomes:UP000018314};
RN [1] {ECO:0000313|EMBL:CCX66668.1, ECO:0000313|Proteomes:UP000018314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1058 {ECO:0000313|Proteomes:UP000018314};
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:CCX66668.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAWU010000159; CCX66668.1; -; Genomic_DNA.
DR AlphaFoldDB; R5CG54; -.
DR STRING; 1262918.BN458_00219; -.
DR Proteomes; UP000018314; 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 Reference proteome {ECO:0000313|Proteomes:UP000018314};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 204..573
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 347
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 687 AA; 79350 MW; A6524505352D88EF CRC64;
MVVRRSKSSK DAGEVAKQPK HIGLVANDSY LAPYEDAIRG RHDHAVWKLN QLTRNGKDTL
EGFASGYDYY GLHKVSRGWV FREWAPNATA IYLVGDFNNW EESERYKAKR IEGTGNWELK
ISEKGMKHGD LYKMHVYWEG GHGERIPAWA QRVVQDDSTK IFSAQVWNPD KPYVWKKKKF
KPSKNPLLIY ECHIGMAQDA EKVGTYTEFK DNVLPRIIVD GYNCIQIMAI QEHPYYGSFG
YHVSSFFAAS SRFGTPEELK SLIDEAHRNG IAVIMDIVHS HAVKNEVEGL GNLAGDPNQY
FYPGDRHEHP AWDSLCFDYG KDDVIHFLLS NCKYWMKEFH FDGFRFDGVT SMLYYSHGLG
EAFCNYGDYF NGHEDDNAIC YLTLANKLIH EINPDAITIA EEVSGMPGLA ARFEDGGFGF
DYRMAMNIPD YWIKTIKERS DEEWKPSSIF WEVKNRRPDE KTISYCESHD QALVGDKTIV
FRLIDADMYW HFKKGDENDI VHRGIALHKM IRLVTAAAIN GGYLNFMGNE FGHPEWIDFP
REGNGWSYKY ARRQWNLVDN HELCYHYLGD FDREMIKVIK SVRNFQNTPV QEIWHNDGDQ
VLAFMRGDLV FVFNFSPTRS YTDYGFLVPT GAYDVVLNTD SKNFGGNGFA DDSMTHVTNY
DPLYVKDHKE WLKLYIPARS AVVLKKN
//
