ID R5FS42_9BACT Unreviewed; 697 AA.
AC R5FS42;
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=BN812_00972 {ECO:0000313|EMBL:CCY03492.1};
OS Prevotella sp. CAG:924.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY03492.1, ECO:0000313|Proteomes:UP000018357};
RN [1] {ECO:0000313|EMBL:CCY03492.1, ECO:0000313|Proteomes:UP000018357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357};
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:CCY03492.1}.
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DR EMBL; CAXK010000226; CCY03492.1; -; Genomic_DNA.
DR AlphaFoldDB; R5FS42; -.
DR STRING; 1262938.BN812_00972; -.
DR Proteomes; UP000018357; 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:UP000018357};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 214..566
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 411
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 697 AA; 80292 MW; 24A10221C2B632F3 CRC64;
MVKSKKTSAA TKTTATPKTK TATKTTVAPK HIGIVKNDPY LEPYEDAIRG RHDHALWKID
QLTQGGKITL SDFANGHEYY GLHHTTRGGW VFREWAPNAT DIYLVGDFND WQETEKYRCT
RIDNGNWELK LPAKAMKHGD LYKMHVKWNG GEGERIPAWC RRVIQDDNTK IFSAQVWDPE
HPYVWKKKTF RPHRDPLFIY ECHVGMAQDA EKVGTYTEFK DNVLPRIIKD GYNCIQIMAI
QEHPYYGSFG YHVSSFFAPS SRFGTPEELK ALIDAAHQQG VAVIMDIVHS HAVKNEVEGL
GNLAGDPNQY FYPGERHEHP AWDSLCFDYG KDDVIHFLLS NCKYWLEEYH FDGFRFDGVT
SMLYYSHGLG EAFTNYGDYF NGHEDDNAIC YLTLANELIH EVNPNAFTIA EEVSGMPGLA
AKFKDGGFGF DYRMAMNIPD YWIKTIKERR DEDWKPSSIF WEVRNRRVDE KTVSYCESHD
QALVGDKTII FRLIDADMYW HFKKGDENDL VHRGIALHKM IRLVTAAAIN GGYLNFMGNE
FGHPEWIDFP REGNGWSYKY ARRQWNLVDN KDLCYHYLGD FDKAMLETLK SEKAFNRTPV
QEIWHNDGDQ ILCFSRGSLI FVFNFSPTRS FTDYGFLVPE GSYNVVLDSD SPAFGGNGLN
DDSVEHMTVP DPLYAPDHKG WLKLYVPARC ALVLRKK
//
