ID U2NNR6_9BACT Unreviewed; 683 AA.
AC U2NNR6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-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=HMPREF9135_2212 {ECO:0000313|EMBL:ERK39710.1};
OS Segatella baroniae F0067.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK39710.1, ECO:0000313|Proteomes:UP000016648};
RN [1] {ECO:0000313|EMBL:ERK39710.1, ECO:0000313|Proteomes:UP000016648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0067 {ECO:0000313|EMBL:ERK39710.1,
RC ECO:0000313|Proteomes:UP000016648};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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:ERK39710.1}.
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DR EMBL; AWEY01000009; ERK39710.1; -; Genomic_DNA.
DR RefSeq; WP_021589275.1; NZ_AWEY01000009.1.
DR AlphaFoldDB; U2NNR6; -.
DR PATRIC; fig|1115809.3.peg.905; -.
DR Proteomes; UP000016648; 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:UP000016648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 187..552
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 397
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 683 AA; 78444 MW; F572E574DC1C96BB CRC64;
MAEKKKVAAG AGKKATQHVG LVKNDPYLEP YEDAVRGRHD HALWKLSQLT DGGKRKLADV
ANGHQYYGLH KTSRGWVFRE WAPNATGICL VGDFNGWTES DRYRAKRIEG TGNWELKLSE
KAVKHGDLYK MHVRWNGGEG ERIPAWATRV VQDEQTKIFS AQVWNPVPYE WKKKKFTPKR
DPLLIYECHV GMGQDAEKVG TYNEFRENVL PRIVKEGYNC IQVMAIQEHP YYGSFGYHVS
SFFAPSSRFG TPEELKALID AAHTAGIAVI MDIVHSHAVK NEVEGLGNLA GDPNQYFYPG
DRHEHPAWDS LCFDYGKDEV IHFLLSNCKY WLEEYHFDGF RFDGVTSMLY YSHGLGEAFC
NYGDYFNGHE DDNAICYLTL ANKLIHEVNP RAFTIAEEVS GMPGLAARFE DGGYGFDYRM
AMNIPDFWIK TIKEQRDEDW KPSSIFWEVK NRRADEKTIS YCESHDQALV GDKTIIFRLI
DADMYWHFKR GDETGLVHRG IALHKMIRLV TLGAINGGYL NFMGNEFGHP EWIDFPREGN
GWSHKYARRQ WNLVDNKDLD YHYLGDFDHD MLAVIKSEKK FNTTPVTEIW HNDGDQILAF
MRGDLLFVFN FSPTRSFTDY GFLVPIGGYE VVLNTDAKAY GGNGLADDSM THLTNYDPLY
VDQHKEWLKL YLPARSAVVL RKI
//
