ID I0TCI4_9BACT Unreviewed; 692 AA.
AC I0TCI4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=HMPREF9969_2246 {ECO:0000313|EMBL:EID33337.1};
OS Prevotella sp. oral taxon 306 str. F0472.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1095752 {ECO:0000313|EMBL:EID33337.1, ECO:0000313|Proteomes:UP000004421};
RN [1] {ECO:0000313|EMBL:EID33337.1, ECO:0000313|Proteomes:UP000004421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0472 {ECO:0000313|EMBL:EID33337.1,
RC ECO:0000313|Proteomes:UP000004421};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (MAR-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:EID33337.1}.
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DR EMBL; AJIN01000042; EID33337.1; -; Genomic_DNA.
DR RefSeq; WP_009435115.1; NZ_AJIN01000042.1.
DR AlphaFoldDB; I0TCI4; -.
DR STRING; 1095752.HMPREF9969_2246; -.
DR PATRIC; fig|1095752.3.peg.1394; -.
DR eggNOG; COG0296; Bacteria.
DR OrthoDB; 9800174at2; -.
DR Proteomes; UP000004421; 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 217..578
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 406
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 692 AA; 79938 MW; 5D51AFC9E912E372 CRC64;
MVTKKSITKS TPKDVVKKKS KSAPAHIGLV KNDSYLSPYE DIIRGRHEHA LWKIKQLTQD
GKMTLSDFAN GYNYYGLHLT DEGWVFREWA PNATDIYLVG DFNGWKELPS YKCKRIEGTG
NWELRLPVHA MEHGQYYKMR VHWNGGEGER IPAWAQRVVQ DENTKIFSAQ VWNVEEPYVW
KKKNFKPSTD PLLIYECHIG MSQDAEKVGS YTEFRENVLP RIIKDGYNAI QIMAIQEHPY
YGSFGYHVSS FFAASSRFGT PEELKALIDE AHRNGIAVIM DIVHSHAVKN EVEGLGNLAG
DPNQYFYPGD RHEHPAWDSL CFDYGKDDVL HFLLSNCKYW LDEYHFDGFR FDGVTSMLYY
SHGLGEAFCD YGDYFNGHQD DNAICYLTLA NCLIHEVNKH AITIAEEVSG MPGLAAKFKD
GGYGFDYRMA MNIPDYWIKT IKELPDEAWK PSSIYWEIKN RRADEKTISY CESHDQALVG
DKTIIFRLID ADMYWHFRKG DENEMAHRGI ALHKMIRLAT IAAMNGGYLN FMGNEFGHPE
WIDFPREGNG WSYKYARRQW NLVDNKELCY HYLGDFDRKM LEVIKSEKKF NATPLQEIWH
NDGDQILAFS RGELLFVFNF SPTRSYADYG FLVPEGSYVV ELNSDAKEFG GNGFADDSVE
HFTNPDPLYT DQHKGWLKLY IPARSAVVLK KK
//
