ID R6Q0Y1_9BACT Unreviewed; 690 AA.
AC R6Q0Y1;
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=BN637_02089 {ECO:0000313|EMBL:CDC26684.1};
OS Prevotella sp. CAG:386.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC26684.1, ECO:0000313|Proteomes:UP000018046};
RN [1] {ECO:0000313|EMBL:CDC26684.1, ECO:0000313|Proteomes:UP000018046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
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:CDC26684.1}.
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DR EMBL; CBEZ010000163; CDC26684.1; -; Genomic_DNA.
DR AlphaFoldDB; R6Q0Y1; -.
DR STRING; 1262925.BN637_02089; -.
DR Proteomes; UP000018046; 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:UP000018046};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 207..559
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 404
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 690 AA; 79344 MW; ADA55890BA779323 CRC64;
MATKKTTTPA KGVKAKTKKT VQPKHIGLVK NDPYLEPYED AIRGRHEHAL WKLGQLTQNG
KKTLNDFANG YDYFGLHKTA RGWVFREWAP NATEIYLIGE FNDWKECPKY KAKRISGTGN
WELKLSEKAI KHGDLYKMKV HWQGGEGERI PAWAQRVVQD EQTKIFSAQV WNPEPYTWKK
KSFRPNTSPL LIYECHIGMG QDAEKVGTYT EFKEKVLPRI IADGYNCIQI MAIQEHPYYG
SFGYHVSSFF AASSRFGTPE ELKSLIDTAH QNGIAVIMDI VHSHAVKNEV EGLGNLAGDP
NQYFYPGDRH EHPAWDSLCF DYGKDEVIHF LLSNCKYWLA EFHFDGFRFD GVTSMLYYSH
GLGEAFMGYG DYFNGHEDDN AICYLTLANL LIHEVNKHAI TIAEEVSGMP GLAAKFTDGG
YGFDYRMAMN IPDYWIKTIK ELPDEAWKPS SIFWEVKNRR ADEKTISYCE SHDQALVGDK
TIIFRLIDAD MYWHFKKGDE NDMAHRGIAL HKMIRLVTAS TINGGYLNFM GNEFGHPEWI
DFPREGNGWS YKYARRQWNL VDNKELCYCY LGDFDKAMIK TIKSEKNFNK TPVQEIWHND
GDQVLAYMRG DLLFVFNFSP TRSFTDYGFL VPTGAYSIVL DTDNKEFGGN GLNDDSMTHL
TTYDPLYVGD RKEWLKLYLP ARSALVLKKN
//
