ID A0A2T6ZJV4_TUBBO Unreviewed; 706 AA.
AC A0A2T6ZJV4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=1,4-alpha-glucan-branching enzyme {ECO:0000256|ARBA:ARBA00020932};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
DE AltName: Full=Glycogen-branching enzyme {ECO:0000256|ARBA:ARBA00031979};
GN ORFNames=B9Z19DRAFT_1089650 {ECO:0000313|EMBL:PUU75771.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU75771.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU75771.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU75771.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) 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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964}.
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:PUU75771.1}.
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; NESQ01000215; PUU75771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6ZJV4; -.
DR STRING; 42251.A0A2T6ZJV4; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000244722; 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:UniProtKB-UniPathway.
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 Hydrolase {ECO:0000313|EMBL:PUU75771.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244722};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 220..574
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 363
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 418
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 706 AA; 80793 MW; 95D828EA3550EE74 CRC64;
MDLTRASKNT VAPATAPVKK VAKSNTPGSM PTDGTGIVEM DPWLGPFKDD LRRRFSKANE
WIQKLNSHEG GLKEFSKGYE KFGINVARNG TITYREWAPN AVNANFIGDF NGWNRQSHPM
KKNEYGVWEI TLPPVNGKPA IPHNTKVKID FQLPSGERVD RLPAWIKRVT QDLSVSPIYD
AVFWNPEKKY VFKHPRPKKP KSARVYEAHV GISTTEYRVG TYTEFTANVL PRIKKLGYNV
IQLMAIQEHA YYASFGYQVT SFFAASSRYG TPEELMELID TAHGMGITVL LDIVHSHACK
NVLDGINMFD GSDHLYFHEG PRGRHELWDS RLFNYGHHEV LRFLISNLRF YLEEYKFDGF
RFDGVTSILY THHGIGTGFS GGYHEYFGGN VDEEGVVYLM LANEMIHENF PEAVTIAEDV
SGMPGLCVPL ALGGVGFDYR LAMAIPDMWI KLLKEKKDDE WDMSNICWIL TNRRHGEKTI
AYAESHDQAL VGDKSLLMWL CDKELYTHMS TLTDFTPIIE RGLALHKMIR LLTHGLGGEG
YLNFEGNEFG HPEWLDFPRA GNNNSYHYAR RQWNILDDPL LRYKFLNDFD ASMQHLEERY
GWLHSPQAYI SLKHEGDKII VFERAGLVFV FNFHPTESFA DFRIGIEQAG TYRIVLNTDR
KELGGLGRID ESVRFFTTDF NWNGRKNFTQ VYIPTRTAIV LALEDA
//