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Database: UniProt
Entry: A0A0S3RZ11_PHAAN
LinkDB: A0A0S3RZ11_PHAAN
Original site: A0A0S3RZ11_PHAAN 
ID   A0A0S3RZ11_PHAAN        Unreviewed;       622 AA.
AC   A0A0S3RZ11;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   Name=Vigan.04G342700 {ECO:0000313|EMBL:BAT85833.1};
GN   ORFNames=VIGAN_04342700 {ECO:0000313|EMBL:BAT85833.1};
OS   Vigna angularis var. angularis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT85833.1, ECO:0000313|Proteomes:UP000291084};
RN   [1] {ECO:0000313|EMBL:BAT85833.1, ECO:0000313|Proteomes:UP000291084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX   PubMed=26616024; DOI=10.1038/srep16780;
RA   Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA   Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA   Tomooka N.;
RT   "The power of single molecule real-time sequencing technology in the de
RT   novo assembly of a eukaryotic genome.";
RL   Sci. Rep. 5:16780-16780(2015).
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; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000256|ARBA:ARBA00004602}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR   EMBL; AP015037; BAT85833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S3RZ11; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000291084; Chromosome 4.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd11321; AmyAc_bac_euk_BE; 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; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
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   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          99..479
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          599..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        297
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   622 AA;  71441 MW;  CA5193375F5EF832 CRC64;
     MSLVFGRFFL PNNVDGSPPI PHGSRVKIRM DTPSGVKDSI PAWIKFSVQA PGEIPYSGIY
     YDPPEEEKYV FKHPQPKRPK SLRIYESHVG MSSPEPMINT YANFRDDVLP RIKKLGYNAV
     QIMAIQEHSY YASFGYHVTN FFAPSSRFGT PEELKSLIDK AHELGLLVLM DIVHSHSSNN
     TLDGLNMFDG TDSHYFHPGS RGYHWMWDSR LFNYGSWEVL RYLLSNARWW LDEYKFDGFR
     FDGVTSMMYT HHGLQVAFTG NYSEYFGMAT DVDAVVYLML ANDLIHGLFP EAVTIGEDVS
     GMPTFCLPTQ DGGVGFDYRL QMAIADKWIE ILKKKDEDWK MGDIVHTLTN RRWLEKCVAY
     AESHDQALVG DKTIAFWLMD KDMYDFMALD RPSTPRIDRG IALHKMIRLI TMGLGGEGYL
     NFMGNEFGHP EWIDFPRGEQ QLPNGSVIPG NNYSYDKCRR RFDLGDADYL RYQGMQEFDR
     AMQLLEEKFG FMTAEHQYIS RKNEGDKVII FERGNLVFVF NFHWHNSYSD YRVGCSTPGK
     YKIVLDSDDA LFGGFNRLNH SAEYFTNEGW YDDRPRSFLV YAPSRTAAVY VLADDDDDLE
     PALSDEAEPA LADEAEPEPV DP
//
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