ID   C5XTD4_SORBI            Unreviewed;       803 AA.
AC   C5XTD4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=SORBI_3004G163700 {ECO:0000313|EMBL:EES06902.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:EES06902.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EES06902.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000763; EES06902.1; -; Genomic_DNA.
DR   RefSeq; XP_002453926.1; XM_002453881.1.
DR   AlphaFoldDB; C5XTD4; -.
DR   SMR; C5XTD4; -.
DR   STRING; 4558.C5XTD4; -.
DR   EnsemblPlants; EES06902; EES06902; SORBI_3004G163700.
DR   GeneID; 8059621; -.
DR   Gramene; EES06902; EES06902; SORBI_3004G163700.
DR   KEGG; sbi:8059621; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   HOGENOM; CLU_011131_2_1_1; -.
DR   InParanoid; C5XTD4; -.
DR   OMA; KMIVCER; -.
DR   OrthoDB; 96at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000000768; Chromosome 4.
DR   ExpressionAtlas; C5XTD4; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IBA:GO_Central.
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   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005982; P:starch metabolic process; IBA:GO_Central.
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:SF13; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 2, CHLOROPLASTIC_AMYLOPLASTIC; 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   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          308..668
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        451
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        506
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   803 AA;  90755 MW;  6FAC41C9AB621378 CRC64;
     MAAFAVSGAA LGGAVRAPRL TGGEEGSLVF RRTGPFLTRA GGARVGGSGT HGAMRAAAAS
     SRKAVVVAEG ENDGLASKAD SAQFQSDELE VPDVTEETMC DAGVADAQAL NRVRVVPPPS
     DGQKIFQIDP MLQGYKYHLE YRYSLYRRIR SDIDEHEGGL EAFSRSYEKF GFNRSAEGIT
     YREWAPGALS AALVGDFNNW DPNADRMSKN EFGVWEIFLP NNADGTSPIP HGTRVKVRMD
     TPSGIKDSIP AWIKYSVQAP GEIPYDGLYY DPPEEVKYVF KHPKPKRPKS LRIYETHVGM
     SSPEPKINTY ANFRDEVLPR IKKLGYNAVQ IMAIQEHSYY GSFGYHVTNF FAPSSRFGTP
     EDLKSMIDRA HELGLLVLMD VVHSHASSNT LDGLNGFDGT DTHYFHSGPR GHHWMWDSRL
     FNYGNWEVLR FLLSNARWWL EEYKFDGFRF DGVTSMMYTH HGLQVTFTGN FNEYFGFATD
     VDAVVYLMLV NDLIHGLYPE AVTIGEDVSG MPTFALPVQD GGVGFDYRMH MAVADKWIEL
     LKQSDEAWKM GDIVHTLTNR RWLEKCVTYA ESHDQALVGD KTIAFWLMDK DMYDFMALDR
     PATPTIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGPQR LPSGKFIPGN
     NNSYDKCRRR FDLGDADYLR YRGMQEFDQA MQHLEQKYGF MTSDHQYISR KHEEDKMIVF
     EKGDLVFVFN FHCNNSYFDY RIGCRKPGMY KVVLDSDAGL FGGFGRIHHA AEHFTTDCSH
     DNRPHSFSVY TPSRTCVVYA PAE
//