ID   GLGB_MAIZE              Reviewed;         799 AA.
AC   Q08047;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme 2, chloroplastic/amyloplastic;
DE            EC=2.4.1.18;
DE   AltName: Full=Q-enzyme;
DE   AltName: Full=Starch-branching enzyme IIB;
DE   Flags: Precursor;
GN   Name=SBE1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 58-65.
RC   STRAIN=cv. W64A X 182E; TISSUE=Endosperm;
RX   PubMed=8278524; DOI=10.1104/pp.102.3.1045;
RA   Fisher D.K., Boyer C.D., Hannah L.C.;
RT   "Starch branching enzyme II from maize endosperm.";
RL   Plant Physiol. 102:1045-1046(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 248-271 AND 305-315.
RC   STRAIN=cv. B73; TISSUE=Endosperm;
RX   PubMed=7849565;
RA   Guan H.P., Baba T., Preiss J.;
RT   "Expression of branching enzyme II of maize endosperm in Escherichia
RT   coli.";
RL   Cell. Mol. Biol. 40:981-988(1994).
CC   -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC       in starch by scission of a 1,4-alpha-linked oligosaccharide from
CC       growing alpha-1,4-glucan chains and the subsequent attachment of the
CC       oligosaccharide to the alpha-1,6 position.
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   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L08065; AAA18571.1; -; mRNA.
DR   PIR; T02981; T02981.
DR   RefSeq; NP_001105316.1; NM_001111846.2.
DR   AlphaFoldDB; Q08047; -.
DR   SMR; Q08047; -.
DR   STRING; 4577.Q08047; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 4577-GRMZM2G032628_P01; -.
DR   GeneID; 542238; -.
DR   KEGG; zma:542238; -.
DR   MaizeGDB; 63943; -.
DR   eggNOG; KOG0470; Eukaryota.
DR   InParanoid; Q08047; -.
DR   OrthoDB; 96at2759; -.
DR   BRENDA; 2.4.1.18; 6752.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q08047; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; 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   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; Direct protein sequencing; Glycosyltransferase;
KW   Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:8278524"
FT   CHAIN           58..799
FT                   /note="1,4-alpha-glucan-branching enzyme 2,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000011147"
FT   ACT_SITE        447
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        502
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   799 AA;  90518 MW;  0B440E0377B8087A CRC64;
     MAFRVSGAVL GGAVRAPRLT GGGEGSLVFR HTGLFLTRGA RVGCSGTHGA MRAAAAARKA
     VMVPEGENDG LASRADSAQF QSDELEVPDI SEETTCGAGV ADAQALNRVR VVPPPSDGQK
     IFQIDPMLQG YKYHLEYRYS LYRRIRSDID EHEGGLEAFS RSYEKFGFNA SAEGITYREW
     APGAFSAALV GDVNNWDPNA DRMSKNEFGV WEIFLPNNAD GTSPIPHGSR VKVRMDTPSG
     IKDSIPAWIK YSVQAPGEIP YDGIYYDPPE EVKYVFRHAQ PKRPKSLRIY ETHVGMSSPE
     PKINTYVNFR DEVLPRIKKL GYNAVQIMAI QEHSYYGSFG YHVTNFFAPS SRFGTPEDLK
     SLIDRAHELG LLVLMDVVHS HASSNTLDGL NGFDGTDTHY FHSGPRGHHW MWDSRLFNYG
     NWEVLRFLLS NARWWLEEYK FDGFRFDGVT SMMYTHHGLQ VTFTGNFNEY FGFATDVDAV
     VYLMLVNDLI HGLYPEAVTI GEDVSGMPTF ALPVHDGGVG FDYRMHMAVA DKWIDLLKQS
     DETWKMGDIV HTLTNRRWLE KCVTYAESHD QALVGDKTIA FWLMDKDMYD FMALDRPSTP
     TIDRGIALHK MIRLITMGLG GEGYLNFMGN EFGHPEWIDF PRGPQRLPSG KFIPGNNNSY
     DKCRRRFDLG DADYLRYHGM QEFDQAMQHL EQKYEFMTSD HQYISRKHEE DKVIVFEKGD
     LVFVFNFHCN NSYFDYRIGC RKPGVYKVVL DSDAGLFGGF SRIHHAAEHF TADCSHDNRP
     YSFSVYTPSR TCVVYAPVE
//