GLGB_MAIZE
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 03-AUG-2022, entry version 144.
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}.
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; 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.GRMZM2G032628_P01; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q08047; -.
DR PRIDE; Q08047; -.
DR GeneID; 542238; -.
DR KEGG; zma:542238; -.
DR MaizeGDB; 63943; -.
DR eggNOG; KOG0470; Eukaryota.
DR OrthoDB; 165238at2759; -.
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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProt.
DR GO; GO:0005982; P:starch metabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 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
