ID A4GUI1_MAIZE Unreviewed; 799 AA.
AC A4GUI1;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
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 {ECO:0000313|EMBL:ABO25741.1};
RN [1] {ECO:0000313|EMBL:ABO25741.1}
RP NUCLEOTIDE SEQUENCE.
RA Huang Y.B., Zhang J.J., Zhou H., Hu Y.F., Tian M.L., Liu H.M., Liu Y.H.;
RT "Molecular cloning and characterization of the amylose-extender gene
RT encoding starch branching enzyme IIb in maize.";
RL Submitted (FEB-2007) 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; 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; EF433557; ABO25741.1; -; mRNA.
DR AlphaFoldDB; A4GUI1; -.
DR UniPathway; UPA00152; -.
DR ExpressionAtlas; A4GUI1; baseline and differential.
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: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 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 2: Evidence at transcript level;
KW Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 304..664
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 447
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 799 AA; 90557 MW; F4D99A942FFA70B1 CRC64;
MAFRVSGAVL GGAVRAPRLT GGGEGSLVFR HTGLFLTRGA RVGCSGTHGA MRAAAAARKA
VMVPEGENDG LASGADSAQF QSDELEVPDI SEETTCGAGV ADAQALNRVR VVPPPSDGQK
IFQIDPMLQG YKYHLEYRYS LYRRIRSDID EHEGGLEAFS RSYEKFGFNR SAEGITYREW
APGAFSAALV GDFNNWDPNA DRMSKNEFGV WEIFLPNNAD GTSPIPHGSR VKVRMDTPSG
IKDSIPAWIK YSVQAPGEIP YNGIYYDPPE EVKYVFRHAQ PKRPKSLRIY ETHVGMSSPE
PKINTYVNFR DEVLPRIKKL GYNAVQIMAI QEHSYYGSFG YHVTNFFAPS SRFGTPEDLK
SLIDRAHELG LLVLMDVVHS HASSNTLDGL NGFDGTDTHY FHSGPRGHHW MWDSRLFNYG
NWEVLRFLLS NARWWLEEYK FDGFRFDGVT SMMYTHHGLQ VTFTGNFNEY FGFATDVDAV
VYLMLVNDLI HGLYPEAVTI GEDVSGMSTF ALPVHDGGVG FDYRMHMAVA DKWIDLLKQS
DETWKMGDIV HTLTNRRWLE KCVTYAESHD QALVGDKTIA FWLMDKDMYD FMALDRPSTP
TIDRGIALHK MIRLITMGLG GEGYLNFMGN EFGHPEWIDF PRGPQRLPSG KFIPGNNNSY
DKCRRRFDLG DADYLRYHGM QEFDQAMQHL EQKYEFMTSD HQYISRKHEE DKVIVFEKGD
LVFVYNFHCN NSYFDYRIGC RKPGVYKVVL DSDAGLFGGF SRIHHAAEHF TADCSHDNRP
YSFSVYTPSR TCVVYAPVE
//
