GLGB1_ARATH
ID GLGB1_ARATH Reviewed; 858 AA.
AC O23647; Q42526;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic;
DE Short=AtSBE II-1;
DE EC=2.4.1.18;
DE AltName: Full=Branching enzyme 3;
DE Short=AtBE3;
DE AltName: Full=Starch-branching enzyme 2-1;
DE Flags: Precursor;
GN Name=SBE2.1; Synonyms=BE3; OrderedLocusNames=At2g36390; ORFNames=F1O11.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX DOI=10.1016/S0168-9452(98)00093-4;
RA Khoshnoodi J., Larsson C.-T., Larsson H., Rask L.;
RT "Differential accumulation of Arabidopsis thaliana Sbe 2.1 and Sbe 2.2
RT transcripts in response to light.";
RL Plant Sci. 135:183-193(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-858, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=8616246; DOI=10.1007/bf00017805;
RA Fisher D.K., Gao M., Kim K.-N., Boyer C.D., Guiltinan M.J.;
RT "Two closely related cDNAs encoding starch branching enzyme from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 30:97-108(1996).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=17028209; DOI=10.1105/tpc.105.037671;
RA Dumez S., Wattebled F., Dauvillee D., Delvalle D., Planchot V., Ball S.G.,
RA D'Hulst C.;
RT "Mutants of Arabidopsis lacking starch branching enzyme II substitute
RT plastidial starch synthesis by cytoplasmic maltose accumulation.";
RL Plant Cell 18:2694-2709(2006).
RN [8]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17698298; DOI=10.1016/j.gene.2007.06.026;
RA Han Y., Sun F.-J., Rosales-Mendoza S., Korban S.S.;
RT "Three orthologs in rice, Arabidopsis, and Populus encoding starch
RT branching enzymes (SBEs) are different from other SBE gene families in
RT plants.";
RL Gene 401:123-130(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
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 {ECO:0000269|PubMed:17028209}.
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 stroma
CC {ECO:0000269|PubMed:18431481}. Plastid, amyloplast {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems, seeds,
CC inflorescences, flowers and leaves, and, to a lower extent, in
CC seedlings. {ECO:0000269|PubMed:17698298, ECO:0000269|PubMed:8616246}.
CC -!- INDUCTION: Induced by light, preferentially when associated with
CC glucose, fructose or sucrose treatment, but repressed by darkness.
CC {ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Modified starch composition. This phenotype is
CC enhanced when associated with SBE2.2 and SBE3 disruptions.
CC {ECO:0000269|PubMed:17028209}.
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; AJ000497; CAA04134.1; -; Genomic_DNA.
DR EMBL; AC006919; AAD24644.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09247.1; -; Genomic_DNA.
DR EMBL; AY136411; AAM97077.1; -; mRNA.
DR EMBL; AK226896; BAE98973.1; -; mRNA.
DR EMBL; U18817; AAB03099.1; -; mRNA.
DR PIR; B84780; B84780.
DR PIR; S65045; S65045.
DR RefSeq; NP_181180.1; NM_129196.4.
DR AlphaFoldDB; O23647; -.
DR SMR; O23647; -.
DR BioGRID; 3556; 8.
DR STRING; 3702.AT2G36390.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR iPTMnet; O23647; -.
DR MetOSite; O23647; -.
DR PaxDb; O23647; -.
DR PRIDE; O23647; -.
DR ProteomicsDB; 230477; -.
DR EnsemblPlants; AT2G36390.1; AT2G36390.1; AT2G36390.
DR GeneID; 818212; -.
DR Gramene; AT2G36390.1; AT2G36390.1; AT2G36390.
DR KEGG; ath:AT2G36390; -.
DR Araport; AT2G36390; -.
DR TAIR; locus:2044903; AT2G36390.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_2_1; -.
DR InParanoid; O23647; -.
DR OMA; KMIVCER; -.
DR OrthoDB; 165238at2759; -.
DR PhylomeDB; O23647; -.
DR BioCyc; ARA:AT2G36390-MON; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:O23647; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O23647; baseline and differential.
DR Genevisible; O23647; AT.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:TAIR.
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:0010021; P:amylopectin biosynthetic process; TAS:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0071332; P:cellular response to fructose stimulus; IEP:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:UniProtKB.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:UniProtKB.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; IEP:UniProtKB.
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; IMP:TAIR.
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; Glycosyltransferase; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..858
FT /note="1,4-alpha-glucan-branching enzyme 2-1,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000415335"
FT REGION 38..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 486
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 541
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 5..7
FT /note="ISG -> RAR (in Ref. 6; AAB03099)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="S -> T (in Ref. 6; AAB03099)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="C -> S (in Ref. 6; AAB03099)"
FT /evidence="ECO:0000305"
FT CONFLICT 745
FT /note="R -> P (in Ref. 6; AAB03099)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 97660 MW; E1D61C0C21D456F1 CRC64;
MVYTISGVRF PHLPSIKKKN SSLHSFNEDL RRSNAVSFSL RKDSRSSGKV FARKPSYDSD
SSSLATTASE KLRGHQSDSS SSASDQVQSR DTVSDDTQVL GNVDVQKTEE AQETETLDQT
SALSTSGSIS YKEDFAKMSH SVDQEVGQRK IPPPGDGKRI YDIDPMLNSH RNHLDYRYGQ
YRKLREEIDK NEGGLEAFSR GYEIFGFTRS ATGITYREWA PGAKAASLIG DFNNWNAKSD
VMARNDFGVW EIFLPNNADG SPAIPHGSRV KIRMDTPSGI KDSIPAWIKY SVQPPGEIPY
NGVYYDPPEE DKYAFKHPRP KKPTSLRIYE SHVGMSSTEP KINTYANFRD DVLPRIKKLG
YNAVQIMAIQ EHAYYASFGY HVTNFFAPSS RFGTPDDLKS LIDKAHELGL VVLMDIVHSH
ASKNTLDGLD MFDGTDGQYF HSGSRGYHWM WDSRLFNYGS WEVLRYLLSN ARWWLEEYKF
DGFRFDGVTS MMYTHHGLQV EFTGNYNEYF GYSTDVDAVV YLMLVNDLIH GLYPEAIVVG
EDVSGMPAFC VPVEDGGVGF DYRLHMAVAD KWIELLKKRD EDWQVGDITF TLTNRRWGEK
CVVYAESHDQ ALVGDKTIAF WLMDKDMYDF MAVDRQATPR VDRGIALHKM IRLITMGLGG
EGYLNFMGNE FGHPEWIDFP RTDQHLPDGR VIAGNNGSYD KCRRRFDLGD AEYLRYHGLQ
EFDRAMQNLE ETYGFMTSEH QYISRKDEGD RVIVFERGNL LFVFNFHWTN SYSDYRIGCS
VPGKYKIVLD SDNSLFGGFN RLDDSAEFFT SDGRHDDRPC SFMVYAPCRT AVVYAAVDDD
DDDERSSLVP IGLLPEDV
