GLGB2_ARATH
ID GLGB2_ARATH Reviewed; 805 AA.
AC Q9LZS3; O81711; Q42531; Q8GYC4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic;
DE Short=AtSBE II-2;
DE EC=2.4.1.18;
DE AltName: Full=Branching enzyme 2;
DE Short=AtBE2;
DE AltName: Full=Starch-branching enzyme 2-2;
DE Flags: Precursor;
GN Name=SBE2.2; Synonyms=BE2; OrderedLocusNames=At5g03650; ORFNames=F17C15.70;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81, 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-805, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-805.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=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 [7]
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 [8]
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).
RN [9]
RP INDUCTION BY GLUCOSE.
RC STRAIN=cv. Columbia;
RX PubMed=19392689; DOI=10.1111/j.1365-313x.2009.03877.x;
RA Bossi F., Cordoba E., Dupre P., Mendoza M.S., Roman C.S., Leon P.;
RT "The Arabidopsis ABA-INSENSITIVE (ABI) 4 factor acts as a central
RT transcription activator of the expression of its own gene, and for the
RT induction of ABI5 and SBE2.2 genes during sugar signaling.";
RL Plant J. 59:359-374(2009).
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: Expressed in seedlings, roots, stems, leaves,
CC inflorescences, seeds and flowers. {ECO:0000269|PubMed:17698298,
CC ECO:0000269|PubMed:8616246}.
CC -!- INDUCTION: Induced by light when associated with glucose, fructose or
CC sucrose treatment. Induction by glucose is mediated by the
CC transcription factor ABI4. {ECO:0000269|PubMed:19392689,
CC ECO:0000269|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: Modified starch composition. This phenotype is
CC enhanced when associated with SBE2.1 and SBE3 disruptions.
CC {ECO:0000269|PubMed:17028209}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
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DR EMBL; AL162506; CAB82930.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90637.1; -; Genomic_DNA.
DR EMBL; AJ005130; CAA06392.1; -; Genomic_DNA.
DR EMBL; U22428; AAB03100.1; -; mRNA.
DR EMBL; AK117729; BAC42378.1; -; mRNA.
DR PIR; S65046; S65046.
DR PIR; T48392; T48392.
DR RefSeq; NP_195985.3; NM_120446.4.
DR AlphaFoldDB; Q9LZS3; -.
DR SMR; Q9LZS3; -.
DR BioGRID; 17045; 8.
DR STRING; 3702.AT5G03650.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q9LZS3; -.
DR PRIDE; Q9LZS3; -.
DR ProteomicsDB; 248574; -.
DR EnsemblPlants; AT5G03650.1; AT5G03650.1; AT5G03650.
DR GeneID; 831769; -.
DR Gramene; AT5G03650.1; AT5G03650.1; AT5G03650.
DR KEGG; ath:AT5G03650; -.
DR Araport; AT5G03650; -.
DR TAIR; locus:2144608; AT5G03650.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_2_2_1; -.
DR InParanoid; Q9LZS3; -.
DR OMA; IPDYWIK; -.
DR OrthoDB; 165238at2759; -.
DR PhylomeDB; Q9LZS3; -.
DR BioCyc; ARA:AT5G03650-MON; -.
DR BioCyc; MetaCyc:AT5G03650-MON; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q9LZS3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZS3; baseline and differential.
DR Genevisible; Q9LZS3; 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..32
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 33..805
FT /note="1,4-alpha-glucan-branching enzyme 2-2,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000415336"
FT ACT_SITE 451
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 506
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 6..7
FT /note="GV -> RS (in Ref. 4; AAB03100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 92591 MW; 7CE130BD9C4941D0 CRC64;
MVVIHGVSLT PRFTLPSRPL NTGFNAGNST LSFFFKKHPL SRKIFAGKQS AEFDSSSQAI
SASEKVLVPD NLDDDPRGFS QIFDLESQTM EYTEAVRTED QTMNVVKERG VKPRIVPPPG
DGKKIYEIDP MLRTYNNHLD YRYGQYKRLR EEIDKYEGGL EAFSRGYEKL GFSRSDAGIT
YREWAPGAKA ASLIGDFNNW NSNADIMTRN EFGVWEIFLP NNTDGSPAIP HGSRVKIRMD
TPSGIKDSIP AWIKFSVQAP GEIPFNGIYY DPPEEEKYVF KHPQPKRPKS LRIYEAHVGM
SSTEPMVNTY ANFRDDVLPR IKKLGYNAVQ IMAIQEHSYY ASFGYHVTNF FAPSSRCGTP
EELKSLIDRA HELGLVVLMD IVHSHASKNT LDGLNMFDGT DAHYFHSGPR GYHWMWDSRL
FNYGSWEVLR YLLSNARWWL EEYKFDGFRF DGVTSMMYTH HGLSVGFTGN YTEYFGLETD
VDAVNYLMLV NDMIHGLYPE AITVGEDVSG MPTFCIPVQD GGVGFDYRLH MAIADKWIEM
LKKRDEDWQM GDIIYTLTNR RWSEKCISYA ESHDQALVGD KTIAFWLMDK DMYDFMAVDR
PSTPLIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGEQR LSDGSVIPGN
NFSYDKCRRR FDLGDADYLR YRGLQEFDQA MQHLEENYGF MTSEHQFISR KDEADRVIVF
ERGDLVFVFN FHWTSSYFDY RIGCSKPGKY KIVLDSDDPL FGGFNRLDRK AEYFTYDGLY
DERPCSFMVY APCRTAVVYA LANHD
