GLGB3_ARATH
ID GLGB3_ARATH Reviewed; 899 AA.
AC D2WL32; F4JEP1; Q8GWK4; Q9LTP8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic;
DE Short=AtSBE III;
DE EC=2.4.1.18;
DE AltName: Full=Branching enzyme 1;
DE Short=AtBE1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2729;
DE AltName: Full=Starch-branching enzyme 3;
DE Flags: Precursor;
GN Name=SBE3; Synonyms=BE1, EMB2729; OrderedLocusNames=At3g20440;
GN ORFNames=MQC12.20;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MUTAGENESIS OF GLU-366, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20377688; DOI=10.1111/j.1744-7909.2010.00930.x;
RA Wang X., Xue L., Sun J., Zuo J.;
RT "The Arabidopsis BE1 gene, encoding a putative glycoside hydrolase
RT localized in plastids, plays crucial roles during embryogenesis and
RT carbohydrate metabolism.";
RL J. Integr. Plant Biol. 52:273-288(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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] (ISOFORM 2).
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 [5]
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 [6]
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 [7]
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. Essential during
CC embryogenesis. {ECO:0000269|PubMed:17028209,
CC ECO:0000269|PubMed:20377688}.
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, ECO:0000269|PubMed:20377688}. Plastid,
CC amyloplast {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=D2WL32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D2WL32-2; Sequence=VSP_042217;
CC Name=3;
CC IsoId=D2WL32-3; Sequence=VSP_042216, VSP_042218, VSP_042219;
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers and inflorescence, and,
CC to a lower extent, in seedlings, roots, stems, leaves, siliques and
CC seeds. {ECO:0000269|PubMed:17698298, ECO:0000269|PubMed:20377688}.
CC -!- DISRUPTION PHENOTYPE: Embryolethal. Embryo developmental arrests at the
CC heart stage associated with reduced cell divisions and abnormal cell
CC differentiation, thereby leading to defects in setting up the shoot
CC apical meristem, embryonic vascular tissues and cotyledons. Modified
CC starch composition. This phenotype is enhanced when associated with
CC SBE2.1 and SBE2.2 disruptions. {ECO:0000269|PubMed:17028209,
CC ECO:0000269|PubMed:20377688}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ374452; ADB29066.1; -; mRNA.
DR EMBL; AB024036; BAB02827.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76378.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76379.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76380.1; -; Genomic_DNA.
DR EMBL; AK118785; BAC43378.1; -; mRNA.
DR RefSeq; NP_001154629.1; NM_001161157.2. [D2WL32-1]
DR RefSeq; NP_001189940.1; NM_001203011.1. [D2WL32-3]
DR RefSeq; NP_188679.2; NM_112935.2. [D2WL32-2]
DR AlphaFoldDB; D2WL32; -.
DR SMR; D2WL32; -.
DR STRING; 3702.AT3G20440.2; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; D2WL32; -.
DR PRIDE; D2WL32; -.
DR ProteomicsDB; 248572; -. [D2WL32-1]
DR EnsemblPlants; AT3G20440.1; AT3G20440.1; AT3G20440. [D2WL32-2]
DR EnsemblPlants; AT3G20440.2; AT3G20440.2; AT3G20440. [D2WL32-1]
DR EnsemblPlants; AT3G20440.3; AT3G20440.3; AT3G20440. [D2WL32-3]
DR GeneID; 821589; -.
DR Gramene; AT3G20440.1; AT3G20440.1; AT3G20440. [D2WL32-2]
DR Gramene; AT3G20440.2; AT3G20440.2; AT3G20440. [D2WL32-1]
DR Gramene; AT3G20440.3; AT3G20440.3; AT3G20440. [D2WL32-3]
DR KEGG; ath:AT3G20440; -.
DR Araport; AT3G20440; -.
DR TAIR; locus:2092349; AT3G20440.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011131_1_1_1; -.
DR InParanoid; D2WL32; -.
DR OMA; KQSYAVH; -.
DR OrthoDB; 165238at2759; -.
DR BioCyc; ARA:AT3G20440-MON; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:D2WL32; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; D2WL32; baseline and differential.
DR Genevisible; D2WL32; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
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:0005975; P:carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43651; PTHR43651; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PIRSF; PIRSF000463; GlgB; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amyloplast; Chloroplast; Glycosyltransferase;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..899
FT /note="1,4-alpha-glucan-branching enzyme 3,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000415337"
FT REGION 47..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 612
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT VAR_SEQ 365
FT /note="P -> PGMTAF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042216"
FT VAR_SEQ 424..453
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_042217"
FT VAR_SEQ 780
FT /note="K -> KVS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042218"
FT VAR_SEQ 881..889
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_042219"
FT MUTAGEN 366
FT /note="E->K: In be1-3; reduced level of BE1 transcription
FT and various developmental defects during post-germination
FT growth such as shorter primary roots, delayed greening of
FT cotyledons and leaf development, yellowish and small leaves
FT leading to smaller plants with altered petals and sepals in
FT flowers."
FT /evidence="ECO:0000269|PubMed:20377688"
SQ SEQUENCE 899 AA; 103525 MW; 6C047303FD5D924E CRC64;
MVSLSNQTRF SFHPNNLVVS EKRRLGISGV NFPRKIKLKI TCFAAERPRQ EKQKKKSQSQ
STSDAEAGVD PVGFLTRLGI ADRIFAQFLR ERHKALKDLK DEIFKRHFDF RDFASGFELL
GMHRHMEHRV DFMDWGPGSR YGAIIGDFNG WSPTENAARE GLFGHDDYGY WFIILEDKLR
EGEEPDELYF QQYNYVDDYD KGDSGVSAEE IFQKANDEYW EPGEDRFIKN RFEVPAKLYE
QMFGPNSPQT LEELGDIPDA ETRYKQWKEE HKDDPPSNLP PCDIIDKGQG KPYDIFNVVT
SPEWTKKFYE KEPPIPYWLE TRKGRKAWLQ KYIPAVPHGS KYRLYFNTPD GPLERVPAWA
TYVQPEDEGK QAYAIHWEPS PEAAYKWKYS KPKVPESLRI YECHVGISGS EPKVSTFEEF
TKKVLPHVKR AGYNAIQLIG VPEHKDYFTV GYRVTNFFAA SSRYGTPDDF KRLVDEAHGL
GLLVFLDIVH SYAAADQMVG LSLFDGSNDC YFHYGKRGHH KHWGTRMFKY GDLDVLHFLI
SNLNWWITEY QVDGYQFHSL ASMIYTHNGF ASFNNDLDDY CNQYVDRDAL MYLILANEIL
HVQHPNIITI AEDATYYPGL CEPVSQGGLG FDYYVNLSAS EMWVSLLDNV PDNEWSMSKI
VSTLVANKEY ADKMLSYAEN HNQSISGGRS FAEILFGGVD NGSPGGKELL DRGISLHKMI
RLITFTSGGR AYLNFMGNEF GHPERVEFPT QSNNFSFSLA NRRWDLLESG VHHHLFSFDK
ELMDLDKSKG ILSRGLPSIH HVNDANMVIS FSRGPFLFIF NFHPSNSYEK YDVGVEEAGE
YTMILNSDEV KYGGQGIVTE DHYLQRSISK RIDGQRNCLE VFLPSRTAQV YKLTRILRI
