ID GLGB_ORYSJ Reviewed; 820 AA. AC Q01401; Q40664; Q5Z7Q1; Q7XZP9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 27-MAR-2024, entry version 159. DE RecName: Full=1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic; DE EC=2.4.1.18; DE AltName: Full=Q-enzyme; DE AltName: Full=Starch-branching enzyme; DE Flags: Precursor; GN Name=SBE1; Synonyms=RBE1; GN OrderedLocusNames=Os06g0726400, LOC_Os06g51084; GN ORFNames=P0017G10.8-1, P0017G10.8-2, P0548E04.28-1, P0548E04.28-2; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Endosperm; RX PubMed=16669000; DOI=10.1104/pp.99.3.1265; RA Nakamura Y., Yamanouchi H.; RT "Nucleotide sequence of a cDNA encoding starch-branching enzyme, or Q- RT enzyme I, from rice endosperm."; RL Plant Physiol. 99:1265-1266(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8455548; DOI=10.1007/bf00282778; RA Kawasaki T., Mizuno K., Baba T., Shimada H.; RT "Molecular analysis of the gene encoding a rice starch branching enzyme."; RL Mol. Gen. Genet. 237:10-16(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 65-81. RX PubMed=1478924; DOI=10.1093/oxfordjournals.jbchem.a123953; RA Mizuno K., Kimura K., Arai Y., Kawasaki T., Shimada H., Baba T.; RT "Starch branching enzymes from immature rice seeds."; RL J. Biochem. 112:643-651(1992). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Wuyunjing 7; TISSUE=Seed; RA Chen X.H., Liu Q.Q., Wu H.K., Wang Z.Y., Gu M.H.; RT "cDNA cloning and sequence analysis of rice Sbe1 and Sbe3 genes."; RL Zhongguo Shuidao Kexue 17:109-112(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Nanjing 37; RA Junwang X., Zhen Z.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [7] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). 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. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q01401-1; Sequence=Displayed; CC Name=2; CC IsoId=Q01401-2; Sequence=VSP_017510; CC -!- MISCELLANEOUS: Isoform 2 lacks the putative transit peptide and may be CC a cytosolic isoform. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA01616.1; Type=Erroneous gene model prediction; Evidence={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; D10752; BAA01584.1; -; mRNA. DR EMBL; D10838; BAA01616.1; ALT_SEQ; Genomic_DNA. DR EMBL; D11082; BAA01855.1; -; mRNA. DR EMBL; AY302112; AAP68993.1; -; mRNA. DR EMBL; AF136268; AAD28284.1; -; mRNA. DR EMBL; AP003685; BAD61712.1; -; Genomic_DNA. DR EMBL; AP003685; BAD61713.1; -; Genomic_DNA. DR EMBL; AP004685; BAD61804.1; -; Genomic_DNA. DR EMBL; AP004685; BAD61805.1; -; Genomic_DNA. DR EMBL; AP014962; BAS99598.1; -; Genomic_DNA. DR EMBL; AK068920; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; JX0243; JX0243. DR RefSeq; XP_015643111.1; XM_015787625.1. DR RefSeq; XP_015643112.1; XM_015787626.1. DR RefSeq; XP_015643113.1; XM_015787627.1. DR PDB; 3AMK; X-ray; 1.90 A; A=66-767. DR PDB; 3AML; X-ray; 1.70 A; A=66-820. DR PDB; 3VU2; X-ray; 2.23 A; A/B=66-767. DR PDB; 7ML5; X-ray; 2.35 A; A=67-767. DR PDBsum; 3AMK; -. DR PDBsum; 3AML; -. DR PDBsum; 3VU2; -. DR PDBsum; 7ML5; -. DR AlphaFoldDB; Q01401; -. DR SMR; Q01401; -. DR STRING; 39947.Q01401; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 39947-Q01401; -. DR EnsemblPlants; Os06t0726400-01; Os06t0726400-01; Os06g0726400. [Q01401-1] DR EnsemblPlants; Os06t0726400-04; Os06t0726400-04; Os06g0726400. [Q01401-2] DR GeneID; 4342117; -. DR Gramene; Os06t0726400-01; Os06t0726400-01; Os06g0726400. [Q01401-1] DR Gramene; Os06t0726400-04; Os06t0726400-04; Os06g0726400. [Q01401-2] DR KEGG; osa:4342117; -. DR eggNOG; KOG0470; Eukaryota. DR InParanoid; Q01401; -. DR OMA; YEMHLGS; -. DR OrthoDB; 96at2759; -. DR BRENDA; 2.4.1.18; 4460. DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation. DR UniPathway; UPA00152; -. DR EvolutionaryTrace; Q01401; -. DR Proteomes; UP000000763; Chromosome 6. DR Proteomes; UP000059680; Chromosome 6. DR ExpressionAtlas; Q01401; baseline and differential. DR GO; GO:0009501; C:amyloplast; ISS:Gramene. 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; ISS:Gramene. 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; ISS:Gramene. 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:SF2; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME, 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. DR Genevisible; Q01401; OS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Amyloplast; Chloroplast; KW Direct protein sequencing; Glycosyltransferase; Plastid; KW Reference proteome; Starch biosynthesis; Transferase; Transit peptide. FT TRANSIT 1..64 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:1478924" FT CHAIN 65..820 FT /note="1,4-alpha-glucan-branching enzyme, FT chloroplastic/amyloplastic" FT /id="PRO_0000011148" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 409 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 464 FT /note="Proton donor" FT /evidence="ECO:0000250" FT VAR_SEQ 1..65 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12869764" FT /id="VSP_017510" FT CONFLICT 13 FT /note="A -> P (in Ref. 1; BAA01584)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="D -> G (in Ref. 8; AK068920)" FT /evidence="ECO:0000305" FT CONFLICT 738 FT /note="N -> S (in Ref. 4; AAP68993)" FT /evidence="ECO:0000305" FT CONFLICT 789 FT /note="E -> G (in Ref. 4; AAP68993)" FT /evidence="ECO:0000305" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:3AMK" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 83..88 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 89..110 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 113..116 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 117..121 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 131..137 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 142..148 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:7ML5" FT STRAND 166..173 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 185..192 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 220..224 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 247..253 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 265..271 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 273..278 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 283..288 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 303..308 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 315..327 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 349..352 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 366..369 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 372..375 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 384..401 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 405..408 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 411..415 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 417..422 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 439..455 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 460..463 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 470..473 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 491..501 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 504..506 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 509..517 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 532..536 FT /evidence="ECO:0007829|PDB:3VU2" FT HELIX 542..547 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 550..553 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 556..559 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 563..583 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 585..590 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 593..595 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 606..608 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 619..623 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 629..646 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 654..660 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 661..664 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 665..670 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 673..678 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 685..694 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 696..703 FT /evidence="ECO:0007829|PDB:3AML" FT HELIX 707..709 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 724..726 FT /evidence="ECO:0007829|PDB:7ML5" FT HELIX 732..734 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 739..747 FT /evidence="ECO:0007829|PDB:3AML" FT STRAND 751..757 FT /evidence="ECO:0007829|PDB:3AML" FT TURN 760..762 FT /evidence="ECO:0007829|PDB:3AML" SQ SEQUENCE 820 AA; 93236 MW; 7DE65880013A7B15 CRC64; MLCLTSSSSS APAPLLPSLA DRPSPGIAGG GGNVRLSVVS SPRRSWPGKV KTNFSVPATA RKNKTMVTVV EEVDHLPIYD LDPKLEEFKD HFNYRIKRYL DQKCLIEKHE GGLEEFSKGY LKFGINTVDG ATIYREWAPA AQEAQLIGEF NNWNGAKHKM EKDKFGIWSI KISHVNGKPA IPHNSKVKFR FRHGGGAWVD RIPAWIRYAT FDASKFGAPY DGVHWDPPAC ERYVFKHPRP PKPDAPRIYE AHVGMSGEEP EVSTYREFAD NVLPRIRANN YNTVQLMAIM EHSYYASFGY HVTNFFAVSS RSGTPEDLKY LVDKAHSLGL RVLMDVVHSH ASNNVTDGLN GYDVGQNTHE SYFHTGDRGY HKLWDSRLFN YANWEVLRFL LSNLRYWMDE FMFDGFRFDG VTSMLYHHHG INKGFTGNYK EYFSLDTDVD AIVYMMLANH LMHKLLPEAT IVAEDVSGMP VLCRPVDEGG VGFDFRLAMA IPDRWIDYLK NKEDRKWSMS EIVQTLTNRR YTEKCIAYAE SHDQSIVGDK TIAFLLMDKE MYTGMSDLQP ASPTINRGIA LQKMIHFITM ALGGDGYLNF MGNEFGHPEW IDFPREGNNW SYDKCRRQWS LVDTDHLRYK YMNAFDQAMN ALEEEFSFLS SSKQIVSDMN EKDKVIVFER GDLVFVFNFH PNKTYKGYKV GCDLPGKYRV ALDSDALVFG GHGRVGHDVD HFTSPEGMPG VPETNFNNRP NSFKVLSPPR TCVAYYRVDE DREELRRGGA VASGKIVTEY IDVEATSGET ISGGWKGSEK DDCGKKGMKF VFRSSDEDCK //