GLGB_ORYSJ
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 03-AUG-2022, entry version 152.
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; 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. [Q01401-1]
DR RefSeq; XP_015643112.1; XM_015787626.1. [Q01401-2]
DR RefSeq; XP_015643113.1; XM_015787627.1. [Q01401-2]
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; 4530.OS06T0726400-01; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q01401; -.
DR PRIDE; Q01401; -.
DR EnsemblPlants; Os06t0726400-01; Os06t0726400-01; Os06g0726400. [Q01401-1]
DR GeneID; 4342117; -.
DR Gramene; Os06t0726400-01; Os06t0726400-01; Os06g0726400. [Q01401-1]
DR KEGG; osa:4342117; -.
DR eggNOG; KOG0470; Eukaryota.
DR InParanoid; Q01401; -.
DR OMA; FGMKWMM; -.
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 Genevisible; Q01401; OS.
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 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 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
