ISOA1_ORYSJ
ID ISOA1_ORYSJ Reviewed; 803 AA.
AC D0TZF0; O80403; Q0J4C6; Q84L53;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Isoamylase 1, chloroplastic {ECO:0000305};
DE Short=OsISA1 {ECO:0000303|PubMed:15618430};
DE EC=3.2.1.68 {ECO:0000269|PubMed:10333591};
DE AltName: Full=Protein SUGARY-1 {ECO:0000303|PubMed:15618430};
DE Flags: Precursor;
GN Name=ISA1 {ECO:0000303|PubMed:10333591};
GN Synonyms=ISA {ECO:0000303|PubMed:20018713},
GN SU1 {ECO:0000303|PubMed:15618430};
GN OrderedLocusNames=Os08g0520900 {ECO:0000312|EMBL:BAT06299.1},
GN LOC_Os08g40930 {ECO:0000305};
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 [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=12834068; DOI=10.1139/g02-130;
RA Rahman S., Nakamura Y., Li Z., Clarke B., Fujita N., Mukai Y., Yamamoto M.,
RA Regina A., Tan Z., Kawasaki S., Morell M.;
RT "The sugary-type isoamylase gene from rice and Aegilops tauschii:
RT characterization and comparison with maize and arabidopsis.";
RL Genome 46:496-506(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=20018713; DOI=10.1073/pnas.0912396106;
RA Tian Z., Qian Q., Liu Q., Yan M., Liu X., Yan C., Liu G., Gao Z., Tang S.,
RA Zeng D., Wang Y., Yu J., Gu M., Li J.;
RT "Allelic diversities in rice starch biosynthesis lead to a diverse array of
RT rice eating and cooking qualities.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:21760-21765(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Tainung 78;
RA Wei F.-J., Lin Y.-R., Hsing Y.-I.;
RT "Oryza sativa japonica TNG78 ISA1 gene, complete gene and upstream +
RT downstream 1K region genomic sequence.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
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 [7]
RP PROTEIN SEQUENCE OF 55-85; 81-90; 392-401; 424-433 AND 489-498, NUCLEOTIDE
RP SEQUENCE [MRNA] OF 79-803, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Endosperm;
RX PubMed=10333591; DOI=10.1007/s004250050560;
RA Fujita N., Kubo A., Francisco P.B., Nakakita M., Harada K., Minaka N.,
RA Nakamura Y.;
RT "Purification, characterization, and cDNA structure of isoamylase from
RT developing endosperm of rice.";
RL Planta 208:283-293(1999).
RN [8]
RP FUNCTION.
RX PubMed=10517831; DOI=10.1104/pp.121.2.399;
RA Kubo A., Fujita N., Harada K., Matsuda T., Satoh H., Nakamura Y.;
RT "The starch-debranching enzymes isoamylase and pullulanase are both
RT involved in amylopectin biosynthesis in rice endosperm.";
RL Plant Physiol. 121:399-410(1999).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15618430; DOI=10.1104/pp.104.051359;
RA Kubo A., Rahman S., Utsumi Y., Li Z., Mukai Y., Yamamoto M., Ugaki M.,
RA Harada K., Satoh H., Konik-Rose C., Morell M., Nakamura Y.;
RT "Complementation of sugary-1 phenotype in rice endosperm with the wheat
RT isoamylase1 gene supports a direct role for isoamylase1 in amylopectin
RT biosynthesis.";
RL Plant Physiol. 137:43-56(2005).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16953433; DOI=10.1007/s00425-006-0331-z;
RA Utsumi Y., Nakamura Y.;
RT "Structural and enzymatic characterization of the isoamylase1 homo-oligomer
RT and the isoamylase1-isoamylase2 hetero-oligomer from rice endosperm.";
RL Planta 225:75-87(2006).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21436381; DOI=10.1104/pp.111.173435;
RA Utsumi Y., Utsumi C., Sawada T., Fujita N., Nakamura Y.;
RT "Functional diversity of isoamylase oligomers: the ISA1 homo-oligomer is
RT essential for amylopectin biosynthesis in rice endosperm.";
RL Plant Physiol. 156:61-77(2011).
RN [12]
RP INTERACTION WITH FLO6/SIP4.
RX PubMed=24456533; DOI=10.1111/tpj.12444;
RA Peng C., Wang Y., Liu F., Ren Y., Zhou K., Lv J., Zheng M., Zhao S.,
RA Zhang L., Wang C., Jiang L., Zhang X., Guo X., Bao Y., Wan J.;
RT "FLOURY ENDOSPERM6 encodes a CBM48 domain-containing protein involved in
RT compound granule formation and starch synthesis in rice endosperm.";
RL Plant J. 77:917-930(2014).
CC -!- FUNCTION: Starch-debranching enzyme involved in amylopectin
CC biosynthesis in endosperm. Functions by removing excess branches or
CC improper branches that interfere with the formation of double helices
CC of the cluster chains of amylopectin and crystallization of starch
CC (PubMed:10517831, PubMed:15618430, PubMed:16953433, PubMed:21436381).
CC Works as ISA1 homooligomer or together with ISA2 as heterooligomer. The
CC heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1
CC homooligomer for various branched polyglucans in vitro, but no marked
CC differences exist in chain preferences for debranching of amylopectin
CC and phytoglycogen between these forms (PubMed:16953433,
CC PubMed:21436381). {ECO:0000269|PubMed:10517831,
CC ECO:0000269|PubMed:15618430, ECO:0000269|PubMed:16953433,
CC ECO:0000269|PubMed:21436381}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68;
CC Evidence={ECO:0000269|PubMed:10333591};
CC -!- ACTIVITY REGULATION: Inhibited by copper chloride, mercury chloride,
CC ammonium molybdate and para-chloromercuribenzoate.
CC {ECO:0000269|PubMed:10333591}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 at 30 degrees Celsius.
CC {ECO:0000269|PubMed:10333591};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Forms a homo-pentamer and a hetero-hexamer composed of five
CC ISA1 and one ISA2 (PubMed:16953433). Interacts with FLO6/SIP4
CC (PubMed:24456533). {ECO:0000269|PubMed:16953433,
CC ECO:0000269|PubMed:24456533}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing endosperm. Expressed
CC at low levels in leaves. {ECO:0000269|PubMed:15618430}.
CC -!- DISRUPTION PHENOTYPE: Replacement of endosperm starch by a water-
CC soluble highly and randomly branched polysaccharide structure called
CC phytoglycogen. {ECO:0000269|PubMed:15618430}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29041.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC75533.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAF24185.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAT06299.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB093426; BAC75533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; GQ150871; ACY56086.1; -; Genomic_DNA.
DR EMBL; GQ150872; ACY56087.1; -; Genomic_DNA.
DR EMBL; GQ150873; ACY56088.1; -; Genomic_DNA.
DR EMBL; GQ150874; ACY56089.1; -; Genomic_DNA.
DR EMBL; GQ150875; ACY56090.1; -; Genomic_DNA.
DR EMBL; GQ150876; ACY56091.1; -; Genomic_DNA.
DR EMBL; KF984388; AII21927.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24185.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014964; BAT06299.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB015615; BAA29041.1; ALT_FRAME; mRNA.
DR RefSeq; XP_015650242.1; XM_015794756.1.
DR AlphaFoldDB; D0TZF0; -.
DR SMR; D0TZF0; -.
DR STRING; 4530.OS08T0520900-00; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; D0TZF0; -.
DR EnsemblPlants; Os08t0520900-01; Os08t0520900-01; Os08g0520900.
DR GeneID; 4346068; -.
DR Gramene; Os08t0520900-01; Os08t0520900-01; Os08g0520900.
DR KEGG; osa:4346068; -.
DR eggNOG; KOG0470; Eukaryota.
DR OrthoDB; 533388at2759; -.
DR BRENDA; 3.2.1.68; 4460.
DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0010368; C:chloroplast isoamylase complex; IEA:EnsemblPlants.
DR GO; GO:0043033; C:isoamylase complex; IDA:UniProtKB.
DR GO; GO:0019156; F:isoamylase activity; IDA:UniProtKB.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chloroplast; Direct protein sequencing;
KW Glycosidase; Hydrolase; Plastid; Reference proteome; Starch biosynthesis;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10333591"
FT CHAIN 55..803
FT /note="Isoamylase 1, chloroplastic"
FT /id="PRO_0000441798"
FT ACT_SITE 432
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 561
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
SQ SEQUENCE 803 AA; 89661 MW; 9DC80176A72292E0 CRC64;
MASLPHCLSA RPLVVAAAPG RPGPGPGPWL RGGARRRNAA FSAGNAGRRV GLRRSVASAV
EVGVGEDEEE GVEEEEEEVE AVVMPERYAL GGACRVLAGM PAPLGATALD GGVNFAVYSA
GASAASLCLF TPDDLEADEV TEEVPLDPLF NRTGNVWHVF IEGELHNMLY GYRFDGMFAP
HCGQYFDVSN VVVDPYAKAV ISRGEYGVPG PGGDCWPQMA GMIPLPYSTF DWQGDLPLRY
PQKDLVIYEM HLRGFTKHSS SNVEHPGTYI GAISKLDYLK ELGVNCVELM PCHEFNELEY
FSCSSKMNFW GYSTINFFSP MIRYSSGGIR NCGRDAINEF KTFVREAHKR GIEVIMDVVF
NHTAEGNEKG PILSFRGIDN STYYMLAPKG EFYNYSGCGN TFNCNHPVVR EFIVDCLRYW
VTEMHVDGFR FDLASIMTRG CSLWDPVNVY GSPVEGDMTT TGTPLATPPL IDMISNDPIL
GDVKLIAEAW DAGGLYQVGQ FPHWKIWSEW NGKYRDIVRQ FIKGTDGFAG GFAECLCGSP
HLYQAGGRKP WHSINFVCAH DGFTLADLVT YNKKYNSSNG EDNRDGENHN LSWNCGEEGE
FAGLSVKRLR KRQMRNFFVS LMVSQGVPMF YMGDEYGHTK GGNNNTYCHD HYVNYFRWDK
KEESSDLQRF CSLMTKFRKQ CESLGLADFP TAQRLHWHGH QPGKPDWSET SRFVAFSTKD
ETKGEIYVAF NASHLPAVVG LPERPGYRWE PLVDTGKPAP YDFLTDDLPD RAHAVHLFSH
FLNSNLYPML SYSSIILELQ PDD
