ISOA2_ORYSJ
ID ISOA2_ORYSJ Reviewed; 800 AA.
AC Q6AU80; A0A0P0WM70; B9FHZ3; Q0DIF3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Isoamylase 2, chloroplastic {ECO:0000305};
DE Short=OsISA2 {ECO:0000303|PubMed:15618430};
DE EC=3.2.1.68 {ECO:0000269|PubMed:16953433};
DE Flags: Precursor;
GN Name=ISA2 {ECO:0000303|PubMed:15618430};
GN OrderedLocusNames=Os05g0393700 {ECO:0000312|EMBL:BAS93869.1},
GN LOC_Os05g32710 {ECO:0000305};
GN ORFNames=OsJ_17304 {ECO:0000312|EMBL:EEE62506.1},
GN OSJNBa0014C03.3 {ECO:0000312|EMBL:AAT93894.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP PROTEIN SEQUENCE OF 35-44, FUNCTION, CATALYTIC ACTIVITY, 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 [8]
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).
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:16953433, PubMed:21436381). Works together with ISA1 as
CC heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher
CC affinity than the ISA1 homooligomer for various branched polyglucans in
CC vitro, but no marked differences exist in chain preferences for
CC debranching of amylopectin and phytoglycogen between these forms
CC (PubMed:16953433, PubMed:21436381). {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:21436381};
CC -!- SUBUNIT: Forms a hetero-hexamer composed of five ISA1 and one ISA2.
CC {ECO:0000269|PubMed:16953433}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in developing endosperm and
CC leaves. {ECO:0000269|PubMed:15618430}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF17370.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS93869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE62506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC132483; AAT93894.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17370.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014961; BAS93869.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000142; EEE62506.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015637296.1; XM_015781810.1.
DR AlphaFoldDB; Q6AU80; -.
DR SMR; Q6AU80; -.
DR STRING; 4530.OS05T0393700-01; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q6AU80; -.
DR GeneID; 4338695; -.
DR KEGG; osa:4338695; -.
DR eggNOG; KOG0470; Eukaryota.
DR HOGENOM; CLU_011725_2_0_1; -.
DR InParanoid; Q6AU80; -.
DR OrthoDB; 533388at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR CDD; cd11346; AmyAc_plant_IsoA; 1.
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; IPR044096; AmyAc_plant_ISA2.
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..34
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16953433"
FT CHAIN 35..800
FT /note="Isoamylase 2, chloroplastic"
FT /id="PRO_0000441799"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 276
FT /note="R -> K (in Ref. 5; EEE62506)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="K -> N (in Ref. 5; EEE62506)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="R -> G (in Ref. 5; EEE62506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 800 AA; 86530 MW; 97F4019B0783508A CRC64;
MASLPAPPTP LGSCPRGRGG GRVVARPRRA GLACAARSCY RFRTDDDGVV DVAVSGEDGD
GGGGGYAVSV EVPGTRGREG GLVLRASGSG EGVPLAPAAG GASLAAELSF DPTRAPFYLS
FLLTDASGAE IRTHRKTSFR VPVGVGPGSP APLGMSISGD GAVNFAVYSK NANAVSLYLY
AAAVGGGGGD EPALEIDLDP YIHRTGNVWH VSLASVDGYV SYAFCCGGIR RPLLDPYAKV
IGDFVSSNSV YDEGVTAPSM RCFASLAIAP SYNWGRDRHP RLPLEKLVVY RANVALFTKD
RSSGLPDDAA GTFTGLSAKV EHFRSLGVNA ILLEPVFPFH QVKGPYFPYH FFSPMNLYSS
KGLSVSAIKS MKDMVRVMHR NGIEVLLEVV FTHTAEGESE CQTISMRGID NSSYYIANGI
AGCKASILNC NHPVTQKLIL DSLRHWVLDF HVDGFCFINA PFLVRGPGGE YLSRPPLLEA
ITFDPVLSMT KIIADPWSPL DISNVQFPFP HWKRWAEVNT RFSIDVRKFL KREALISDLA
TRLCGSGDLF STRGPAFSFN HVSRNSGLSL VDLVSFSNDD LLSESSWNCG EEGPSENSAV
LQTRLRQIRN FLFILFVSLG VPVLNMGDEC GHSAAGSVSY KDRGPLNWRG MKTTFVKEVT
GFISFLTALR SRRGDIFQRR EFLKLENIHW YGSDLCEPGW DDPTSNFLCM HINAEVDEMA
ADSVRGDLYI CFNANEESVS AALPALAEGS VWLRLVDTSL AFPGFFATES NPKVQQVPGL
SSYHVEAHTC VLFESKSALA
