SU1_MAIZE
ID SU1_MAIZE Reviewed; 789 AA.
AC O22637; A0A1D6PXQ9; B6U0X5; Q41742;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Isoamylase SU1, chloroplastic {ECO:0000305};
DE EC=3.2.1.68 {ECO:0000269|PubMed:9625695};
DE AltName: Full=Protein SUGARY 1 {ECO:0000303|PubMed:7773016};
DE Flags: Precursor;
GN Name=SU1 {ECO:0000303|PubMed:7773016};
GN ORFNames=ZEAMMB73_Zm00001d049753 {ECO:0000312|EMBL:AQK51280.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Endosperm;
RX PubMed=7773016; DOI=10.2307/3870080;
RA James M.G., Robertson D.S., Myers A.M.;
RT "Characterization of the maize gene sugary1, a determinant of starch
RT composition in kernels.";
RL Plant Cell 7:417-429(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Beatty M.K., Myers A.M., James M.G.;
RT "Genomic nucleotide sequence of a full-length wild-type allele of the maize
RT sugary1 (Su1) gene.";
RL Plant Physiol. 115:1731-1731(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9625695; DOI=10.1104/pp.117.2.425;
RA Rahman A., Wong K.S., Jane J.L., Myers A.M., James M.G.;
RT "Characterization of SU1 isoamylase, a determinant of storage starch
RT structure in maize.";
RL Plant Physiol. 117:425-435(1998).
CC -!- FUNCTION: Isoamylase starch-debranching enzyme involved in amylopectin
CC biosynthesis in endosperm (PubMed:7773016, PubMed:9625695). Functions
CC by removing excess branches or improper branches that interfere with
CC the formation of double helices of the cluster chains of amylopectin
CC and crystallization of starch (PubMed:9625695).
CC {ECO:0000269|PubMed:7773016, ECO:0000269|PubMed:9625695}.
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:9625695};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:9625695};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:9625695};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: During endosperm development, expressed in kernels
CC from 10 to 30 days after pollination (at protein level).
CC {ECO:0000269|PubMed:9625695}.
CC -!- DISRUPTION PHENOTYPE: In maize kernels, mutations in SU1 result in,
CC increased sucrose concentration, decreased concentration of
CC amylopectin, the branched component of starch, and accumulation of the
CC highly branched glucopolysaccharide phytoglycogen.
CC {ECO:0000269|PubMed:7773016}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA91298.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AQK51280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U18908; AAA91298.1; ALT_INIT; mRNA.
DR EMBL; AF030882; AAB97167.1; -; Genomic_DNA.
DR EMBL; CM000780; AQK51280.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU970890; ACG43008.1; -; mRNA.
DR PIR; T01321; T01321.
DR RefSeq; XP_008678357.1; XM_008680135.1.
DR AlphaFoldDB; O22637; -.
DR SMR; O22637; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; O22637; -.
DR PRIDE; O22637; -.
DR EnsemblPlants; Zm00001eb174590_T001; Zm00001eb174590_P001; Zm00001eb174590.
DR GeneID; 542318; -.
DR Gramene; Zm00001eb174590_T001; Zm00001eb174590_P001; Zm00001eb174590.
DR KEGG; zma:542318; -.
DR MaizeGDB; 112979; -.
DR HOGENOM; CLU_011725_1_1_1; -.
DR OrthoDB; 533388at2759; -.
DR BRENDA; 3.2.1.68; 6752.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; O22637; baseline and differential.
DR GO; GO:0010368; C:chloroplast isoamylase complex; IEA:EnsemblPlants.
DR GO; GO:0019156; F:isoamylase activity; IEA:EnsemblPlants.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005983; P:starch catabolic process; IEA:EnsemblPlants.
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 Chloroplast; Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..789
FT /note="Isoamylase SU1, chloroplastic"
FT /id="PRO_0000455589"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 473
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 546
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT CONFLICT 112
FT /note="C -> S (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="Q -> E (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Y -> C (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="V -> E (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="N -> G (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="N -> F (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="K -> E (in Ref. 1; AAA91298)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="G -> E (in Ref. 4; ACG43008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 88353 MW; F3046F120834EBC4 CRC64;
MAQQLPCVSS PRPLLAVPAG RWRAGVRGRP NVAGLGRGRL SLHAAAARPV AEAVQAEEDD
DDDDEEVAEE RFALGGACRV LAGMPAPLGA TALRGGVNFA VYSSGASAAS LCLFAPGDLK
ADRVTEEVPL DPLLNRTGNV WHVFIHGDQL HGMLYGYRFD GVFAPERGQY YDVSNVVVDP
YAKAVVSRGE YGVPAPGGSC WPQMAGMIPL PYNKFDWQGD LPLGYHQKDL VIYEMHLRGF
TKHNSSKTKH PGTYIGAVSK LDHLKELGVN CIELMPCHEF NELEYFSSSS KMNFWGYSTI
NFFSPMARYS SSGIRDSGCG AINEFKAFVR EAHKRGIEVI MDVVFNHTAE GNEKGPILSF
RGIDNSTYYM LAPKGEFYNY SGCGNTFNCN HPVVREFIVD CLRYWVTEMH VDGFRFDLAS
ILTRGCSLWD PVNVYGSPME GDMITTGTPL VAPPLIDMIS NDPILGNVKL IAEAWDAGGL
YQVGQFPHWN VWSEWNGKYR DTVRQFIKGT DGFAGAFAEC LCGSPQLYQA GGRKPWHSIN
FVCAHDGFTL ADLVTYNSKY NLSNGEDNRD GENHNLSWNC GEEGEFASLS VRRLRKRQMR
NFFVCLMVSQ GVPMFYMGDE YGHTKGGNNN TYCHDHYVNY FRWDKKEEQS SDLYRFCRLM
TKFRKECESL GLEDFPTSER LKWHGHQPGK PDWSEASRFV AFTMKDETKG EIYVAFNTSH
LPVVVGLPER SGFRWEPVVD TGKEAPYDFL TDGLPDRAVT VYQFSHFLNS NLYPMLSYSS
IILVLRPDV
