1A16_ORYSJ
ID 1A16_ORYSJ Reviewed; 542 AA.
AC Q9SNN8; A0A0P0WSK8; A0A0U5BZC1; B9FRB5;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 6 {ECO:0000303|PubMed:17012402};
DE Short=ACC synthase 6 {ECO:0000303|PubMed:17012402};
DE Short=OsACS6 {ECO:0000303|PubMed:17012402};
DE EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
DE AltName: Full=Protein SUBSTANDARD STARCH GRAIN 6 {ECO:0000303|PubMed:26792122};
GN Name=ACS6 {ECO:0000303|PubMed:17012402};
GN Synonyms=ACC6 {ECO:0000305}, SSG6 {ECO:0000303|PubMed:26792122};
GN OrderedLocusNames=Os06g0130400 {ECO:0000312|EMBL:BAS95974.1},
GN LOC_Os06g03990 {ECO:0000305};
GN ORFNames=OsJ_19995 {ECO:0000312|EMBL:EEE65026.1},
GN P0493C11.5 {ECO:0000312|EMBL:BAA84790.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26792122; DOI=10.1104/pp.15.01811;
RA Matsushima R., Maekawa M., Kusano M., Tomita K., Kondo H., Nishimura H.,
RA Crofts N., Fujita N., Sakamoto W.;
RT "Amyloplast membrane protein SUBSTANDARD STARCH GRAIN6 controls starch
RT grain size in rice endosperm.";
RL Plant Physiol. 170:1445-1459(2016).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [7]
RP TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=17012402; DOI=10.1104/pp.106.085258;
RA Iwai T., Miyasaka A., Seo S., Ohashi Y.;
RT "Contribution of ethylene biosynthesis for resistance to blast fungus
RT infection in young rice plants.";
RL Plant Physiol. 142:1202-1215(2006).
CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC a direct precursor of ethylene in higher plants (By similarity).
CC Required for the regulation of starch grain size in endosperm
CC (PubMed:26792122). {ECO:0000250|UniProtKB:P37821,
CC ECO:0000269|PubMed:26792122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC ChEBI:CHEBI:59789; EC=4.4.1.14;
CC Evidence={ECO:0000250|UniProtKB:P37821};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P37821};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast membrane
CC {ECO:0000269|PubMed:26792122}. Note=Localizes to the amyloplast
CC membrane surrounding starch grains in endosperm, pollen, and pericarp.
CC {ECO:0000269|PubMed:26792122}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:17012402}.
CC -!- DISRUPTION PHENOTYPE: Enlarged starch grains in endosperm, spherical
CC starch grains in pollen, decreased number of chloroplasts in leaves,
CC enlarged chloroplasts with increased number of starch granules in
CC leaves, reduced number of total panicles and slight reduction of seed
CC weight. {ECO:0000269|PubMed:26792122}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; LC050636; BAU36891.1; -; mRNA.
DR EMBL; AP000559; BAA84790.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18603.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95974.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65026.1; -; Genomic_DNA.
DR EMBL; AK065212; BAG89419.1; -; mRNA.
DR RefSeq; XP_015644133.1; XM_015788647.1.
DR AlphaFoldDB; Q9SNN8; -.
DR SMR; Q9SNN8; -.
DR STRING; 4530.OS06T0130400-01; -.
DR PaxDb; Q9SNN8; -.
DR PRIDE; Q9SNN8; -.
DR EnsemblPlants; Os06t0130400-01; Os06t0130400-01; Os06g0130400.
DR GeneID; 4340002; -.
DR Gramene; Os06t0130400-01; Os06t0130400-01; Os06g0130400.
DR KEGG; osa:4340002; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9SNN8; -.
DR OMA; KKLTRFC; -.
DR OrthoDB; 1156861at2759; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0033097; C:amyloplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Amyloplast; Ethylene biosynthesis; Lyase; Membrane; Plastid;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..542
FT /note="1-aminocyclopropane-1-carboxylate synthase 6"
FT /id="PRO_0000455673"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P37821"
FT CONFLICT 224
FT /note="V -> M (in Ref. 1; BAU36891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 59475 MW; 6CA6F08B63E4BD42 CRC64;
MRRSGNGGAA KKKKKRSASA ASERRPRADG GMRIVVPLQG VVQGRGGLVL GSLIPCALFY
FFQLYIKRNR ASPPPPPGSP TAASAAAVSP IHRSLSRGLL APRAALPAIS ARGASVRDDD
SLYYAGLRRC AADPYHPVTN PSGIIQLGLA ENYLSLDLVG RWMEEHAAEA ASMAGGEDED
ERELSIRGLA AYQPYDGILA LKMALAGFMR QIMQGSVSFE PSQVVITSGA TPAMEILSFC
LADPGNAFLV PSPYYPGWDR DIKWRTGIEL IPVPCRSTDN FNISITALEI AYNQAKKRGI
KVRGVLISNP NNPTGSFVPK QTLHDLLEFA AEKNIHLISD EVFAGSTYGS GKFVSVAEVV
DDLEDFDKGR VHIIYGLSKD LSLAGFRVGV IYSYNESIVT AAAKIARFSS VSTPTQRLLV
AMLSDQKFIS DYLKVNRERL RKMYHLFVDA LDQVGIECYK SSGGFYCWAD MSKFIRSYSE
KGERKLWDRL LEEAKVNVTP GSSCHCIEPG WFRCCFTTLS EHDIPVLVQR LRTITDSHKP
NH
