ALFP_ORYSJ
ID ALFP_ORYSJ Reviewed; 388 AA.
AC Q40677; Q2R9Z9; Q2RA00; Q2RA01; Q53P95; Q53P96; U5KP25;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Fructose-bisphosphate aldolase, chloroplastic {ECO:0000305};
DE EC=4.1.2.13 {ECO:0000305};
DE AltName: Full=Chloroplastic aldolase {ECO:0000303|PubMed:8163192};
DE Short=AldP {ECO:0000303|PubMed:8163192};
DE Flags: Precursor;
GN Name=ALDP {ECO:0000305};
GN OrderedLocusNames=Os11g0171300 {ECO:0000312|EMBL:BAT12868.1},
GN LOC_Os11g07020 {ECO:0000312|EMBL:ABA91630.2};
GN ORFNames=OsJ_33121 {ECO:0000312|EMBL:EAZ17583.1};
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 [GENOMIC DNA].
RX PubMed=8163192; DOI=10.1016/0378-1119(94)90574-6;
RA Tsutsumi K., Kagaya Y., Hidaka S., Suzuki J., Tokairin Y., Hirai T., Hu D.,
RA Ishikawa K., Ejiri S.;
RT "Structural analysis of the chloroplastic and cytoplasmic aldolase-encoding
RT genes implicated the occurrence of multiple loci in rice.";
RL Gene 141:215-220(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo; TISSUE=Seed;
RA Yoon U.H.;
RT "Structural and expression analysis of immature seed genes in Oryza sativa
RT L.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
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 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 [8]
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 [9]
RP TISSUE SPECIFICITY, AND INDUCTION BY LIGHT.
RX PubMed=1363521; DOI=10.1266/jjg.67.335;
RA Kwon S., Kikuchi S., Oono K.;
RT "Molecular cloning and characterization of gravity specific cDNA in rice
RT (Oryza sativa L.) suspension callus.";
RL Jpn. J. Genet. 67:335-348(1992).
RN [10]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 39-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=cv. Nipponbare;
RX PubMed=16758443; DOI=10.1002/pmic.200600043;
RA Nozu Y., Tsugita A., Kamijo K.;
RT "Proteomic analysis of rice leaf, stem and root tissues during growth
RT course.";
RL Proteomics 6:3665-3670(2006).
CC -!- FUNCTION: Plays a key role in glycolysis and gluconeogenesis.
CC {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000250|UniProtKB:Q9SJQ9};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q944G9}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000250|UniProtKB:Q9SJU4}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf mesophyll cells.
CC {ECO:0000269|PubMed:1363521}.
CC -!- INDUCTION: By exposure to light. {ECO:0000269|PubMed:1363521}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX95073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABA91631.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABA91632.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D13513; BAA02730.1; -; Genomic_DNA.
DR EMBL; JX972166; AGT38460.1; -; mRNA.
DR EMBL; AC128643; AAX95072.1; -; Genomic_DNA.
DR EMBL; AC128643; AAX95073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000010; ABA91630.2; -; Genomic_DNA.
DR EMBL; DP000010; ABA91631.2; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000010; ABA91632.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008217; BAF27707.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT12868.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ17583.1; -; Genomic_DNA.
DR EMBL; AK104899; BAG97016.1; -; mRNA.
DR PIR; T03679; T03679.
DR RefSeq; XP_015616895.1; XM_015761409.1.
DR AlphaFoldDB; Q40677; -.
DR SMR; Q40677; -.
DR IntAct; Q40677; 1.
DR STRING; 4530.OS11T0171300-01; -.
DR PaxDb; Q40677; -.
DR PRIDE; Q40677; -.
DR EnsemblPlants; Os11t0171300-01; Os11t0171300-01; Os11g0171300.
DR GeneID; 4349897; -.
DR Gramene; Os11t0171300-01; Os11t0171300-01; Os11g0171300.
DR KEGG; osa:4349897; -.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q40677; -.
DR OMA; EVASMVW; -.
DR OrthoDB; 799973at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q40677; OS.
DR GO; GO:0005737; C:cytoplasm; ISS:Gramene.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010287; C:plastoglobule; IEA:UniProtKB-SubCell.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Glycolysis; Lyase; Plastid;
KW Reference proteome; Schiff base; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16758443"
FT CHAIN 39..388
FT /note="Fructose-bisphosphate aldolase, chloroplastic"
FT /id="PRO_0000001112"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 257
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 388
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT CONFLICT 156
FT /note="L -> R (in Ref. 1; BAA02730)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="G -> A (in Ref. 1; BAA02730)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="A -> R (in Ref. 1; BAA02730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42006 MW; 4FFF6FAE1F6619E0 CRC64;
MASATLLKSS FLPKKSEWGA TRQAAAPKPV TVSMVVRAGA YDDELVKTAK TIASPGRGIL
AMDESNATCG KRLASIGLEN TEANRQAYRT LLVTAPGLGQ YISGAILFEE TLYQSTVDGK
KIVDILTEQK IVPGIKVDKG LVPLAGSNNE SWCQGLDGLA SREAAYYQQG ARFAKWRTVV
SIPNGPSELA VKEAAWGLAR YAAISQDNGL VPIVEPEILL DGEHGIDRTF EVAQKVWAET
FFYMAENNVM FEGILLKPSM VTPGAECKDR ATPEQVSDYT LKLLHRRIPP AVPGIMFLSG
GQSEVEATQN LNAMNQGPNP WHVSFSYARA LQNTCLKTWG GQPENVKAAQ DALLLRAKAN
SLAQLGKYTS DGEAAEAKEG MFVKNYVY
