ALFC2_ORYSJ
ID ALFC2_ORYSJ Reviewed; 358 AA.
AC Q10A30; Q40676;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Fructose-bisphosphate aldolase 2, cytoplasmic {ECO:0000305};
DE EC=4.1.2.13 {ECO:0000250|UniProtKB:Q9SJQ9};
DE AltName: Full=Cytoplasmic aldolase-alpha {ECO:0000303|PubMed:8163192};
DE Short=AldC-alpha {ECO:0000303|PubMed:8163192};
GN Name=FBA2 {ECO:0000305};
GN OrderedLocusNames=Os10g0163340 {ECO:0000312|EMBL:BAT10026.1},
GN LOC_Os10g08022 {ECO:0000312|EMBL:ABG65931.1};
GN ORFNames=OsJ_30817 {ECO:0000312|EMBL:EAZ15405.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [3]
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 [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).
CC -!- FUNCTION: Fructose-bisphosphate aldolase that plays a key role in
CC glycolysis and gluconeogenesis. {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: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9SJQ9}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; D13512; BAA02729.1; -; Genomic_DNA.
DR EMBL; DP000086; ABG65931.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT10026.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ15405.1; -; Genomic_DNA.
DR EMBL; AK071547; BAG92549.1; -; mRNA.
DR EMBL; AK099184; BAG93981.1; -; mRNA.
DR RefSeq; XP_015613786.1; XM_015758300.1.
DR AlphaFoldDB; Q10A30; -.
DR SMR; Q10A30; -.
DR STRING; 4530.OS10T0163340-01; -.
DR iPTMnet; Q10A30; -.
DR PaxDb; Q10A30; -.
DR PRIDE; Q10A30; -.
DR EnsemblPlants; Os10t0163340-01; Os10t0163340-01; Os10g0163340.
DR GeneID; 107277365; -.
DR Gramene; Os10t0163340-01; Os10t0163340-01; Os10g0163340.
DR KEGG; osa:107277365; -.
DR eggNOG; KOG1557; Eukaryota.
DR HOGENOM; CLU_031243_0_2_1; -.
DR OMA; THQDIAM; -.
DR OrthoDB; 799973at2759; -.
DR PlantReactome; R-OSA-1119519; Calvin cycle.
DR PlantReactome; R-OSA-1119570; Cytosolic glycolysis.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q10A30; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..358
FT /note="Fructose-bisphosphate aldolase 2, cytoplasmic"
FT /id="PRO_0000437242"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT ACT_SITE 225
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 266..268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT SITE 358
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250|UniProtKB:P00883"
FT CONFLICT 92
FT /note="V -> I (in Ref. 1; BAA02729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38705 MW; 74CCD519EB83F5BB CRC64;
MSAYCGKYKD ELIKNAAYIG TPGKGILAAD ESTGTIGKRF ASINVENVED NRRAFRELLF
CTPGALQYIS GVILFDETLY QKTKDGKPFV DVLKEAGALP GIKVDKGTIE VAGTDKETTT
QGHDDLGKQC AKYYEAGARF AKWRAVLKIG PNQPSQLAID LNAQGLACYA IICQENGLVP
IVEPEILVDG PHDIDRCAYV SEVVLAACYK ALNEHHVLLE GTLLKPNMVT PGSDAKKVAP
EVIAEYTVRT LQRTVPPAVP AIVFLSGGQS EEEATLNLNA MNKLSAKKPW SLSFSFGRAL
QQSTLKAWAG KTENVEKARA AFLVRCKANS EATLGTYKGD AVLGEGAAES LHVKDYKY
