ID G4YN42_PHYSP Unreviewed; 358 AA.
AC G4YN42;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN ORFNames=PHYSODRAFT_284519 {ECO:0000313|EMBL:EGZ29837.1},
GN PHYSODRAFT_284520 {ECO:0000313|EMBL:EGZ29838.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ29837.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ29837.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EMBL:EGZ29837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ29837.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Aerts A., Grimwood J., Schmutz J., Lucas S., Hammon N., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Dehal P., Chapman J., Putman N.H.,
RA Salamov A.A., Terry A., Rokhsar D.S., Boore J.L., Tripathy S., Tyler B.M.,
RA Grigoriev I.V.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000256|ARBA:ARBA00002181}.
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:0000256|ARBA:ARBA00000441};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00005812}.
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DR EMBL; JH159151; EGZ29837.1; -; Genomic_DNA.
DR EMBL; JH159151; EGZ29838.1; -; Genomic_DNA.
DR RefSeq; XP_009517112.1; XM_009518817.1.
DR RefSeq; XP_009517113.1; XM_009518818.1.
DR AlphaFoldDB; G4YN42; -.
DR STRING; 1094619.G4YN42; -.
DR EnsemblProtists; EGZ29837; EGZ29837; PHYSODRAFT_284519.
DR EnsemblProtists; EGZ29838; EGZ29838; PHYSODRAFT_284520.
DR GeneID; 20639809; -.
DR GeneID; 20639810; -.
DR KEGG; psoj:PHYSODRAFT_284519; -.
DR KEGG; psoj:PHYSODRAFT_284520; -.
DR InParanoid; G4YN42; -.
DR OMA; HIDFVFH; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 358 AA; 39325 MW; 70AE6028391416A0 CRC64;
MGLLDIVQPG VLNGEDVVKV YKYAQEHNFA IPAVNVTSSS TANAALQAAR DIKSPIIIQT
SNGGAAFYAG KGIDNKNQNG SILGAIAAAY HVRAMAAHYG VPVILHSDHC AKKLLPWFDG
MLEADEKYFK EHGVPLWSSH MLDLSEEPME ENVAISKKYF ERMAKMNLIL EVELGITGGE
EDGVDNSEVD NASLYSQPED ILLAYNELGA VSPYFTIAAA FGNVHGVYKP GNVKLHPEIL
GDFQKFVAKE KGLAAEKPVF FVFHGGSGST AQEIQTAVGN GVVKMNIDTD TQWAYWNGLR
KFYEDKKGYL QGQIGNPEGP DAPNKKYYDP RVWVRKSEES MIARLHEAYH NLNCVNVL
//
