ALF_ASPOR
ID ALF_ASPOR Reviewed; 362 AA.
AC Q9HGY9; Q2UKP5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fbaA; ORFNames=AO090003000725;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Nakajima K., Kunihiro S., Sano M., Eto S., Machida M.;
RT "Molecular cloning and characterization of glycolytic gene from Aspergillus
RT oryzae.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB12232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB032272; BAB12232.1; ALT_FRAME; mRNA.
DR EMBL; AP007155; BAE57870.1; -; Genomic_DNA.
DR RefSeq; XP_001819872.1; XM_001819820.2.
DR AlphaFoldDB; Q9HGY9; -.
DR SMR; Q9HGY9; -.
DR STRING; 510516.Q9HGY9; -.
DR PRIDE; Q9HGY9; -.
DR EnsemblFungi; BAE57870; BAE57870; AO090003000725.
DR GeneID; 5991855; -.
DR KEGG; aor:AO090003000725; -.
DR VEuPathDB; FungiDB:AO090003000725; -.
DR HOGENOM; CLU_036923_1_0_1; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:1904408; F:melatonin binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 2: Evidence at transcript level;
KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178756"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 269..271
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 290..293
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 39721 MW; 636526911421E17E CRC64;
MGVGVLEKLS RKTGVIVGDD VLRLFEHAQQ NNYAIPAVNV TSSSTVVASL EAARDQNCPI
VLQLSQGGAA YFAGKGVSND GQQASIAGGI AAAHYIRSLA PAYGIPVVLH TDHCAKKLLP
WLDGLLDEDE RYFKLHGEPL FSSHMIDLSE EPVDYNIQTT AAYLKRAAPM KQWLEMEIGI
TGGEEDGVNN EDVDNNSLYT QPEDILAIHK ALSPISPYFS IAAGFGNVHG VYKPGNVKLH
PELLKKHQAY VKEKIGSNKD KPVFFVFHGG SGSSKEEYKE AISYGVVKVN VDTDMQFAYM
SGIRDYILKK KDYLMTAVGN PEGEDKPNKK SFDPRVWVRE GEKTMSQRVK VALEDFNTAG
QL
