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   13-SEP-2023, entry version 118.
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   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   OrthoDB; 275443at2759; -.
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; 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   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
//