ALF_NEUCR
ID ALF_NEUCR Reviewed; 362 AA.
AC P53444; A7UX41; Q7S1C1; V5IKX9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
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=fba; ORFNames=NCU07807;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=74A;
RA Yamashita R., Stuart W.D.;
RT "DNA sequence of fructose-1,6-bisphosphate aldolase in N. crassa.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
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DR EMBL; L42380; AAB00930.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42348.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42349.1; -; Genomic_DNA.
DR PIR; T47260; T47260.
DR RefSeq; XP_011394728.1; XM_011396426.1.
DR RefSeq; XP_011394729.1; XM_011396427.1.
DR AlphaFoldDB; P53444; -.
DR SMR; P53444; -.
DR STRING; 5141.EFNCRP00000007989; -.
DR PRIDE; P53444; -.
DR EnsemblFungi; ESA42348; ESA42348; NCU07807.
DR EnsemblFungi; ESA42349; ESA42349; NCU07807.
DR GeneID; 3874540; -.
DR KEGG; ncr:NCU07807; -.
DR VEuPathDB; FungiDB:NCU07807; -.
DR HOGENOM; CLU_036923_1_0_1; -.
DR InParanoid; P53444; -.
DR OMA; PRTWGKL; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central.
DR GO; GO:1904408; F:melatonin binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178759"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
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"
FT CONFLICT 1..15
FT /note="MGIFDELNLPAGVLY -> MRCPIPEHKQNLTFSLPL (in Ref. 1;
FT AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..59
FT /note="II -> SS (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="G -> C (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..84
FT /note="REA -> ARD (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="L -> RI (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..126
FT /note="PWLDGML -> FGDGIP (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..212
FT /note="AF -> DS (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="A -> G (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="E -> D (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="H -> Q (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> P (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> F (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..360
FT /note="ALKDFNAAG -> GPQGPSNTTV (in Ref. 1; AAB00930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 39889 MW; C402186EEEBD9368 CRC64;
MGIFDELNLP AGVLYGDDVL KLFQYAREKQ FAIPACNVTS SSTAVAALEA ARDQKAPIIL
QTSQGGAAFF AGKGIKDSAE KREASVAGAI AAAHYIRSIA PIYGIPVVLH TDHCAKKLLP
WLDGMLEEDE KFFKANGVPL FSSHMIDLSE EPVEENISTC VKYLKRMAPM KQWLEMEIGI
TGGEEDGVDN SEVDNASLYT QPEDIWQIEE AFRPISPYFS IAAGFGNVHG VYAPGNVKLH
PELLGKHQAY VSEKLGGKDK KPVFFVFHGG SGSSKEEYRE AISNGVVKVN VDTDLQWSYL
VGIRDYILNN IDYLRSQVGN PEGPNKPNKK KYDPRVWIRE GEKTMKARVE EALKDFNAAG
TV
