ALF2_PARBA
ID ALF2_PARBA Reviewed; 363 AA.
AC Q8J0N6; Q6PT81;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Fructose-bisphosphate aldolase 2;
DE Short=FBP aldolase 2;
DE Short=FBPA 2;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase 2;
GN Name=FBA2;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=15588996; DOI=10.1016/j.fgb.2004.10.003;
RA Carneiro L.C., de Faria F.P., Felipe M.S.S., Pereira M.,
RA de Almeida Soares C.M.;
RT "Paracoccidioides brasiliensis presents two different cDNAs encoding
RT homologues of the fructose 1,6-biphosphate aldolase: protein isolation,
RT cloning of the cDNAs and genes, structural, phylogenetic, and expression
RT analysis.";
RL Fungal Genet. Biol. 42:51-60(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 -!- INDUCTION: Only detected in the mycelia phase, but not in yeast cells.
CC {ECO:0000269|PubMed:15588996}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- CAUTION: The DNA coding for this protein is not found in the complete
CC genome of strain ATCC MYA-826 / Pb01. {ECO:0000305}.
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DR EMBL; AY172327; AAN85569.2; -; mRNA.
DR EMBL; AY581212; AAS99115.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8J0N6; -.
DR SMR; Q8J0N6; -.
DR PRIDE; Q8J0N6; -.
DR UniPathway; UPA00109; UER00183.
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 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 TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 2.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 2: Evidence at transcript level;
KW Glycolysis; Lyase; Metal-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..363
FT /note="Fructose-bisphosphate aldolase 2"
FT /id="PRO_0000178760"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 265..267
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 39770 MW; 929C731386F46D76 CRC64;
MGVKDLLSRK TGVIVGDDVL RLFQHAQENV FAIPAIMVTS SSTGSALEAA RDKSPIVLQT
SNGAAYFAGK GKGVSNDGQS VAGSIAIAAA HYIRSQAPAY GIPVVLHTDH CAKKLLPWLD
GMLDADECYS KLHNEPLFSS HMIDLSEESV EWNIETTAKY LKRAAPMKQW LEMEIGITGG
EEDGVNNESV DNNSLYTQPE DIYTIYKTLS AISPYFSIAA GFGNVHGVYR GDIALRPLLR
HLHNAKYDEQ LKCLQDPLGF FVFHGGSGSS HQPATSITSE FAAKGRVDLE KVAYLPGTSS
LVIAPKDYLM SPYGIPVVLH TDHCKYFDPR VQIREGLKHM SARVQEAKDD FNDSNQAKKL
LPW
