ALF1_PARBA
ID ALF1_PARBA Reviewed; 360 AA.
AC Q96UH7; C1GU00; Q8X219;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Fructose-bisphosphate aldolase 1;
DE Short=FBP aldolase 1;
DE Short=FBPA 1;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase 1;
GN Name=FBA1; ORFNames=PAAG_01995;
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], PROTEIN SEQUENCE OF 328-339 AND
RP 343-359, AND INDUCTION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
RN [3]
RP PROTEIN SEQUENCE OF 2-37, AND INDUCTION.
RX PubMed=11418327; DOI=10.1016/s1286-4579(01)01409-5;
RA da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A.,
RA de Almeida Soares C.M.;
RT "Two-dimensional electrophoresis and characterization of antigens from
RT Paracoccidioides brasiliensis.";
RL Microbes Infect. 3:535-542(2001).
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: Preferentially expressed in yeast cells, the host parasitic
CC phase. {ECO:0000269|PubMed:11418327, ECO:0000269|PubMed:15588996}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AY057387; AAL25625.2; -; Genomic_DNA.
DR EMBL; AY233454; AAL34519.2; -; mRNA.
DR EMBL; KN293995; EEH39806.1; -; Genomic_DNA.
DR RefSeq; XP_002796107.1; XM_002796061.2.
DR AlphaFoldDB; Q96UH7; -.
DR SMR; Q96UH7; -.
DR STRING; 502779.Q96UH7; -.
DR PRIDE; Q96UH7; -.
DR EnsemblFungi; EEH39806; EEH39806; PAAG_01995.
DR GeneID; 9099250; -.
DR KEGG; pbl:PAAG_01995; -.
DR VEuPathDB; FungiDB:PAAG_01995; -.
DR eggNOG; KOG4153; Eukaryota.
DR HOGENOM; CLU_036923_0_0_1; -.
DR OMA; PRTWGKL; -.
DR OrthoDB; 773537at2759; -.
DR BRENDA; 4.1.2.13; 15939.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000002059; Partially assembled 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; -; 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 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11418327"
FT CHAIN 2..360
FT /note="Fructose-bisphosphate aldolase 1"
FT /id="PRO_0000377379"
FT ACT_SITE 110
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 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 267..269
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT CONFLICT 248
FT /note="Y -> H (in Ref. 1; AAL25625/AAL34519)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> C (in Ref. 1; AAL25625/AAL34519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39632 MW; 67475F644C58E162 CRC64;
MGVKDILSRK TGVIVGDDVL RLFQHAQEKV FAIPAINVTS SSTVVAALEA ARDKNSPIIL
QVSQGGAAFF AGKGVPNGKQ EASVAGAIAA AHYIRSIAPS YGIPVVLHTD HCAKKLLPWL
DGMLDADECY FKLHNEPLFS SHMIDLSEES VEWNIETTAK YLKRAAPMKQ WLEMEIGITG
GEEDGVNNES VDNNSLYTQP EDIYTIYKTL SAISPYFSIA AGFGNVHGVY KPGNVRLHPE
LLSKHQAYVK EKTGSSKNKP VYLVFHGGSG STKAEFKEAI SYGVVKVNLD TDLQYAYLSG
VRDFVLKKKD YLMSAVGNPE GEDKPNKKYF DPRVWIREGE KTMSARVQEA FDDFNTSNQL
