ID ALF_COCIM Reviewed; 302 AA. AC P0CJ44; J3K6Q1; J3K765; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=Putative fructose-bisphosphate aldolase; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Putative fructose-1,6-bisphosphate aldolase; GN ORFNames=CIMG_05755; OS Coccidioides immitis (strain RS) (Valley fever fungus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=246410; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS; RX PubMed=19717792; DOI=10.1101/gr.087551.108; RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R., RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y., RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M., RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T., RA Henn M.R., Birren B.W., Taylor J.W.; RT "Comparative genomic analyses of the human fungal pathogens Coccidioides RT and their relatives."; RL Genome Res. 19:1722-1731(2009). RN [2] RP GENOME REANNOTATION. RC STRAIN=RS; RX PubMed=20516208; DOI=10.1101/gr.103911.109; RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J., RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D., RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A., RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J., RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R., RA Taylor J.W., Rounsley S.D.; RT "Population genomic sequencing of Coccidioides fungi reveals recent RT hybridization and transposon control."; RL Genome Res. 20:938-946(2010). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG704912; EAS30276.3; -; Genomic_DNA. DR RefSeq; XP_001241859.1; XM_001241858.2. DR PDB; 3PM6; X-ray; 2.20 A; A/B=1-302. DR PDBsum; 3PM6; -. DR AlphaFoldDB; P0CJ44; -. DR SMR; P0CJ44; -. DR STRING; 246410.P0CJ44; -. DR GeneID; 4561677; -. DR KEGG; cim:CIMG_05755; -. DR VEuPathDB; FungiDB:CIMG_05755; -. DR InParanoid; P0CJ44; -. DR OMA; TCYSAIR; -. DR OrthoDB; 1763470at2759; -. DR UniPathway; UPA00109; UER00183. DR EvolutionaryTrace; P0CJ44; -. DR Proteomes; UP000001261; Unassembled 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; cd00947; TBP_aldolase_IIB; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR SUPFAM; SSF51569; Aldolase; 1. PE 1: Evidence at protein level; KW 3D-structure; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..302 FT /note="Putative fructose-bisphosphate aldolase" FT /id="PRO_0000403787" FT ACT_SITE 86 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 193 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 223 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 224..226 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 245..248 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT HELIX 12..20 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 33..45 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 56..62 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 91..99 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 122..137 FT /evidence="ECO:0007829|PDB:3PM6" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 170..177 FT /evidence="ECO:0007829|PDB:3PM6" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 204..214 FT /evidence="ECO:0007829|PDB:3PM6" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 230..238 FT /evidence="ECO:0007829|PDB:3PM6" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 248..261 FT /evidence="ECO:0007829|PDB:3PM6" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 267..288 FT /evidence="ECO:0007829|PDB:3PM6" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:3PM6" SQ SEQUENCE 302 AA; 33389 MW; 3FBF318A0A3421C6 CRC64; MPHPSLKSNR ALPLLTFART HSFAIPAICV YNLEGILAII RAAEHKRSPA MILLFPWAIQ YADSLLVRTA ASACRAASVP ITLHLDHAQD PEIIKRAADL SRSETHEPGF DSIMVDMSHF SKEENLRLTR ELVAYCNARG IATEAEPGRI EGGEDGVQDT VDLEGVLTTP EESEEFVATG INWLAPAFGN VHGNYGPRGV QLDYERLQRI NEAVGERVGL VLHGADPFTK EIFEKCIERG VAKVNVNRAV NNEYVKVMRE KAGSLPITRL HEEVTNAMQA AVEKIMDMID STGKAEFMMD EK //