ALF_COCIM
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 03-AUG-2022, entry version 59.
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}.
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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 EnsemblFungi; EAS30276; EAS30276; CIMG_05755.
DR GeneID; 4561677; -.
DR KEGG; cim:CIMG_05755; -.
DR VEuPathDB; FungiDB:CIMG_05755; -.
DR InParanoid; P0CJ44; -.
DR OMA; NNMEIVQ; -.
DR OrthoDB; 1284023at2759; -.
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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 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
