ALF_NOSS1
ID ALF_NOSS1 Reviewed; 359 AA.
AC Q8YNK2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000250|UniProtKB:Q55664};
DE Short=FBP aldolase {ECO:0000250|UniProtKB:Q55664};
DE Short=FBPA {ECO:0000250|UniProtKB:Q55664};
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000250|UniProtKB:Q55664};
GN Name=fda {ECO:0000312|EMBL:BAB76262.1}; OrderedLocusNames=all4563;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1] {ECO:0000312|EMBL:BAB76262.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 282-289, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
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|UniProtKB:Q55664}.
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 Evidence={ECO:0000250|UniProtKB:Q55664};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q55664};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250|UniProtKB:Q55664};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000250|UniProtKB:Q55664}.
CC -!- MASS SPECTROMETRY: Mass=38764; Mass_error=1; Method=MALDI;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000255}.
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DR EMBL; BA000019; BAB76262.1; -; Genomic_DNA.
DR PIR; AC2376; AC2376.
DR RefSeq; WP_010998695.1; NZ_RSCN01000007.1.
DR AlphaFoldDB; Q8YNK2; -.
DR SMR; Q8YNK2; -.
DR STRING; 103690.17133699; -.
DR EnsemblBacteria; BAB76262; BAB76262; BAB76262.
DR KEGG; ana:all4563; -.
DR eggNOG; COG0191; Bacteria.
DR OMA; NNMEIVQ; -.
DR OrthoDB; 827430at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000002483; Chromosome.
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 InterPro; IPR006412; Fruct_bisP_Calv.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01521; FruBisAldo_II_B; 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:0000250|UniProtKB:Q55664"
FT CHAIN 2..359
FT /note="Fructose-bisphosphate aldolase"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT /id="PRO_0000366199"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 50
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 199
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 233..235
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
FT BINDING 275..278
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:Q55664"
SQ SEQUENCE 359 AA; 38617 MW; E91D84D7591007B1 CRC64;
MALVPLRLLL DHAAENGYGI PAFNVNNLEQ IQAILKAAAE TDSPVILQAS RGARNYAGEN
FLRHLILAAV ETYPEIPIVM HQDHGNAPST CYSAIKNNFT SVMMDGSLEA DAKTPASFEY
NVNVTREVVN VAHALGVSVE GELGCLGSLE TGAGEAEDGH GFEGTLDHSQ LLTDPDEAVN
FVEATQVDAL AVAIGTSHGA YKFTRKPTGE ILAISRIEEI HRRLPNTHLV MHGSSSVPED
LIALINEYGG AIPETYGVPV EEIQKGIKSG VRKVNIDTDN RLAITAAVRE ALAKNPKEFD
PRHFLKPSIT YMQKVCAERY VQFGTAGNAS KIKQVSLETF AAKYAKGELN AISKAAAKV
