ID   ALF1_SYNY3              Reviewed;         300 AA.
AC   P74309;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 127.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fda; Synonyms=fbaB; OrderedLocusNames=slr0943;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18403.1; -; Genomic_DNA.
DR   PIR; S76144; S76144.
DR   AlphaFoldDB; P74309; -.
DR   SMR; P74309; -.
DR   IntAct; P74309; 1.
DR   STRING; 1148.gene:10499279; -.
DR   PaxDb; 1148-1653490; -.
DR   EnsemblBacteria; BAA18403; BAA18403; BAA18403.
DR   KEGG; syn:slr0943; -.
DR   eggNOG; COG3588; Bacteria.
DR   InParanoid; P74309; -.
DR   PhylomeDB; P74309; -.
DR   BioCyc; MetaCyc:FBABSYN-MONOMER; -.
DR   SABIO-RK; P74309; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00949; FBP_aldolase_I_bact; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00729; FBP_aldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   InterPro; IPR023014; FBA_I_Gram+-type.
DR   PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..300
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000216913"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        218
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   300 AA;  33149 MW;  EDAE4D24F58FE667 CRC64;
     MMTLEPNQEQ LKKMKSHPGF IAALDQSGGS TPGALADYGI EPNTYSGDDQ MFALVHQMRT
     RIMTSPGFTG DRILAAILFE DTMNREVDGE PTANYLWQNK QIVPILKVDK GLAQEKDGSQ
     LMKPIPQLDS LLMKAKKKGI FGTKMRSFIK HANPAGIEAI VDQQFELAQQ IIAAGLVPII
     EPEVDIHCSE KAQAEALLKQ AMLKHLNQLP KGQWVMLKLT LPEQDNLYSN CIEHANVLRV
     VALSGGYSQA EANERLSRNH GVIASFSRAL TEGLTAQQTD AEFNTMLDES IEKIYQASIT
//