ID   ALF1_HALS3              Reviewed;         263 AA.
AC   B0R3Y0;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000303|PubMed:25216252};
DE            EC=4.1.2.13 {ECO:0000269|PubMed:25216252};
DE   AltName: Full=Fructose-bisphosphate aldolase class I {ECO:0000303|PubMed:25216252};
DE            Short=FBP aldolase {ECO:0000303|PubMed:25216252};
GN   Name=fba1; OrderedLocusNames=OE_2019F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=25216252; DOI=10.1371/journal.pone.0107475;
RA   Gulko M.K., Dyall-Smith M., Gonzalez O., Oesterhelt D.;
RT   "How do haloarchaea synthesize aromatic amino acids?";
RL   PLoS ONE 9:E107475-E107475(2014).
CC   -!- FUNCTION: Has aldolase activity with fructose 1,6-bisphosphate. May
CC       play a role in the biosynthesis of aromatic amino acids (AroAA).
CC       {ECO:0000269|PubMed:25216252}.
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:0000269|PubMed:25216252};
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR   EMBL; AM774415; CAP13445.1; -; Genomic_DNA.
DR   RefSeq; WP_010902472.1; NC_010364.1.
DR   AlphaFoldDB; B0R3Y0; -.
DR   SMR; B0R3Y0; -.
DR   EnsemblBacteria; CAP13445; CAP13445; OE_2019F.
DR   GeneID; 5952641; -.
DR   GeneID; 62886300; -.
DR   KEGG; hsl:OE_2019F; -.
DR   HOGENOM; CLU_057069_2_2_2; -.
DR   OMA; FVKVNYP; -.
DR   PhylomeDB; B0R3Y0; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..263
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000431483"
FT   ACT_SITE        177
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   263 AA;  28083 MW;  25FF044B6A77494F CRC64;
     MRPFEDSPIS RDGKVLILAY DHGLEHGPVD FEAVPATKDP EAVWDVATHD AVSAMAAQKG
     IAEAYYPSYS DDVNLLAKLN GTSNLWMGEP DSAVNWTVDY AADVGADAVG FTLYGGSNSE
     VEMAEEFRDA QEAARDHDLP VVMWSYPRGQ GLKNDKNPDT IAYAARQALE LGADIAKVKY
     PGSTDAMSHA VDMAGPTNVV MSGGSKTSDR DFLESVKGAI DAGASGLAVG RNVWQREHPA
     AFLDGLEAVV YEEASVDEAL GRI