ID   ALF1_HALSA              Reviewed;         263 AA.
AC   Q9HRI2;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000250|UniProtKB:B0R3Y0};
DE            EC=4.1.2.13 {ECO:0000250|UniProtKB:B0R3Y0};
DE   AltName: Full=Fructose-bisphosphate aldolase class I {ECO:0000250|UniProtKB:B0R3Y0};
DE            Short=FBP aldolase {ECO:0000250|UniProtKB:B0R3Y0};
GN   OrderedLocusNames=VNG_0683C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:0000250|UniProtKB:B0R3Y0}.
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:B0R3Y0};
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR   EMBL; AE004437; AAG19176.1; -; Genomic_DNA.
DR   PIR; D84226; D84226.
DR   RefSeq; WP_010902472.1; NC_002607.1.
DR   AlphaFoldDB; Q9HRI2; -.
DR   SMR; Q9HRI2; -.
DR   STRING; 64091.VNG_0683C; -.
DR   PaxDb; Q9HRI2; -.
DR   EnsemblBacteria; AAG19176; AAG19176; VNG_0683C.
DR   GeneID; 5952641; -.
DR   GeneID; 62886300; -.
DR   KEGG; hal:VNG_0683C; -.
DR   PATRIC; fig|64091.14.peg.524; -.
DR   HOGENOM; CLU_057069_2_2_2; -.
DR   InParanoid; Q9HRI2; -.
DR   OMA; FVKVNYP; -.
DR   OrthoDB; 36379at2157; -.
DR   PhylomeDB; Q9HRI2; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; ISS: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   3: Inferred from homology;
KW   Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..263
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138956"
FT   ACT_SITE        177
FT                   /note="Schiff-base intermediate with substrate"
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