ID   ALF1_AERPE              Reviewed;         272 AA.
AC   Q9YG90;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Probable fructose-bisphosphate aldolase class 1;
DE            EC=4.1.2.13;
DE   AltName: Full=Probable fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase;
GN   Name=fba; OrderedLocusNames=APE_0011.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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   -!- ACTIVITY REGULATION: Activated by citrate. {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR   EMBL; BA000002; BAA78920.2; -; Genomic_DNA.
DR   PIR; F72752; F72752.
DR   AlphaFoldDB; Q9YG90; -.
DR   SMR; Q9YG90; -.
DR   STRING; 272557.APE_0011.1; -.
DR   EnsemblBacteria; BAA78920; BAA78920; APE_0011.1.
DR   KEGG; ape:APE_0011.1; -.
DR   PATRIC; fig|272557.25.peg.5; -.
DR   eggNOG; arCOG04044; Archaea.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd00958; DhnA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   NCBIfam; NF040816; Fbpase1_Arch; 1.
DR   PANTHER; PTHR47916:SF1; 3-HYDROXY-5-PHOSPHONOOXYPENTANE-2,4-DIONE THIOLASE-RELATED; 1.
DR   PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..272
FT                   /note="Probable fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_0000138947"
FT   ACT_SITE        184
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   272 AA;  29583 MW;  D992DAFA81A6ADAF CRC64;
     MISSQDVGKR VRLSRILPDG RSVIFAFDHG IEHGPGEIPE ERLDPRLLIR EVVEAGVDAI
     MTTPGIARLT WDIWANRVAM IIKVSGKTSI RPQDDQFLQS AISSVDEVVA LGGDGVAATV
     YWGSQFEDKM LERWTRIRLR AEKLGLPALQ LAYPRGPHIK NRYAVDIVAY GARAAMETGA
     DLIKTYYTGS TESFRRVVSA AGGVPVLMSG GARTPSPQEF LHKVYSVMEA GGGGVVVGRN
     IFQAGDIRAM VKAIRAIVHE GFDPEKASKL LG
//