ID   ALF1_PORG3              Reviewed;         293 AA.
AC   B2RLG9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000255|HAMAP-Rule:MF_00729};
DE            EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_00729};
DE   AltName: Full=Fructose-bisphosphate aldolase class I;
DE            Short=FBP aldolase {ECO:0000255|HAMAP-Rule:MF_00729};
GN   Name=fda {ECO:0000255|HAMAP-Rule:MF_00729};
GN   OrderedLocusNames=PGN_1695;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC   2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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:0000255|HAMAP-Rule:MF_00729};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00729}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00729}.
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DR   EMBL; AP009380; BAG34214.1; -; Genomic_DNA.
DR   RefSeq; WP_012458465.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RLG9; -.
DR   SMR; B2RLG9; -.
DR   GeneID; 29256860; -.
DR   KEGG; pgn:PGN_1695; -.
DR   eggNOG; COG3588; Bacteria.
DR   HOGENOM; CLU_081560_0_0_10; -.
DR   OrthoDB; 9813469at2; -.
DR   BioCyc; PGIN431947:G1G2V-1903-MONOMER; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000008842; 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; Schiff base.
FT   CHAIN           1..293
FT                   /note="Fructose-bisphosphate aldolase class 1"
FT                   /id="PRO_1000132711"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT   ACT_SITE        211
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ   SEQUENCE   293 AA;  32987 MW;  CDBA3CFF649DCE91 CRC64;
     MNKEQLQQMR QAPGFVGALD QSGGSTPKAL KAYGIQPDAY QSEEEMFDLI HQMRTRMITS
     PAFATGKIIG VILFERTMRG KIEGMPTADF LWEKRHIVPF LKVDKGLQDE ANGVQLMKPF
     PELGKLCEEA VGYHVFGTKM RSVIKQANEQ GIRDIVEQQF QWGKEILSHG LVPILEPEVD
     IHCPEKAKAE EILKRELLAQ LDKMTEPVML KITIPTVDNF YKEIIEHPMM LRVVALSGGY
     SREQANELLS RNHGVIASFS RALVEGLSVQ QTDAEFNAML EASIEDVYQA SIK
//