ALF1_TREDE
ID ALF1_TREDE Reviewed; 295 AA.
AC Q73QV3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
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}; OrderedLocusNames=TDE_0340;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS10835.1; -; Genomic_DNA.
DR RefSeq; NP_970954.1; NC_002967.9.
DR RefSeq; WP_002681313.1; NC_002967.9.
DR AlphaFoldDB; Q73QV3; -.
DR SMR; Q73QV3; -.
DR STRING; 243275.TDE_0340; -.
DR EnsemblBacteria; AAS10835; AAS10835; TDE_0340.
DR GeneID; 2739339; -.
DR KEGG; tde:TDE_0340; -.
DR PATRIC; fig|243275.7.peg.329; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_081560_0_0_12; -.
DR OMA; GVFGTKM; -.
DR OrthoDB; 945470at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000008212; 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; -; 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; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..295
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000216914"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00729"
SQ SEQUENCE 295 AA; 32805 MW; 5C1A6403A7D4EA20 CRC64;
MDKVKLERMK NDKGFIAALD QSGGSTPKAL AAYGVPETAY SNEKEMFDLV HAMRTRIITG
KAFNSNNILG AILFEQTMER EIEGMPTADF LWEKKKILPF LKVDKGLADL KDGVQLMKPI
PNLDAMLKHA VEKHIFGTKM RSVIKEANPK GIKAVVDQQF ELGIQIAKAG LVPIIEPEVD
IKSPDKAKCE EILKKELEEH LKTLPKDLLV MFKLSIPTKE NLYEEFTKHP QVVRVVALSG
GYSRDDANKL LAKNRGMIAS FSRALAEGLF ASQSDAEFNA TLEKTIKGVY EASIT