ALF1_THETK
ID ALF1_THETK Reviewed; 263 AA.
AC P58315; G4RK17;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Fructose-bisphosphate aldolase class 1;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase;
DE Short=FBPA;
GN Name=fba; OrderedLocusNames=TTX_1278;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND SUBUNIT.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=11387336; DOI=10.1074/jbc.m103447200;
RA Siebers B., Brinkmann H., Doerr C., Tjaden B., Lilie H., van der Oost J.,
RA Verhees C.H.;
RT "Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of
RT archaeal type class I aldolases.";
RL J. Biol. Chem. 276:28710-28718(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=12941964; DOI=10.1074/jbc.m305922200;
RA Lorentzen E., Pohl E., Zwart P., Stark A., Russell R.B., Knura T.,
RA Hensel R., Siebers B.;
RT "Crystal structure of an archaeal class I aldolase and the evolution of
RT (betaalpha)8 barrel proteins.";
RL J. Biol. Chem. 278:47253-47260(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLU-144 AND PHE-146 IN
RP COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF TRP-144 AND TYR-146,
RP REACTION MECHANISM, AND SUBUNIT.
RX PubMed=15766250; DOI=10.1021/bi048192o;
RA Lorentzen E., Siebers B., Hensel R., Pohl E.;
RT "Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase:
RT structural analysis of reaction intermediates.";
RL Biochemistry 44:4222-4229(2005).
CC -!- FUNCTION: Catalyzes the reversible cleavage of fructose 1,6-
CC bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and
CC dihydroxyacetone phosphate (DHAP).
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:11387336};
CC -!- ACTIVITY REGULATION: Activated by citrate.
CC {ECO:0000269|PubMed:11387336}.
CC -!- SUBUNIT: Homodecamer (dimer of pentamers).
CC {ECO:0000269|PubMed:11387336, ECO:0000269|PubMed:12941964,
CC ECO:0000269|PubMed:15766250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR EMBL; AJ310483; CAC48235.1; -; Genomic_DNA.
DR EMBL; FN869859; CCC81912.1; -; Genomic_DNA.
DR RefSeq; WP_014127167.1; NC_016070.1.
DR PDB; 1OJX; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J=1-263.
DR PDB; 1OK4; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=1-263.
DR PDB; 1OK6; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-263.
DR PDB; 1W8S; X-ray; 1.85 A; A/B/C/D/E/F/G/H/I/J=1-263.
DR PDB; 2YCE; X-ray; 1.93 A; A/B/C/D/E/F/G/H/I/J=1-263.
DR PDBsum; 1OJX; -.
DR PDBsum; 1OK4; -.
DR PDBsum; 1OK6; -.
DR PDBsum; 1W8S; -.
DR PDBsum; 2YCE; -.
DR AlphaFoldDB; P58315; -.
DR SMR; P58315; -.
DR STRING; 768679.TTX_1278; -.
DR EnsemblBacteria; CCC81912; CCC81912; TTX_1278.
DR GeneID; 11262157; -.
DR KEGG; ttn:TTX_1278; -.
DR PATRIC; fig|768679.9.peg.1292; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_2_2; -.
DR OMA; FVKVNYP; -.
DR OrthoDB; 36379at2157; -.
DR BRENDA; 4.1.2.13; 6329.
DR SABIO-RK; P58315; -.
DR EvolutionaryTrace; P58315; -.
DR Proteomes; UP000002654; 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; -; 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 3D-structure; Cytoplasm; Glycolysis; Lyase; Reference proteome;
KW Schiff base.
FT CHAIN 1..263
FT /note="Fructose-bisphosphate aldolase class 1"
FT /id="PRO_0000138952"
FT ACT_SITE 146
FT /note="Proton donor"
FT ACT_SITE 177
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 24..25
FT /ligand="substrate"
FT BINDING 29
FT /ligand="substrate"
FT BINDING 33
FT /ligand="substrate"
FT BINDING 144
FT /ligand="substrate"
FT BINDING 148
FT /ligand="substrate"
FT BINDING 177..179
FT /ligand="substrate"
FT BINDING 202..204
FT /ligand="substrate"
FT BINDING 231..232
FT /ligand="substrate"
FT MUTAGEN 144
FT /note="W->E: Loss of FBP aldolase activity; when associated
FT with F-146."
FT /evidence="ECO:0000269|PubMed:15766250"
FT MUTAGEN 146
FT /note="Y->F: The catalytic activity is at least 3-fold
FT lower than for the wild-type. Loss of FBP aldolase
FT activity; when associated with E-144."
FT /evidence="ECO:0000269|PubMed:15766250"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:1W8S"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:1W8S"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1W8S"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:1W8S"
SQ SEQUENCE 263 AA; 28705 MW; 1399A6D0CF4F0D9E CRC64;
MANLTEKFLR IFARRGKSII LAYDHGIEHG PADFMDNPDS ADPEYILRLA RDAGFDGVVF
QRGIAEKYYD GSVPLILKLN GKTTLYNGEP VSVANCSVEE AVSLGASAVG YTIYPGSGFE
WKMFEELARI KRDAVKFDLP LVVWSYPRGG KVVNETAPEI VAYAARIALE LGADAMKIKY
TGDPKTFSWA VKVAGKVPVL MSGGPKTKTE EDFLKQVEGV LEAGALGIAV GRNVWQRRDA
LKFARALAEL VYGGKKLAEP LNV
