ID Q3SIQ9_THIDA Unreviewed; 340 AA.
AC Q3SIQ9;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN OrderedLocusNames=Tbd_1513 {ECO:0000313|EMBL:AAZ97466.1};
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ97466.1, ECO:0000313|Proteomes:UP000008291};
RN [1] {ECO:0000313|EMBL:AAZ97466.1, ECO:0000313|Proteomes:UP000008291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ97466.1,
RC ECO:0000313|Proteomes:UP000008291};
RX PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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:0000256|RuleBase:RU003994};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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DR EMBL; CP000116; AAZ97466.1; -; Genomic_DNA.
DR RefSeq; WP_011312025.1; NC_007404.1.
DR AlphaFoldDB; Q3SIQ9; -.
DR STRING; 292415.Tbd_1513; -.
DR KEGG; tbd:Tbd_1513; -.
DR eggNOG; COG3588; Bacteria.
DR HOGENOM; CLU_031243_0_0_4; -.
DR OrthoDB; 9793595at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000008291; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR NCBIfam; NF033379; FrucBisAld_I; 1.
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.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|RuleBase:RU003994};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW Reference proteome {ECO:0000313|Proteomes:UP000008291}.
SQ SEQUENCE 340 AA; 36356 MW; 54F7C70EB977978C CRC64;
MNLDELQAVA RAIVAPQKGV LAADESGPTI KKRFDTIAVE STEKSRRRYR EIMFTAESIE
RYIGGVILYD ETLRQSTRDG TPFPQLLAGR GIIPGIKVDQ GAKPLALCPG EKVTEGLDGL
RERLVEYHGL GAQFAKWRAV IDIDAHDLPS PFGIHANAHA LARYAALCQE VGLVPIVEPE
VLMDGAHDVE RCEAVTARAL EAVFAELDAH GVGLEGVLLK PNMVVAGKKS TRQAGVQEVA
EATLRCLRRH VPAAVPGIVF LSGGQSAEEA TAHLSAMNAM GPHPWQVSFS YGRALQAPVL
AAWRGHEANA AAAQAALLER ARLNGLARDG AYGPEMESAG
//
