ID A0A3M8P5U4_9BACL Unreviewed; 295 AA.
AC A0A3M8P5U4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Fructose-bisphosphate aldolase class 1 {ECO:0000256|HAMAP-Rule:MF_00729};
DE EC=4.1.2.13 {ECO:0000256|HAMAP-Rule:MF_00729};
DE AltName: Full=Fructose-bisphosphate aldolase class I {ECO:0000256|HAMAP-Rule:MF_00729};
DE Short=FBP aldolase {ECO:0000256|HAMAP-Rule:MF_00729};
GN Name=fda {ECO:0000256|HAMAP-Rule:MF_00729};
GN ORFNames=EEX84_11355 {ECO:0000313|EMBL:RNF38982.1};
OS Planococcus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1848460 {ECO:0000313|EMBL:RNF38982.1, ECO:0000313|Proteomes:UP000275473};
RN [1] {ECO:0000313|EMBL:RNF38982.1, ECO:0000313|Proteomes:UP000275473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCB217 {ECO:0000313|EMBL:RNF38982.1,
RC ECO:0000313|Proteomes:UP000275473};
RX PubMed=29300160; DOI=10.1099/ijsem.0.002548;
RA Gan L.;
RT "Planococcus salinus sp. nov., a moderately halophilic bacterium isolated
RT from a saline-alkali soil.";
RL Int. J. Syst. Evol. Microbiol. 68:589-595(2018).
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|ARBA:ARBA00000441, ECO:0000256|HAMAP-
CC Rule:MF_00729};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|HAMAP-Rule:MF_00729}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|HAMAP-
CC Rule:MF_00729}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RNF38982.1}.
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DR EMBL; RIAX01000008; RNF38982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8P5U4; -.
DR OrthoDB; 9813469at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000275473; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_00729};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00729};
KW Reference proteome {ECO:0000313|Proteomes:UP000275473};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00729}.
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00729"
SQ SEQUENCE 295 AA; 32703 MW; DE7B446E1C7F0128 CRC64;
MNTQQFDVIK NGKGFIAALD QSGGSTPKAL KLYGVSEDTY STEEEMFDLV HEMRTRIITA
PAFNSESILG AILFEQTMER KIESQFTADY LWEQKGVVPF LKIDKGLAEE EDGVQLMKPN
PDLKDLLKRA NGYNIFGTKM RSVIKEANPE GIKKVVDQQF VVAMEVINAG LVPIIEPEVD
IHSADKEQIE TLLNTEILSH LGNLGKEDYV ILKLTIPTLN NFYKELIEHP NVVRVVALSG
GYSREEAIQK LAANEGLIAS FSRALSEGLS ADQTDEDFNA TLEESIKGIY AASIT
//
