ALD2_ECO45
ID ALD2_ECO45 Reviewed; 213 AA.
AC B7MMH7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=5-methylthioribulose-1-phosphate/5-deoxyribulose-1-phosphate aldolase {ECO:0000303|PubMed:31950558};
DE EC=4.1.2.62 {ECO:0000269|PubMed:31950558};
GN Name=ald2 {ECO:0000303|PubMed:31950558};
GN OrderedLocusNames=ECS88_4903 {ECO:0000312|EMBL:CAR06049.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25922 / DSM 1103 / NCIB 12210 / ExPEC;
RX PubMed=31950558; DOI=10.1111/mmi.14459;
RA North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA Tabita F.R.;
RT "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT products that is widespread in bacteria, including pathogenic Escherichia
RT coli.";
RL Mol. Microbiol. 113:923-937(2020).
CC -!- FUNCTION: Uses 5-methylthioribulose-1-phosphate to yield 2-
CC (methylthio)acetaldehyde and dihydroxyacetone phosphate. Can also use
CC 5-deoxyribulose 1-phosphate to yield acetaldehyde and dihydroxyacetone
CC phosphate. Part of a bifunctional DHAP-shunt salvage pathway for SAM
CC by-products. {ECO:0000269|PubMed:31950558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 2-
CC (methylsulfanyl)acetaldehyde + dihydroxyacetone phosphate;
CC Xref=Rhea:RHEA:56940, ChEBI:CHEBI:57642, ChEBI:CHEBI:58548,
CC ChEBI:CHEBI:141184; EC=4.1.2.62;
CC Evidence={ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56941;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-deoxy-D-ribulose 1-phosphate = acetaldehyde +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:61300, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:144504; EC=4.1.2.62;
CC Evidence={ECO:0000269|PubMed:31950558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61301;
CC Evidence={ECO:0000269|PubMed:31950558};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:31950558};
CC Note=Binds 1 cobalt ion per subunit (By similarity). Can also use
CC Mn(2+) (PubMed:31950558). {ECO:0000250|UniProtKB:P0AB87,
CC ECO:0000269|PubMed:31950558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=275 uM for 5-methylthioribulose-1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC KM=598 uM for 5-deoxyribulose 1-phosphate
CC {ECO:0000269|PubMed:31950558};
CC KM=827 uM for ribulose-1-phosphate {ECO:0000269|PubMed:31950558};
CC Note=kcat is 22 sec(-1) with 5-methylthioribulose-1-phosphate as
CC substrate. kcat is 22 sec(-1) with 5-deoxyribulose 1-phosphate as
CC substrate. kcat is 8.7 sec(-1) with ribulose-1-phosphate as
CC substrate. {ECO:0000269|PubMed:31950558};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway. {ECO:0000305|PubMed:31950558}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene precludes growth of the
CC strain with 5-deoxyribose. {ECO:0000269|PubMed:31950558}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. {ECO:0000305}.
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DR EMBL; CU928161; CAR06049.1; -; Genomic_DNA.
DR RefSeq; WP_000439687.1; NC_011742.1.
DR AlphaFoldDB; B7MMH7; -.
DR SMR; B7MMH7; -.
DR EnsemblBacteria; CAR06049; CAR06049; ECS88_4903.
DR KEGG; ecz:ECS88_4903; -.
DR HOGENOM; CLU_006033_3_0_6; -.
DR OMA; IHTHQPV; -.
DR UniPathway; UPA00904; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0005996; P:monosaccharide metabolic process; IEA:UniProt.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cobalt; Lyase; Metal-binding;
KW Methionine biosynthesis.
FT CHAIN 1..213
FT /note="5-methylthioribulose-1-phosphate/5-deoxyribulose-1-
FT phosphate aldolase"
FT /id="PRO_0000450354"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 73
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 92
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 94
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 155
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 113
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 131
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT SITE 209
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ SEQUENCE 213 AA; 23179 MW; 49B94B0E58E7E99B CRC64;
MERIKLAEKI ISTCREMNAS GLNQGTSGNV SARYTGGMLI TPSGIAYSKM TPDMIVFVDD
KGKPEAGKIP SSEWLIHLAC YKARPELNAV IHTHAVNSTA VAIHNHSIPA IHYMVAVSGT
DHIPCIPYYT FGSPELADGV SKGIRESKSL LMQHHGMLAM DVTLEKTLWL AGETETLADL
YIKCGGLHHD VPVLSEAEMT IVLEKFKTYG LKA
