ID   RHMA_ECOSM              Reviewed;         267 AA.
AC   B1LLJ9;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=2-keto-3-deoxy-L-rhamnonate aldolase {ECO:0000255|HAMAP-Rule:MF_01290};
DE            Short=KDR aldolase {ECO:0000255|HAMAP-Rule:MF_01290};
DE            EC=4.1.2.53 {ECO:0000255|HAMAP-Rule:MF_01290};
DE   AltName: Full=2-dehydro-3-deoxyrhamnonate aldolase {ECO:0000255|HAMAP-Rule:MF_01290};
GN   Name=rhmA {ECO:0000255|HAMAP-Rule:MF_01290};
GN   OrderedLocusNames=EcSMS35_2399;
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC;
RX   PubMed=18708504; DOI=10.1128/jb.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-
CC       deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
CC       {ECO:0000255|HAMAP-Rule:MF_01290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-3-deoxy-L-rhamnonate = (S)-lactaldehyde + pyruvate;
CC         Xref=Rhea:RHEA:25784, ChEBI:CHEBI:15361, ChEBI:CHEBI:18041,
CC         ChEBI:CHEBI:58371; EC=4.1.2.53; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01290};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01290};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01290};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01290}.
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDR aldolase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01290}.
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DR   EMBL; CP000970; ACB17621.1; -; Genomic_DNA.
DR   RefSeq; WP_000992957.1; NC_010498.1.
DR   AlphaFoldDB; B1LLJ9; -.
DR   SMR; B1LLJ9; -.
DR   EnsemblBacteria; ACB17621; ACB17621; EcSMS35_2399.
DR   KEGG; ecm:EcSMS35_2399; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; SATWAKK; -.
DR   Proteomes; UP000007011; Chromosome.
DR   GO; GO:0106099; F:2-keto-3-deoxy-L-rhamnonate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_01290; KDR_aldolase; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR023593; KDR_aldolase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..267
FT                   /note="2-keto-3-deoxy-L-rhamnonate aldolase"
FT                   /id="PRO_0000353170"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   SITE            74
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
FT   SITE            88
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01290"
SQ   SEQUENCE   267 AA;  28859 MW;  C10E230ADA21FE63 CRC64;
     MNALLSNPFK ERLRKGEVQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTIQDLYHQ
     LQAVAPYASQ PVIRPVEASK SLIKQVLDIG AQTLLIPMVD TADQARQVVS ATRYPPYGER
     GVGASVARAA RWGRIENYMA HVNDSLCLLV QVESKTALDN LDEILGVEGI DGVFIGPADL
     SASLGYPDNA GHPEVQRIIE TSIRRIRAAG KAAGFLAVAP DMAQQCLAWG ANFVAVGVDT
     MLYSDALDQR LAMFKSGKNG PRVKGSY