ID   RHMA_SALPC              Reviewed;         267 AA.
AC   C0Q079;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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}; OrderedLocusNames=SPC_1422;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN45583.1; -; Genomic_DNA.
DR   RefSeq; WP_000992941.1; NC_012125.1.
DR   AlphaFoldDB; C0Q079; -.
DR   SMR; C0Q079; -.
DR   EnsemblBacteria; ACN45583; ACN45583; SPC_1422.
DR   KEGG; sei:SPC_1422; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; SATWAKK; -.
DR   Proteomes; UP000001599; 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_1000165270"
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;  28727 MW;  960305AEB85E3B8F CRC64;
     MNALLSNPFK EGLRKGDTQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTVQDLYHQ
     LQAIAPYASQ PVIRPIEGSK ALIKQVLDIG AQTLLIPMVD TAEQARQVVS ATRYPPLGQR
     GVGASVARAA RWGRIDNYMA QANESLCLLV QVESKVALEN LDAILEVEGI DGVFIGPADL
     SASLGYPDNA GHPEVQRIIE ACIYRIRAAG KAAGFLAVDP AMAQKCLAWG ANFVAVGVDT
     MLYTEALDSR LAMFKSVQSV STAKRSY