ID   RHMA_SALG2              Reviewed;         267 AA.
AC   B5RCB4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=SG2317;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(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; AM933173; CAR38148.1; -; Genomic_DNA.
DR   RefSeq; WP_000992937.1; NC_011274.1.
DR   AlphaFoldDB; B5RCB4; -.
DR   SMR; B5RCB4; -.
DR   EnsemblBacteria; CAR38148; CAR38148; SG2317.
DR   KEGG; seg:SG2317; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; SATWAKK; -.
DR   Proteomes; UP000008321; 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_1000140399"
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;  28760 MW;  F4A956E1BCCC03FF CRC64;
     MNALLSNPFK EGLREGDTQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTVQDLYHQ
     LQAIAPYASQ PVIRLIEGSK ALIKQVLDIG AQTLLIPMVD TAEQARQVVS ATRYPPLGQR
     GVGASVARAA RWGRIDNYMA QANESLCLLV QVESKVALEN LDAILEVEGI DGVFIGPADL
     SASLGYPDNA GHPEVQRIIE SCIYRIRAAG KAAGFLAVDP AMAQKCLAWG ANFVAVGVDT
     MLYTEALDSR LAMFKSVQSV STAKRSY