ID   RHMA_ECO7I              Reviewed;         267 AA.
AC   B7NN63;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=ECIAI39_2389;
OS   Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI39 / 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).
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; CU928164; CAR18515.1; -; Genomic_DNA.
DR   RefSeq; WP_000992958.1; NC_011750.1.
DR   RefSeq; YP_002408347.1; NC_011750.1.
DR   AlphaFoldDB; B7NN63; -.
DR   SMR; B7NN63; -.
DR   STRING; 585057.ECIAI39_2389; -.
DR   EnsemblBacteria; CAR18515; CAR18515; ECIAI39_2389.
DR   KEGG; ect:ECIAI39_2389; -.
DR   PATRIC; fig|585057.6.peg.2489; -.
DR   HOGENOM; CLU_059964_1_0_6; -.
DR   OMA; SATWAKK; -.
DR   Proteomes; UP000000749; 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_1000140394"
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;  28931 MW;  084356DD126AE81F CRC64;
     MNALLSNPFK ERLRKGEVQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTIQDLYHQ
     LQAVAPYASQ PVIRPVEASK SLIKQVLDIG AQTLLIPMVD TADQARQVVS ATRYPPYGER
     GVGASVARAA RWGRIENYMA QVNDSLCLLV QVESKTALDH LDEILDVEGI DGVFIGPADL
     SASLGYPDNA GHPEVQRIIE TSIRRIRAAG KAAGFLAVAP DMAQQCLAWG ANFVAVGVDT
     MLYSDALDQR LAMFKSGKNG PRVKGSY