ID RHMA_SALTI Reviewed; 267 AA.
AC Q8Z549; Q7CB77;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 117.
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=STY2519, t0574;
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AE014613; AAO68280.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD07522.1; -; Genomic_DNA.
DR RefSeq; NP_456832.1; NC_003198.1.
DR RefSeq; WP_000992948.1; NZ_WSUR01000039.1.
DR AlphaFoldDB; Q8Z549; -.
DR SMR; Q8Z549; -.
DR STRING; 220341.gene:17586419; -.
DR KEGG; stt:t0574; -.
DR KEGG; sty:STY2519; -.
DR PATRIC; fig|220341.7.peg.2550; -.
DR eggNOG; COG3836; Bacteria.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; YVDLEHT; -.
DR OrthoDB; 86160at2; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Phosphoenolpyruvate-binding domains; 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 PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF5; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 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_0000353176"
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; 28842 MW; D7031DD3D94643E6 CRC64;
MNALLSNPFK EGLRKRDTQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTVQDLYHQ
LQAIAPYASQ PVIRPIEGSK ALIKQVLDIG AQTLLIPMVD TAEQARQVVS ATRYPPLGQR
GVGASVARAA RWGRIDNYMA QANESLCLLV QVESKVALEN LDAILEVEGI DGVFIGPADL
SASLGYPDNA GHPEVQRIIE SCIYRIRAAG KAAGFLAVDP AMAQKCLAWG ANFVAVGVDT
MLYTEALDSR LAMFKSVQSV STAKRSY
//
