RHMA_SALPA
ID RHMA_SALPA Reviewed; 267 AA.
AC Q5PI50;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=SPA0574;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76576.1; -; Genomic_DNA.
DR RefSeq; WP_000992940.1; NC_006511.1.
DR AlphaFoldDB; Q5PI50; -.
DR SMR; Q5PI50; -.
DR EnsemblBacteria; AAV76576; AAV76576; SPA0574.
DR KEGG; spt:SPA0574; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; SATWAKK; -.
DR Proteomes; UP000008185; 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_0000353174"
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; 28782 MW; 41531074885E3B9D 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
MLYTEALDNR LVMFKSVQSV STAKRSY
