RHMA_SHISS
ID RHMA_SHISS Reviewed; 267 AA.
AC Q3YZW1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SSON_2306;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000038; AAZ88951.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YZW1; -.
DR SMR; Q3YZW1; -.
DR EnsemblBacteria; AAZ88951; AAZ88951; SSON_2306.
DR KEGG; ssn:SSON_2306; -.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OMA; SATWAKK; -.
DR Proteomes; UP000002529; 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_0000353180"
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; 28894 MW; 66A5111AFBC15F53 CRC64;
MNALLTNPFK ERLRKGEVQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTIQDLYHQ
LQAVAPYASQ PVIRPVEGSK SLIKQVLDIG AQTLLIPMVD TADQARQVAS ATRYPPYGER
GVGASVARAA RWGRIENYMA QVNDSLCLLV QVESKTALDN LDEILDVEGI DGVFIGPADL
SASLGYPDNA GHPEVQRIIE TSIRRIRAAG KAAGFLAVAP DMAQQCLAWG ANFVAVGVDT
MLYSDALDQR LAMFKSGKNG PRIKGSY
