ID D2TGZ6_CITRI Unreviewed; 267 AA.
AC D2TGZ6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=2-keto-3-deoxy-L-rhamnonate aldolase {ECO:0000256|HAMAP-Rule:MF_01290};
DE Short=KDR aldolase {ECO:0000256|HAMAP-Rule:MF_01290};
DE EC=4.1.2.53 {ECO:0000256|HAMAP-Rule:MF_01290};
DE AltName: Full=2-dehydro-3-deoxyrhamnonate aldolase {ECO:0000256|HAMAP-Rule:MF_01290};
GN Name=rhmA {ECO:0000256|HAMAP-Rule:MF_01290};
GN OrderedLocusNames=ROD_26581 {ECO:0000313|EMBL:CBG89401.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG89401.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG89401.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG89401.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
CC -!- FUNCTION: Catalyzes the reversible retro-aldol cleavage of 2-keto-3-
CC deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.
CC {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01290};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01290};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01290};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01290}.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDR aldolase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01290}.
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DR EMBL; FN543502; CBG89401.1; -; Genomic_DNA.
DR RefSeq; WP_012906822.1; NC_013716.1.
DR AlphaFoldDB; D2TGZ6; -.
DR STRING; 637910.ROD_26581; -.
DR KEGG; cro:ROD_26581; -.
DR eggNOG; COG3836; Bacteria.
DR HOGENOM; CLU_059964_1_0_6; -.
DR OrthoDB; 86160at2; -.
DR Proteomes; UP000001889; 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 {ECO:0000256|HAMAP-Rule:MF_01290, ECO:0000313|EMBL:CBG89401.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01290};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01290}.
FT DOMAIN 19..245
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT SITE 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
FT SITE 88
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01290"
SQ SEQUENCE 267 AA; 28726 MW; B0BC6CFA1D559A32 CRC64;
MNALLANPFK EGLRKGEVQI GLWLSSTTSY MAEIAATSGY DWLLIDGEHA PNTVQDLYHQ
LQAIAPYASQ PVIRPVEGTK ALIKQVLDIG AQTLLIPMVD TAEQARQVVA ATRYPPLGER
GVGASVARAA RWGRIDNYMA QANESLCLLV QVESKTALDN LDAILDVEGI DGVFIGPADL
SASLGYPDNA GHPEVQRIIQ ESLRRIRAAG KAAGFLAVDP AMAQKCLQWG ANFVAVGVDT
MLYTEALDRR LAMFKAVSSA TPVKSSY
//
