ID   RHMD_TOLAT              Reviewed;         401 AA.
AC   C4LDK0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=L-rhamnonate dehydratase {ECO:0000255|HAMAP-Rule:MF_01288};
DE            Short=RhamD {ECO:0000255|HAMAP-Rule:MF_01288};
DE            EC=4.2.1.90 {ECO:0000255|HAMAP-Rule:MF_01288};
GN   Name=rhmD {ECO:0000255|HAMAP-Rule:MF_01288}; OrderedLocusNames=Tola_1175;
OS   Tolumonas auensis (strain DSM 9187 / TA4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Tolumonas.
OX   NCBI_TaxID=595494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9187 / TA4;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA   Beller H.;
RT   "Complete sequence of Tolumonas auensis DSM 9187.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-
CC       L-rhamnonate (KDR). {ECO:0000255|HAMAP-Rule:MF_01288}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O;
CC         Xref=Rhea:RHEA:23080, ChEBI:CHEBI:15377, ChEBI:CHEBI:58118,
CC         ChEBI:CHEBI:58371; EC=4.2.1.90; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01288};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01288};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01288};
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01288}.
CC   -!- MISCELLANEOUS: Reaction proceeds via a syn dehydration.
CC       {ECO:0000255|HAMAP-Rule:MF_01288}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. RhamD subfamily. {ECO:0000255|HAMAP-Rule:MF_01288}.
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DR   EMBL; CP001616; ACQ92796.1; -; Genomic_DNA.
DR   RefSeq; WP_012729395.1; NC_012691.1.
DR   AlphaFoldDB; C4LDK0; -.
DR   SMR; C4LDK0; -.
DR   STRING; 595494.Tola_1175; -.
DR   EnsemblBacteria; ACQ92796; ACQ92796; Tola_1175.
DR   KEGG; tau:Tola_1175; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_1_0_6; -.
DR   OMA; HFVISQP; -.
DR   OrthoDB; 743369at2; -.
DR   Proteomes; UP000009073; Chromosome.
DR   GO; GO:0050032; F:L-rhamnonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; IEA:InterPro.
DR   CDD; cd03327; MR_like_2; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   HAMAP; MF_01288; Rhamnon_dehydrat; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR023444; L-Rhamnon_dehydrat.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00006; rhamnonate_dehydratase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   SUPFAM; SSF54826; SSF54826; 1.
DR   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..401
FT                   /note="L-rhamnonate dehydratase"
FT                   /id="PRO_1000214214"
FT   ACT_SITE        325
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         276
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   SITE            298
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   SITE            345
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
SQ   SEQUENCE   401 AA;  44290 MW;  4E8CA2DE21931F3F CRC64;
     MVLPKIKEVR AWFTGGATAE KGAGGADYHD QGNHHWIDDH IATPMSKYKQ YEQSRQSFGI
     NVLGTLVIEV EADNGQIGFA VSTAGEMGCF IVEKHLNRFI EGKCVSDIKL IHDQMLGATM
     YYAGSGGLVM NTISCVDLAL WDLFGKVVGL PVYKLLGGAV RDEIQFYATG ARPDLAKEMG
     FIGGKMPTHW GPHDGDKGIR KDAAMVAEYR EKCGPDFWLM LDCWMSQDVN YATKLAYACA
     PYNLKWIEEC LPPQQYEGYR ELKRNAPPGM MVTSGEHHGT LQSFQTLSET GIDIMQPDVG
     WCGGLTTLVE VAAIAKARGQ LVVPHGSSVY SHHAVITFTN TPFSEFLMTS PDCSVLRPQF
     DPILINEPVP VNGRIHKSVL DKPGFGVELN RDCKLKRPYT H