ID   RHMD_SACEN              Reviewed;         390 AA.
AC   A4FLW9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=SACE_5860;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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   -!- 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; AM420293; CAM05044.1; -; Genomic_DNA.
DR   RefSeq; WP_009943127.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FLW9; -.
DR   SMR; A4FLW9; -.
DR   STRING; 405948.SACE_5860; -.
DR   EnsemblBacteria; CAM05044; CAM05044; SACE_5860.
DR   KEGG; sen:SACE_5860; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_1_0_11; -.
DR   OMA; CEAYYIP; -.
DR   OrthoDB; 743369at2; -.
DR   Proteomes; UP000006728; 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..390
FT                   /note="L-rhamnonate dehydratase"
FT                   /id="PRO_0000351702"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         211
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         265
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   BINDING         335
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   SITE            288
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
FT   SITE            335
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01288"
SQ   SEQUENCE   390 AA;  43636 MW;  634FEA9500D50A24 CRC64;
     MKIRQVRALT VTGGGADYHD QAEDHWIDDH VATPMAKYPE YRASRQAFGI NVLGTLVVEV
     EAEDGTVGVG VTTAGEPGAY IVEKHLARFV EGASVTDVEK IWDQMFNATL YYGRKGLVLN
     AISAVDLALY DLLGKIRQEP VYALLGGPVR DELQCYATTG RPDVAKELGF LGGKMTLQHG
     PAEGVEGLHA NIERLRKMRE QVGPDFWLMF DCWMALDVEY ATRLAHAAAE YDLKWLEEAL
     IPDDYWGYGE LRRRMPSTML MTTGEHEHTR YGFRLLLEMG RPDIIQPDVN WCGGITELIK
     ISALADAHGA MVVPHGSSVY SYHFVITRHN SPFTEFLMMH PQATEVVPMF SPLLLDEPVP
     VGGRLRLPET PGFGVRLNPE VELRRPYDHD