(data stored in ACNUC29543 zone)

SWISSPROT: RHMD_PARP8

ID   RHMD_PARP8              Reviewed;         392 AA.
AC   B2JLI8;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
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};
GN   OrderedLocusNames=Bphy_3468;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- FUNCTION: Catalyzes the dehydration of L-rhamnonate to 2-keto-3-
CC       deoxy-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-
CC       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}.
DR   EMBL; CP001044; ACC72621.1; -; Genomic_DNA.
DR   RefSeq; WP_012402794.1; NC_010623.1.
DR   SMR; B2JLI8; -.
DR   STRING; 391038.Bphy_3468; -.
DR   EnsemblBacteria; ACC72621; ACC72621; Bphy_3468.
DR   GeneID; 27743146; -.
DR   KEGG; bph:Bphy_3468; -.
DR   eggNOG; ENOG4105CXK; Bacteria.
DR   eggNOG; COG4948; LUCA.
DR   HOGENOM; HOG000113755; -.
DR   KO; K12661; -.
DR   OMA; ERLDFYC; -.
DR   OrthoDB; 743369at2; -.
DR   BioCyc; BPHY391038:G1GBS-3567-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
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   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   PANTHER; PTHR13794:SF59; PTHR13794:SF59; 1.
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   PROSITE; PS00908; MR_MLE_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JLI8.
DR   SWISS-2DPAGE; B2JLI8.
KW   Complete proteome; Lyase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    392       L-rhamnonate dehydratase.
FT                                /FTId=PRO_0000351687.
FT   ACT_SITE    318    318       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   METAL       214    214       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   METAL       240    240       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   METAL       268    268       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   BINDING      22     22       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   BINDING      48     48       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   BINDING     338    338       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01288}.
FT   SITE        291    291       Increases basicity of active site His.
FT                                {ECO:0000255|HAMAP-Rule:MF_01288}.
FT   SITE        338    338       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_01288}.
SQ   SEQUENCE   392 AA;  43927 MW;  64ACC3B4117CA0FD CRC64;
     MAMPSIRHVR AFVVRGGGAD YHDQADGHWI DDHISTPMAR YPEYRQSRQS FGINVLGTLV
     VEIEASDGTV GFAVTTGGEI GAFIVEKHLA RFLEGQLVTD IEKMWDQMYF STLYYGRKGV
     VLNTISGVDL ALWDLLAKVR KEPVYQLLGG PVRDELQFYA TGARPDLAKE MGFIGGKLPL
     QHSPAEGEEG LRKNIDKLAE MRGRVGGDFW LMYDCWMSLD VTYATKLAKA AHEHGLKWIE
     EALPPDDYWG YAELRRNVPR GMMVSTGEHE ATRWGFRMLL EMGCCDLIQP DVGWCGGITE
     LVKISALADA HNVLVVPHGS SVYSYHFVVT RHNSPFAEFL MMAPKADQVV PMFTPLLLDE
     PVPVNGRMRV PDTPGFGVRL NPECKLERPY QH
//

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