ID   IMAND_PAESJ             Reviewed;         407 AA.
AC   C6CVY9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=D-galactonate dehydratase family member Pjdr2_1176;
GN   OrderedLocusNames=Pjdr2_1176;
OS   Paenibacillus sp. (strain JDR-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=324057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDR-2;
RX   PubMed=22675593; DOI=10.4056/sigs.2374349;
RA   Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA   Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S., Nolan M.,
RA   Pati A., Martin J., Copeland A., Land M.L., Goodwin L., Jones J.B.,
RA   Ingram L.O., Shanmugam K.T., Preston J.F.;
RT   "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL   Stand. Genomic Sci. 6:1-10(2012).
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=JDR-2;
RX   PubMed=24697546; DOI=10.1021/bi500264p;
RA   Wichelecki D.J., Balthazor B.M., Chau A.C., Vetting M.W., Fedorov A.A.,
RA   Fedorov E.V., Lukk T., Patskovsky Y.V., Stead M.B., Hillerich B.S.,
RA   Seidel R.D., Almo S.C., Gerlt J.A.;
RT   "Discovery of function in the enolase superfamily: D-mannonate and D-
RT   gluconate dehydratases in the D-mannonate dehydratase subgroup.";
RL   Biochemistry 53:2722-2731(2014).
CC   -!- FUNCTION: Has no detectable activity with D-mannonate and with a panel
CC       of 70 other acid sugars (in vitro), in spite of the conservation of the
CC       residues that are expected to be important for catalytic activity and
CC       cofactor binding. May have evolved a divergent function.
CC       {ECO:0000269|PubMed:24697546}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000305}.
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DR   EMBL; CP001656; ACS99853.1; -; Genomic_DNA.
DR   RefSeq; WP_015842800.1; NC_012914.1.
DR   AlphaFoldDB; C6CVY9; -.
DR   SMR; C6CVY9; -.
DR   STRING; 324057.Pjdr2_1176; -.
DR   EnsemblBacteria; ACS99853; ACS99853; Pjdr2_1176.
DR   KEGG; pjd:Pjdr2_1176; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_9; -.
DR   OMA; DWDTRAY; -.
DR   OrthoDB; 1825548at2; -.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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   InterPro; IPR034589; D-mannonate_dehydratase-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR034593; Mandelate_racemase_DgoD-like.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; PTHR48080; 1.
DR   PANTHER; PTHR48080:SF6; PTHR48080:SF6; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 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   Magnesium; Metal-binding.
FT   CHAIN           1..407
FT                   /note="D-galactonate dehydratase family member Pjdr2_1176"
FT                   /id="PRO_0000429910"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  45281 MW;  51475A1D14807304 CRC64;
     MAKITGIECI RTRKNGTWTI VKVMTDQDGL YGLGSASDVY NPEAVVQIIE QLLAPLLIGK
     DAANIEDLWQ TMYMSGYWRN GALLHTAIGG IDMALWDIKG KEAGLPVYQL LGGACRAAVP
     CYGHAGGKDI AELKEDVHRF IEEGYTVIRV QMGGYGGGGF IDRDKANIPQ QAWGSGPVFD
     EQSYLHAIPH MFEQLRNEFG MGVQFTHDVH EHLTPVNAIQ LAKRVEPYSL FFLEDAIAPE
     QIGWYRHLRQ QSATPQAVGE LFVNPQEWTQ LIKEQLIDFI RVRVSKAGGI SACRKIAALA
     EAFGVRTAWQ EGGENDPVNQ AAAVHLDMAI WNFGIQEVNH FKPEEKDAFE GHIERKGGYL
     YPSQKPGLGI ELDELKAQQL LGEGWSKSVY FNPYQLDRKA DGTLVRP