ID   IMAND_PECPW             Reviewed;         399 AA.
AC   D0KC90;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=D-galactonate dehydratase family member Pecwa_4254;
GN   OrderedLocusNames=Pecwa_4254;
OS   Pectobacterium parmentieri (strain WPP163) (Pectobacterium wasabiae (strain
OS   WPP163)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WPP163;
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., Ovchinnikova G.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium wasabiae WPP163.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=WPP163;
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; CP001790; ACX89978.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0KC90; -.
DR   SMR; D0KC90; -.
DR   KEGG; pwa:Pecwa_4254; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_6; -.
DR   OMA; MVNAYWR; -.
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   SFLD; SFLDG00033; mannonate_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   Magnesium; Metal-binding.
FT   CHAIN           1..399
FT                   /note="D-galactonate dehydratase family member Pecwa_4254"
FT                   /id="PRO_0000429913"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         278
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45150 MW;  CD8125B10C9E6692 CRC64;
     MLPTIITDIE CLVTRPDRHN LVTVVVHTNK GVTGYGCATF QQRPLAVKAM VDEYLKPLLV
     GRDANHIEDL WHMMMVNAYW RNGPVINNAV AGVDMALWDI KGKLADMPLY HLFGGKSRDA
     IAAYSHAASD TLDGLYQEVE RLYAQGYRHI RCQLGFYGGN PDALHSTRQP TEGAYYDQDQ
     YMANTLAMFR ALREKYGDRF HILHDVHERL FPNQAVQFAK AVETYRPYFI EDILPPAQNE
     WLAQIRSQSA VPLATGELFN NPAEWQNLVI NRQVDFIRCH VSQIGGITPA LKLGVFCQNF
     GVRLAWHCPP DMTPIGAAVN IHLNIHLHNA AIQEFVAYPE NTRKVFPQAV EPENGYLYPI
     ERPGIGVGID LDAARQFPVV YRPHEWTQSR LPDGTIHTP