ID   IMAND_CROTZ             Reviewed;         399 AA.
AC   C9Y5D5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=D-galactonate dehydratase family member Ctu_1p00430;
GN   OrderedLocusNames=Ctu_1p00430;
OS   Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OG   Plasmid pCTU1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
RX   PubMed=21037008; DOI=10.1128/jb.01162-10;
RA   Stephan R., Lehner A., Tischler P., Rattei T.;
RT   "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT   pathogen causing deaths in neonates.";
RL   J. Bacteriol. 193:309-310(2011).
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032;
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; FN543094; CBA34580.1; -; Genomic_DNA.
DR   RefSeq; WP_012815801.1; NC_013283.1.
DR   AlphaFoldDB; C9Y5D5; -.
DR   SMR; C9Y5D5; -.
DR   EnsemblBacteria; CBA34580; CBA34580; Ctu_1p00430.
DR   GeneID; 60374574; -.
DR   KEGG; ctu:Ctu_1p00430; -.
DR   PATRIC; fig|693216.3.peg.4037; -.
DR   HOGENOM; CLU_030273_6_1_6; -.
DR   OMA; MVNAYWR; -.
DR   Proteomes; UP000002069; Plasmid pCTU1.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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; 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.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Metal-binding; Plasmid.
FT   CHAIN           1..399
FT                   /note="D-galactonate dehydratase family member Ctu_1p00430"
FT                   /id="PRO_0000429905"
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;  44861 MW;  8FF9117D558BD300 CRC64;
     MTPVIIKNIE CFITRPDRHN LVTVRVTTDQ GVTGHGCATF QQRPLAVKTL VEEYLQPLLT
     GRDANNIEDL WQMMNVNAYW RNGPVMNNAI SGVDMALWDI KSQLAGMPLY QLFGGKSRDA
     IPAYSHASGD TLDALFASVD ALIEKGYRHI RCQLGFYGGT ASGLHAPENP TPGAWFDQQE
     YMSNTVDMFR ALREKYGWKL HILHDVHERL FPQQAIQLAK QLEPYQPYFI EDILPPQQSA
     WLEQVRQHSC VPLAMGELFN NPSEWHDLIV NRRIDFIRCH VSQIGGITPA LKLAHLCQAF
     GVRLAWHGPG DMTPVGVAVN THLNIHLHNA AIQEFIPRSA MTDKIFPGAP EVKDGFIYPP
     VNAGIGVGFN EELARAHPVM YRPHEWTQSR LPDGTLHTP