ID   IMND2_VIBCY             Reviewed;         399 AA.
AC   A6AMN2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=D-galactonate dehydratase family member A1Q3065;
GN   ORFNames=A1Q_3065;
OS   Vibrio campbellii (strain HY01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=410291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HY01;
RA   Heidelberg J., Sebastian Y.;
RT   "Annotation of Vibrio harveyi HY01.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=HY01;
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; AAWP01000007; EDL70093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6AMN2; -.
DR   SMR; A6AMN2; -.
DR   HOGENOM; CLU_030273_6_1_6; -.
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 A1Q3065"
FT                   /id="PRO_0000429919"
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;  45420 MW;  CCB5C686926427F1 CRC64;
     MNKNTISNIE CVITKPDRHN LITVIVETES GVTGYGCATF QQRPLAVKTM VDEYLKPLLI
     GKDANNIEDL WQMMMVNAYW RNGPVINNAI SGVDMALWDI KAKLANMPLH QLFGGKSRDA
     IQVYTHATSD TMEGLYEQVD KYLEQGYQHI RCQLGFYGGV PENIQTAQNP TQGSYYDQDQ
     YIENTVEMFK NLREKYGKQF HILHDVHERL FPNQAIQFAK QVEQYNPFFI EDILPPSQTE
     WLDNIRNQSS VSLALGELFN NPEEWKALII NRRVDFIRCH VSQIGGITPA LKLGHFCESF
     GVRIAWHCPP DMTPIGAAVN THLNVHLHNA AIQEHVEYKA NTQRVFPNAA EPINGYLYAS
     EIAGIGVEMD CEAAQDFPVE YRPHEWTQSR LPDGSIHTP