ID   IMAND_ENTCS             Reviewed;         399 AA.
AC   C9CN91;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=D-galactonate dehydratase family member ECAG_02205;
GN   ORFNames=ECAG_02205;
OS   Enterococcus casseliflavus (strain EC10).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=565654;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC10;
RG   The Broad Institute Genome Sequencing Platform;
RA   Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RT   "The genome sequence of Enterococcus casseliflavus strain EC10 (892361).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=EC10;
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; GG692817; EEV36644.1; -; Genomic_DNA.
DR   RefSeq; WP_005228495.1; NZ_GG692817.1.
DR   AlphaFoldDB; C9CN91; -.
DR   SMR; C9CN91; -.
DR   EnsemblBacteria; EEV36644; EEV36644; ECAG_02205.
DR   HOGENOM; CLU_030273_6_1_9; -.
DR   Proteomes; UP000003948; Unassembled WGS sequence.
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..399
FT                   /note="D-galactonate dehydratase family member ECAG_02205"
FT                   /id="PRO_0000429907"
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;  44739 MW;  19961492E6B8A82A CRC64;
     MTPTIITDVK AFAIKPDRHN LVVVKVETNK GVSGLGCATF QFRPLAVKTV VDEYLRPLLL
     GRDANQIEDL WQVMNVNSYW RNGPITNNAI SGVDMALWDI KGQLADMPLY QLLGGKARTA
     IPAYTHAVAD NLEDLYQEID RFLAEGYRYI RCQLGFYGGN PSQLQTPDQP IAGSYFDQTD
     YMDTTLKMFA AIQERYGNQF QMLHDVHERL HPNQAIQFAK AAEPFNLFFL EDILPPDQNK
     WLQQLRSQSA TPIATGELFN NPMEWQELVK NQQIDFMRAH VSQIGGITPA LKLAHFCDAM
     GIRIAWHTPS DISPVGLAVN NHLNIHLHNA AIQETIAIPA NTQSVFGGSP QPENGYFYPI
     EKSGIGITFD EAAAAEFPVV YRPHEWTQSR TPDGTLITP