ID   IMAND_ENTBW             Reviewed;         404 AA.
AC   A8RQK7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=D-galactonate dehydratase family member CLOBOL_02770;
GN   ORFNames=CLOBOL_02770;
OS   Enterocloster bolteae (strain ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM
OS   12243 / WAL 16351) (Clostridium bolteae).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=411902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM 12243 / WAL 16351;
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium bolteae (ATCC BAA-613).";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM 12243 / WAL 16351;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABCC02000026; EDP16856.1; -; Genomic_DNA.
DR   RefSeq; WP_002565301.1; NZ_DS480683.1.
DR   AlphaFoldDB; A8RQK7; -.
DR   SMR; A8RQK7; -.
DR   STRING; 411902.CLOBOL_02770; -.
DR   EnsemblBacteria; EDP16856; EDP16856; CLOBOL_02770.
DR   GeneID; 61858074; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_9; -.
DR   Proteomes; UP000005396; 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..404
FT                   /note="D-galactonate dehydratase family member
FT                   CLOBOL_02770"
FT                   /id="PRO_0000429904"
FT   BINDING         210
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  45758 MW;  B44E4CEE335B5412 CRC64;
     MDNITIRDIK VFVTAPRGIN LVIVKVETSE PELFGYGCAT FTWRHKAVVT AIEEYLCPML
     KGRSVHNIED IWQTMMGSSY WRNGPILNNA ISGVDEALWD IKGKLAGMPL YSLLGGKARE
     GVTVYRHADG GCLEEVKECI SRYIEEGYRH IRCHMGTYGG NFDGRRQQMV KPEGAPEGAY
     FHPKMYMDSV IRLFEQVRKD FGWELEVMHD VHERLSLADT LAFTKELEPF KLFFLEDSLA
     PDQVGYYKYM REQTAVPFAM GELFTNPAEW KTIIQNQWID FIRVHLSDIG GITPAVKLAH
     FCDAYGVRTA WHGPNDLSPI GMCAQMHLDL NSHNFGIQEF SGFTQEEEAV FPGCPKIRDG
     YAYVDDTPGI GVGFDEKEAA KYPAVDMDHS WLFARLPDGT AVRP