ID   IMAND_OCEGH             Reviewed;         408 AA.
AC   Q2CIN0;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=D-galactonate dehydratase family member OG2516_05608;
GN   ORFNames=OG2516_05608;
OS   Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS   HTCC2516).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Oceanicola.
OX   NCBI_TaxID=314256;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516;
RX   PubMed=20418400; DOI=10.1128/jb.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516;
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; AAOT01000003; EAR52559.1; -; Genomic_DNA.
DR   RefSeq; WP_007254649.1; NZ_CH724107.1.
DR   AlphaFoldDB; Q2CIN0; -.
DR   SMR; Q2CIN0; -.
DR   STRING; 314256.OG2516_05608; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_5; -.
DR   OMA; EYMRHTE; -.
DR   OrthoDB; 1825548at2; -.
DR   Proteomes; UP000003635; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..408
FT                   /note="D-galactonate dehydratase family member
FT                   OG2516_05608"
FT                   /id="PRO_0000429915"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  45331 MW;  EDD15D5E00240584 CRC64;
     MKITDAKVFV GGPGKNYVTV KVMTDSGVYG LGDATLNNRE TLPAKYLTDY LVPNLIGMDP
     RRSEDIWQFL YRGAYFRRGP VAMAAFGAID MALWDIKGKL ADMPLYQLFG GKSRDGAMVY
     GHATGADLED LMDSIAHYVE QGYKAVRVQC GIPGMPTASY AVPEERGASK HYISDFSGIR
     PKTEIWDSGK YLRWMPGALM AIRERFGPDL HILHDVHHRL TPREAAQFAK AVEPVDLYWL
     EDPTPAEDQA ALRLVRQHST TPIAIGEVFN SIWECNKLIE EELIDFIRVA ATYAGGITHV
     KRIVDLAGLH HVRTGFHGAP SHSPLCMAAH AHLNAWAPNF GIQEYLVLGT PDCDALFPSD
     HRMEDGMVHV SDAPGLGVDF DEAEAARYEY RPGSHPVVRL TDGTMWDY