ID   IMAND_ENT38             Reviewed;         399 AA.
AC   A4W7D6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=D-galactonate dehydratase family member Ent638_0932;
GN   OrderedLocusNames=Ent638_0932;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, SUBUNIT,
RP   AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=638;
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   -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:24697546}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. GalD subfamily. {ECO:0000305}.
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DR   EMBL; CP000653; ABP59616.1; -; Genomic_DNA.
DR   RefSeq; WP_012016337.1; NC_009436.1.
DR   PDB; 3TJI; X-ray; 1.80 A; A/B/C/D=1-399.
DR   PDBsum; 3TJI; -.
DR   AlphaFoldDB; A4W7D6; -.
DR   SMR; A4W7D6; -.
DR   STRING; 399742.Ent638_0932; -.
DR   EnsemblBacteria; ABP59616; ABP59616; Ent638_0932.
DR   KEGG; ent:Ent638_0932; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_6; -.
DR   OMA; MVNAYWR; -.
DR   OrthoDB; 1825548at2; -.
DR   Proteomes; UP000000230; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IDA: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   1: Evidence at protein level;
KW   3D-structure; Magnesium; Metal-binding.
FT   CHAIN           1..399
FT                   /note="D-galactonate dehydratase family member Ent638_0932"
FT                   /id="PRO_0000429906"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:24697546"
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:0000269|PubMed:24697546"
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:0000269|PubMed:24697546"
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"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          34..37
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           55..59
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           84..105
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          121..131
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           132..144
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           161..163
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           178..196
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          198..205
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           212..222
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          228..231
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           236..241
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           242..248
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           266..270
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          275..277
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           287..299
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           314..326
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           340..345
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          362..365
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           371..375
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   HELIX           385..387
FT                   /evidence="ECO:0007829|PDB:3TJI"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:3TJI"
SQ   SEQUENCE   399 AA;  44684 MW;  AEB210294864550F CRC64;
     MTPVIIKNIE CFITRPDRHN LVTVRVTTEQ GITGHGCATF QQRPLAVKTL VDEYLQPLMI
     GRDANNIEDL WQMMNVNAYW RNGPLMNNAI SGVDMALWDI KGQLAGMPLY QLFGGKSRDA
     IPAYSHASGE TLEALFASVD ALIAQGYRHI RCQLGFYGGT PSALHAPDNP TPGAWFDQQE
     YMSNTVEMFH ALREKYGWKL HILHDVHERL FPQQAVQLAK QLEPFQPYFI EDILPPQQSA
     WLEQVRQQSC VPLALGELFN NPAEWHDLIV NRRIDFIRCH VSQIGGITPA LKLAHLCQAF
     GVRLAWHGPG DMTPIGVAVN THLNIHLHNA AIQEFIPRSA TTNDVFPGAP EVKEGFVYPP
     VQPGIGVGFN EALALAHPVL YRPHEWTQSR LPDGTIHTP