ID   IMND2_ENTGE             Reviewed;         402 AA.
AC   C9A1P5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=D-galactonate dehydratase family member EGBG_02030;
GN   ORFNames=EGBG_02030;
OS   Enterococcus gallinarum (strain EG2).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=565653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG2;
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 gallinarum strain EG2 (1,134,897).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC   STRAIN=EG2;
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; GG670289; EEV33428.1; -; Genomic_DNA.
DR   RefSeq; WP_003127878.1; NZ_GG670289.1.
DR   AlphaFoldDB; C9A1P5; -.
DR   SMR; C9A1P5; -.
DR   STRING; 565653.EGBG_02030; -.
DR   EnsemblBacteria; EEV33428; EEV33428; EGBG_02030.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_9; -.
DR   Proteomes; UP000003059; 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..402
FT                   /note="D-galactonate dehydratase family member EGBG_02030"
FT                   /id="PRO_0000429909"
FT   BINDING         207
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  44802 MW;  B3C40986A0491484 CRC64;
     MMKALVIEDI KVITTAPEGI NLVAVKVTTN DPSIYGVGCA TFTQRYEVVV TAIDKYLKPF
     LIGKDPQRIE DIWRTASVSS YWRNGPVLNN ALSGIDMALW DIKGKLANMP LYQLFGGKVR
     DAVPAYIHAD AQSVSDAVEL VQTRVDQGWK QIRVQIGGYG GNNQAMHLPK DNTPGVYYDP
     DVYMKTMIEG FEKLREKFGD SIKLCHDVHE RLSPSEAVKF ANQLEKFDLL FLEDALPPEQ
     VQWFEHLRSH TNIPLAMGEL FNNPHEWTGL IQNRTIDYLR LHLSQVGGIT PTRKIISLAD
     AYGVRTAWHG PGDMTGIGHA VNTHLSITST NFGIQEWSCS IKENTYKVFP GTPVAKDGYI
     YLNDQPGIGV DIDEEAAAAF PTHDRMADWT LCRLPDGSAG RP