ID   IMAND_PSECP             Reviewed;         409 AA.
AC   B8HCK2;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=D-galactonate dehydratase family member Achl_0790;
GN   OrderedLocusNames=Achl_0790;
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC   13794 / A6;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
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; CP001341; ACL38785.1; -; Genomic_DNA.
DR   RefSeq; WP_015936010.1; NC_011886.1.
DR   AlphaFoldDB; B8HCK2; -.
DR   SMR; B8HCK2; -.
DR   STRING; 452863.Achl_0790; -.
DR   EnsemblBacteria; ACL38785; ACL38785; Achl_0790.
DR   KEGG; ach:Achl_0790; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_6_1_11; -.
DR   OMA; DWDTRAY; -.
DR   OrthoDB; 1825548at2; -.
DR   Proteomes; UP000002505; Chromosome.
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.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding.
FT   CHAIN           1..409
FT                   /note="D-galactonate dehydratase family member Achl_0790"
FT                   /id="PRO_0000429901"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="D-arabinonate"
FT                   /ligand_id="ChEBI:CHEBI:16157"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  45479 MW;  E63C85E53B271E5A CRC64;
     MKIIAADVFV TSPSRNFVTL RITTEDGVTG IGDATLNGRE LAVAAYLKEH VAQLLIGKDP
     HRIEDTWQFL YRSSYWRRGP VTMAAIAAVD MALWDIKGKV AGMPVYQLLG GASRNGLRAY
     GHASGADIPS LFDSVREHLE LGYKSIRIQT AVPGIKAVYG VAAQAQASGE RYDYEPAGRG
     AFPVEEDWDT RAYLRHLPSV FEAVRNEFGP EIPLLHDGHH RMTPIQAAKL GKALEPYDLF
     WLEDCTPAEN QEALRLVRQH TTTPLAIGEI FNTVYDYQTI IKEQLIDYVR AASTHFGGIS
     PLKKVMDFAA QYQIKSGFHG PTDISPVGFA AQLHVGLAIH NYGIQEYMQH SDKTNEVFHQ
     SMTFKDGYLH PGDEPGIGVE FNEEAAAAFP YQQAYLPYNR LVDGTVHDW