IMAND_CLOB8
ID IMAND_CLOB8 Reviewed; 399 AA.
AC A6M2W4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=D-galactonate dehydratase family member Cbei_4837;
GN OrderedLocusNames=Cbei_4837;
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-398 IN COMPLEX WITH MAGNESIUM.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of putative mandelate racemase/muconate lactonizing
RT protein from Clostridium beijerinckii NCIMB 8052.";
RL Submitted (APR-2009) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-399 IN COMPLEX WITH MAGNESIUM,
RP FUNCTION, AND LACK OF D-MANNONATE DEHYDRATASE ACTIVITY.
RC STRAIN=ATCC 51743 / NCIMB 8052;
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; CP000721; ABR36944.1; -; Genomic_DNA.
DR RefSeq; WP_012060989.1; NC_009617.1.
DR PDB; 3GY1; X-ray; 1.60 A; A/B=2-398.
DR PDB; 3S47; X-ray; 1.70 A; A/B=2-399.
DR PDBsum; 3GY1; -.
DR PDBsum; 3S47; -.
DR AlphaFoldDB; A6M2W4; -.
DR SMR; A6M2W4; -.
DR STRING; 290402.Cbei_4837; -.
DR DNASU; 5295990; -.
DR EnsemblBacteria; ABR36944; ABR36944; Cbei_4837.
DR KEGG; cbe:Cbei_4837; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_6_1_9; -.
DR OMA; DWDTRAY; -.
DR OrthoDB; 1825548at2; -.
DR EvolutionaryTrace; A6M2W4; -.
DR Proteomes; UP000000565; 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 Cbei_4837"
FT /id="PRO_0000429903"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24697546, ECO:0000269|Ref.2"
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, ECO:0000269|Ref.2"
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, ECO:0000269|Ref.2"
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:3GY1"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3S47"
FT HELIX 178..196
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:3GY1"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:3GY1"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3GY1"
SQ SEQUENCE 399 AA; 45262 MW; D24C80EB2A142995 CRC64;
MEPTIITDVL CYITKPDRHN LVVVKVETNK GIYGLGCATF QQRPKAVSLV VSEYLKPILI
GRDANNIEDL WQMMMVNSYW RNGPILNNAI SGVDMALWDI KGKLANMPLY QLFGGKSRDA
IAAYTHAVAD NLEDLYTEID EIRKKGYQHI RCQLGFYGGN SSEFHTTDNP TQGSYFDQDE
YMRTTVSMFS SLREKYGYKF HILHDVHERL FPNQAVQFAK DVEKYKPYFI EDILPPDQNE
WLGQIRSQTS TPLATGELFN NPMEWKSLIA NRQVDFIRCH VSQIGGITPA LKLGSLCAAF
GVRIAWHTPS DITPIGVAVN IHLNINLHNA AIQENIEIND NTRCVFSGIP EAKNGFFYPI
ESPGIGVDID ENEIIKYPVE YRPHEWTQSR IPDGTIVTP
