IMND1_ENTGE
ID IMND1_ENTGE Reviewed; 399 AA.
AC C8ZZN2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=D-galactonate dehydratase family member EGBG_01401;
GN ORFNames=EGBG_01401;
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 X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, FUNCTION,
RP 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; GG670287; EEV32799.1; -; Genomic_DNA.
DR RefSeq; WP_003127127.1; NZ_GG670287.1.
DR PDB; 4HNL; X-ray; 1.48 A; A=1-399.
DR PDBsum; 4HNL; -.
DR AlphaFoldDB; C8ZZN2; -.
DR SMR; C8ZZN2; -.
DR STRING; 565653.EGBG_01401; -.
DR PRIDE; C8ZZN2; -.
DR EnsemblBacteria; EEV32799; EEV32799; EGBG_01401.
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; 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 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 EGBG_01401"
FT /id="PRO_0000429908"
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:4HNL"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 178..196
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:4HNL"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:4HNL"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4HNL"
SQ SEQUENCE 399 AA; 44846 MW; CAAF2A6A9E0417D1 CRC64;
MTPTIITDVK SFAIKPDRHN LVVVKVETNK GISGLGCSTF QFRPLAVKTV VDEYLRPLLM
GRDANEIEDI WQVMNVNSYW RNGPITNNAI SGIDMALWDI KGQLADMPLY QLLGGKARTA
IPAYTHAVAD NLDDLYHEID RFLAAGYRYI RCQLGFYGGN PSQLQTPEEP ISGSYFDQTD
YMETTLKMFA AIKEKYGNQF QMLHDVHERL HPNQAIQFAK AAEPYQLFFL EDILPPDQSH
WLTQLRSQSA TPIATGELFN NPMEWQELVK NRQIDFMRAH VSQIGGITPA LKLAHFCDAM
GVRIAWHTPS DISPVGLAVN THLNIHLHNA AIQETIELPA NTQSVFVGSP QPKGGFFYPM
EKSGIGITFD EEAAADFPVV YRPHEWTQSR TPDGTLITP
