IDND_ECOLI
ID IDND_ECOLI Reviewed; 343 AA.
AC P39346; Q2M642;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=L-idonate 5-dehydrogenase (NAD(P)(+));
DE EC=1.1.1.264;
GN Name=idnD; Synonyms=yjgV; OrderedLocusNames=b4267, JW4224;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9658018; DOI=10.1128/jb.180.14.3704-3710.1998;
RA Bausch C., Peekhaus N., Utz C., Blais T., Murray E., Lowary T., Conway T.;
RT "Sequence analysis of the GntII (subsidiary) system for gluconate
RT metabolism reveals a novel pathway for L-idonic acid catabolism in
RT Escherichia coli.";
RL J. Bacteriol. 180:3704-3710(1998).
CC -!- FUNCTION: Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to
CC 5-ketogluconate (5KG). {ECO:0000269|PubMed:9658018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-idonate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH;
CC Xref=Rhea:RHEA:21176, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58143, ChEBI:CHEBI:58349;
CC EC=1.1.1.264; Evidence={ECO:0000269|PubMed:9658018};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-idonate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH;
CC Xref=Rhea:RHEA:21172, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58143;
CC EC=1.1.1.264; Evidence={ECO:0000269|PubMed:9658018};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate acid metabolism; L-idonate degradation.
CC -!- INTERACTION:
CC P39346; P0A9P0: lpdA; NbExp=2; IntAct=EBI-552913, EBI-542856;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14003; AAA97164.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77224.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78264.1; -; Genomic_DNA.
DR PIR; S56493; S56493.
DR RefSeq; NP_418688.1; NC_000913.3.
DR RefSeq; WP_001197411.1; NZ_SSUV01000014.1.
DR PDB; 6DKH; X-ray; 2.61 A; A/B/C/D=1-343.
DR PDBsum; 6DKH; -.
DR AlphaFoldDB; P39346; -.
DR SMR; P39346; -.
DR BioGRID; 4259666; 722.
DR DIP; DIP-10010N; -.
DR IntAct; P39346; 5.
DR STRING; 511145.b4267; -.
DR PaxDb; P39346; -.
DR PRIDE; P39346; -.
DR EnsemblBacteria; AAC77224; AAC77224; b4267.
DR EnsemblBacteria; BAE78264; BAE78264; BAE78264.
DR GeneID; 944769; -.
DR KEGG; ecj:JW4224; -.
DR KEGG; eco:b4267; -.
DR PATRIC; fig|1411691.4.peg.2436; -.
DR EchoBASE; EB2430; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_5_6; -.
DR InParanoid; P39346; -.
DR OMA; EYKSGHY; -.
DR PhylomeDB; P39346; -.
DR BioCyc; EcoCyc:IDONDEHYD-MON; -.
DR BioCyc; MetaCyc:IDONDEHYD-MON; -.
DR BRENDA; 1.1.1.264; 2026.
DR UniPathway; UPA00793; -.
DR PRO; PR:P39346; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0050572; F:L-idonate 5-dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0102198; F:L-idonate 5-dehydrogenase activity (NAD-dependent); IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046183; P:L-idonate catabolic process; IMP:EcoCyc.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gluconate utilization; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..343
FT /note="L-idonate 5-dehydrogenase (NAD(P)(+))"
FT /id="PRO_0000160881"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT STRAND 1..12
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 15..25
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 27..39
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6DKH"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:6DKH"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:6DKH"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:6DKH"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:6DKH"
SQ SEQUENCE 343 AA; 37147 MW; 7A3C6E6C0CED6F09 CRC64;
MQVKTQSCVV AGKKTVAVTE QTIDWNNNGT LVQITRGGIC GSDLHYYQEG KVGNFMIKAP
MVLGHEVIGK VIHSDSSELH EGQTVAINPS KPCGHCKYCI EHNENQCTDM RFFGSAMYFP
HVDGGFTRYK MVETSQCVPY PAKADEKVMA FAEPLAVAIH AAHQAGELQG KRVFISGVGP
IGCLIVSAVK TLGAAEIVCA DVSPRSLSLG KEMGADVLVN PQNDDMDHWK AEKGYFDVSF
EVSGHPSSVN TCLEVTRARG VMVQVGMGGA MAEFPMMTLI GKEISLRGSF RFTSEFNTAV
SWLANGVINP LPLLSAEYPF TDLEEALRFA GDKTQAAKVQ LVF
