OTNI_ECOLI
ID OTNI_ECOLI Reviewed; 258 AA.
AC Q46891; Q2MA90;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=2-oxo-tetronate isomerase {ECO:0000250|UniProtKB:Q57151};
DE EC=5.3.1.35 {ECO:0000250|UniProtKB:Q57151};
DE AltName: Full=2-dehydrotetronate isomerase {ECO:0000305};
DE AltName: Full=Glyoxylate-induced protein YgbM;
GN Name=otnI {ECO:0000250|UniProtKB:Q57151}; Synonyms=ygbM;
GN OrderedLocusNames=b2739, JW2709;
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=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 [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RX PubMed=12112708; DOI=10.1002/prot.10160;
RA Kim Y., Skarina T., Beasley S., Laskowski R., Arrowsmith C., Joachimiak A.,
RA Edwards A., Savchenko A.;
RT "Crystal structure of Escherichia coli EC1530, a glyoxylate induced protein
RT YgbM.";
RL Proteins 48:427-430(2002).
CC -!- FUNCTION: Catalyzes the isomerization of 2-oxo-tetronate to 3-oxo-
CC tetronate. {ECO:0000250|UniProtKB:Q57151}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-L-erythronate = 3-dehydro-L-erythronate;
CC Xref=Rhea:RHEA:52564, ChEBI:CHEBI:136669, ChEBI:CHEBI:136670;
CC EC=5.3.1.35; Evidence={ECO:0000250|UniProtKB:Q57151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-D-erythronate = 3-dehydro-D-erythronate;
CC Xref=Rhea:RHEA:52560, ChEBI:CHEBI:57958, ChEBI:CHEBI:136668;
CC EC=5.3.1.35; Evidence={ECO:0000250|UniProtKB:Q57151};
CC -!- SIMILARITY: Belongs to the hyi family. OtnI subfamily. {ECO:0000305}.
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DR EMBL; U29579; AAA69249.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75781.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76816.1; -; Genomic_DNA.
DR PIR; G65054; G65054.
DR RefSeq; NP_417219.1; NC_000913.3.
DR RefSeq; WP_001136934.1; NZ_LN832404.1.
DR PDB; 1K77; X-ray; 1.63 A; A=1-258.
DR PDBsum; 1K77; -.
DR AlphaFoldDB; Q46891; -.
DR SMR; Q46891; -.
DR BioGRID; 4261446; 5.
DR IntAct; Q46891; 1.
DR STRING; 511145.b2739; -.
DR DrugBank; DB01942; Formic acid.
DR jPOST; Q46891; -.
DR PaxDb; Q46891; -.
DR PRIDE; Q46891; -.
DR EnsemblBacteria; AAC75781; AAC75781; b2739.
DR EnsemblBacteria; BAE76816; BAE76816; BAE76816.
DR GeneID; 947207; -.
DR KEGG; ecj:JW2709; -.
DR KEGG; eco:b2739; -.
DR PATRIC; fig|511145.12.peg.2833; -.
DR EchoBASE; EB2910; -.
DR eggNOG; COG3622; Bacteria.
DR HOGENOM; CLU_050006_1_2_6; -.
DR InParanoid; Q46891; -.
DR OMA; CEYRPRA; -.
DR PhylomeDB; Q46891; -.
DR BioCyc; EcoCyc:G7420-MON; -.
DR EvolutionaryTrace; Q46891; -.
DR PRO; PR:Q46891; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008903; F:hydroxypyruvate isomerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046487; P:glyoxylate metabolic process; IBA:GO_Central.
DR InterPro; IPR026040; HyI-like.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PIRSF; PIRSF006241; HyI; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..258
FT /note="2-oxo-tetronate isomerase"
FT /id="PRO_0000209109"
FT ACT_SITE 143
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 240
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12112708,
FT ECO:0007744|PDB:1K77"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12112708,
FT ECO:0007744|PDB:1K77"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12112708,
FT ECO:0007744|PDB:1K77"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:12112708,
FT ECO:0007744|PDB:1K77"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1K77"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1K77"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1K77"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1K77"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:1K77"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1K77"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1K77"
SQ SEQUENCE 258 AA; 29217 MW; 07392B724316D7DD CRC64;
MPRFAANLSM MFTEVPFIER FAAARKAGFD AVEFLFPYNY STLQIQKQLE QNHLTLALFN
TAPGDINAGE WGLSALPGRE HEAHADIDLA LEYALALNCE QVHVMAGVVP AGEDAERYRA
VFIDNIRYAA DRFAPHGKRI LVEALSPGVK PHYLFSSQYQ ALAIVEEVAR DNVFIQLDTF
HAQKVDGNLT HLIRDYAGKY AHVQIAGLPD RHEPDDGEIN YPWLFRLFDE VGYQGWIGCE
YKPRGLTEEG LGWFDAWR
