ID   OTNI_PECAS              Reviewed;         262 AA.
AC   Q6CZ23;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=2-oxo-tetronate isomerase {ECO:0000303|PubMed:27402745};
DE            EC=5.3.1.35 {ECO:0000269|PubMed:27402745};
DE   AltName: Full=2-dehydrotetronate isomerase {ECO:0000305};
GN   Name=otnI {ECO:0000303|PubMed:27402745};
GN   OrderedLocusNames=ECA4330 {ECO:0000312|EMBL:CAG77227.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=27402745; DOI=10.1073/pnas.1605546113;
RA   Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S.,
RA   Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V.,
RA   Jacobson M.P., Almo S.C., Gerlt J.A.;
RT   "Assignment of function to a domain of unknown function: DUF1537 is a new
RT   kinase family in catabolic pathways for acid sugars.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016).
CC   -!- FUNCTION: Catalyzes the isomerization of 2-oxo-tetronate to 3-oxo-
CC       tetronate. {ECO:0000269|PubMed:27402745}.
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:0000269|PubMed:27402745};
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:0000269|PubMed:27402745};
CC   -!- SIMILARITY: Belongs to the hyi family. OtnI subfamily. {ECO:0000305}.
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DR   EMBL; BX950851; CAG77227.1; -; Genomic_DNA.
DR   RefSeq; WP_011095794.1; NC_004547.2.
DR   AlphaFoldDB; Q6CZ23; -.
DR   SMR; Q6CZ23; -.
DR   STRING; 218491.ECA4330; -.
DR   EnsemblBacteria; CAG77227; CAG77227; ECA4330.
DR   GeneID; 57211023; -.
DR   KEGG; eca:ECA4330; -.
DR   PATRIC; fig|218491.5.peg.4409; -.
DR   eggNOG; COG3622; Bacteria.
DR   HOGENOM; CLU_050006_1_2_6; -.
DR   OMA; CEYRPRA; -.
DR   OrthoDB; 1007505at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..262
FT                   /note="2-oxo-tetronate isomerase"
FT                   /id="PRO_0000439754"
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:0000250|UniProtKB:Q46891"
FT   BINDING         178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q46891"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q46891"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q46891"
SQ   SEQUENCE   262 AA;  29345 MW;  C68522F1C7E33CF5 CRC64;
     MPKFAANLSM LFTDVPFLDR FKAAADAGFT SVEYLFPYEY PAPLLAEKLR ENGLKQVLFN
     TAPGNIAAGE WGVSALPDRI EDARRDIDNA LEYALALNCP SVLVMGGVVP PGEDRDAYQQ
     TFIDNLRYAA DKFAPHGINI MIEALSAKVK PNYLFASQYQ ALELANLIDR PNIYIQVDFF
     HAQIVDGNLT QIIHDLDGRI GHIQIASVPA RHEPDEGEIN YPFIFAELDR VNYSGWIGCE
     YNPRGKTEDG LGWAEPWLEK KH