ID   OTNI_HAEIN              Reviewed;         258 AA.
AC   Q57151;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; OrderedLocusNames=HI_1013;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
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; L42023; AAC22674.1; -; Genomic_DNA.
DR   PIR; C64108; C64108.
DR   RefSeq; NP_439174.1; NC_000907.1.
DR   RefSeq; WP_005693349.1; NC_000907.1.
DR   AlphaFoldDB; Q57151; -.
DR   SMR; Q57151; -.
DR   STRING; 71421.HI_1013; -.
DR   EnsemblBacteria; AAC22674; AAC22674; HI_1013.
DR   KEGG; hin:HI_1013; -.
DR   PATRIC; fig|71421.8.peg.1057; -.
DR   eggNOG; COG3622; Bacteria.
DR   HOGENOM; CLU_050006_1_2_6; -.
DR   OMA; CEYRPRA; -.
DR   PhylomeDB; Q57151; -.
DR   BioCyc; HINF71421:G1GJ1-1053-MON; -.
DR   BioCyc; MetaCyc:MON-20183; -.
DR   Proteomes; UP000000579; 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   Carbohydrate metabolism; Isomerase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..258
FT                   /note="2-oxo-tetronate isomerase"
FT                   /id="PRO_0000209110"
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   258 AA;  29348 MW;  94555C63D1E0D69F CRC64;
     MPKFAANLTM MFNEVPFLDR FEAAAKAGFK YVEFLWPYDY PAQELKAILD KHGLKVVLFN
     TPAGDVNKGE WGGSAIPGRE ADSHRDIDLA LEYALALGCP NVHIMSAVVP EGASREEYKQ
     TFIKNVRYAS DKYKPYGIKI QLEALSPEVK PNYLLKSQFD TLEVVELVDR DNVFVQLDYF
     HAQNVDGNLA RLTDKLNGKF AHVQIASVPD RHEPDEGEIN YQYIFDKLDE IGYTGYVGCE
     YKPRGETVTG LDWFQKYK