OTNI_CUPNH
ID OTNI_CUPNH Reviewed; 260 AA.
AC Q0KBD1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Synonyms=hyi1 {ECO:0000312|EMBL:CAJ92690.1};
GN OrderedLocusNames=H16_A1558 {ECO:0000312|EMBL:CAJ92690.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
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 -!- DISRUPTION PHENOTYPE: Deletion decreases growth with L-threonate or D-
CC erythronate as carbon source. Deletion of both otnI and hyi abolishes
CC growth with L-threonate or D-erythronate.
CC {ECO:0000269|PubMed:27402745}.
CC -!- SIMILARITY: Belongs to the hyi family. OtnI subfamily. {ECO:0000305}.
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DR EMBL; AM260479; CAJ92690.1; -; Genomic_DNA.
DR RefSeq; WP_010810014.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0KBD1; -.
DR SMR; Q0KBD1; -.
DR STRING; 381666.H16_A1558; -.
DR EnsemblBacteria; CAJ92690; CAJ92690; H16_A1558.
DR GeneID; 57643657; -.
DR KEGG; reh:H16_A1558; -.
DR PATRIC; fig|381666.6.peg.1943; -.
DR eggNOG; COG3622; Bacteria.
DR HOGENOM; CLU_050006_1_2_4; -.
DR OMA; CEYRPRA; -.
DR OrthoDB; 1007505at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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..260
FT /note="2-oxo-tetronate isomerase"
FT /id="PRO_0000439753"
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 260 AA; 28312 MW; 6EC65F6D4DB182BF CRC64;
MPRFAANLSM MYNEHAFLDR FAAAAADGFR AVEFLFPYEH AAAELRARLD ANGLTQALFN
AAPGDWAAGE RGLAALPGRE ADFRGTIGRA LEYAGVIGND RIHVMAGLIP ADADRARCRA
TYLENLAFAA NAAAAQGVTV LIEPINTRDM PGYFLNRQDD GQAICKEVGA ANLKVQFDCY
HCQIVEGDVA MKLKRDIAGI GHIQIAGVPE RHEPDVGELN YPYLFEVMDT LGYDGWIGCE
YRPRAGTSAG LGWLKPYLGR
