OTNK_CUPNH
ID OTNK_CUPNH Reviewed; 432 AA.
AC Q0KBC8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=3-oxo-tetronate kinase {ECO:0000303|PubMed:27402745};
DE EC=2.7.1.217 {ECO:0000269|PubMed:27402745};
DE AltName: Full=3-dehydrotetronate 4-kinase {ECO:0000305};
GN Name=otnK {ECO:0000303|PubMed:27402745};
GN OrderedLocusNames=H16_A1561 {ECO:0000312|EMBL:CAJ92693.1};
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).
RN [3] {ECO:0007744|PDB:5DMH}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ADP.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RA Vetting M.W., Al Obaidi N.F., Morisco L.L., Benach J., Wasserman S.R.,
RA Attonito J.D., Chamala S., Chowdhury S., Love J., Seidel R.D., Whalen K.L.,
RA Gerlt J.A., Almo S.C.;
RT "Crystal structure of a domain of unknown function (DUF1537) from Ralstonia
RT eutropha H16 (H16_A1561), Target EFI-511666, complex with ADP.";
RL Submitted (SEP-2015) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of 3-oxo-
CC tetronate to 3-oxo-tetronate 4-phosphate.
CC {ECO:0000269|PubMed:27402745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-L-erythronate + ATP = 3-dehydro-4-O-phospho-L-
CC erythronate + ADP + H(+); Xref=Rhea:RHEA:52552, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:136592, ChEBI:CHEBI:136670,
CC ChEBI:CHEBI:456216; EC=2.7.1.217;
CC Evidence={ECO:0000269|PubMed:27402745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-D-erythronate + ATP = 3-dehydro-4-O-phospho-D-
CC erythronate + ADP + H(+); Xref=Rhea:RHEA:52556, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57958, ChEBI:CHEBI:136593,
CC ChEBI:CHEBI:456216; EC=2.7.1.217;
CC Evidence={ECO:0000269|PubMed:27402745};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use L-threonate or
CC D-erythronate as a carbon source. {ECO:0000269|PubMed:27402745}.
CC -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
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DR EMBL; AM260479; CAJ92693.1; -; Genomic_DNA.
DR RefSeq; WP_011615151.1; NZ_CP039287.1.
DR PDB; 5DMH; X-ray; 1.80 A; A/B=1-432.
DR PDBsum; 5DMH; -.
DR AlphaFoldDB; Q0KBC8; -.
DR SMR; Q0KBC8; -.
DR STRING; 381666.H16_A1561; -.
DR EnsemblBacteria; CAJ92693; CAJ92693; H16_A1561.
DR GeneID; 57643660; -.
DR KEGG; reh:H16_A1561; -.
DR PATRIC; fig|381666.6.peg.1946; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_4; -.
DR OMA; CSVMTNK; -.
DR OrthoDB; 771666at2; -.
DR BioCyc; MetaCyc:MON-20189; -.
DR BRENDA; 2.7.1.217; 231.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10840; -; 1.
DR Gene3D; 3.40.980.20; -; 1.
DR InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR InterPro; IPR010737; DUF1537.
DR InterPro; IPR031475; NBD_C.
DR InterPro; IPR042213; NBD_C_sf.
DR Pfam; PF17042; NBD_C; 1.
DR Pfam; PF07005; SBD_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..432
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000439681"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 370..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|Ref.3"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:5DMH"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 340..360
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:5DMH"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5DMH"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:5DMH"
SQ SEQUENCE 432 AA; 44532 MW; 5140C560342EFA23 CRC64;
MTAGTLAHRP LLGCIADDFT GATDLANTLV RNGMRTVQTI GLPDVGAVQD IGEADALVVA
LKSRTIPAVE AVAQSLAALQ WLRAQGCRQF VFKYCSTFDS TDAGNIGPVA EALLAALDSD
FTIACPAFPE NGRTIFRGHL FVGDALLNES GMEHHPLTPM TDASLVRVLQ RQSKNKVGLL
RYDAVARGAH ATAERIAALR SDGVRMAIAD AVSDADLFTL GEACANLPLI TGGSGIALGL
PENFRRAGLL PQRGDAASVP AIDGPGVVLA GSASRATNGQ VARWLEQGRP ALRIDPLALA
RGEAVADAAL AFAAGHGEPV LIYATSSPDE VKAVQAELGV ERAGHLVEQC LATVAAGLLA
RGTRRFVVAG GETSGAVVQA LGVRALRIGA QIAPGVPATV TLDAKPLALA LKSGNFGGPD
FFDEALRQLG GH
