ID   OIAK_PARG4              Reviewed;         470 AA.
AC   B1G889;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=3-oxo-isoapionate kinase {ECO:0000303|PubMed:29867142};
DE            EC=2.7.1.231 {ECO:0000269|PubMed:29867142};
GN   Name=oiaK {ECO:0000303|PubMed:29867142};
GN   ORFNames=BgramDRAFT_5557 {ECO:0000312|EMBL:EDT07588.1};
OS   Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 /
OS   NCIMB 13744 / C4D1M).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=396598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Tiedje J., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Burkholderia graminis
RT   C4D1M.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA   Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA   Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA   Andersen H.M., Almo S.C., Gerlt J.A.;
RT   "Functional assignment of multiple catabolic pathways for D-apiose.";
RL   Nat. Chem. Biol. 14:696-705(2018).
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the
CC       phosphorylation of 3-oxo-isoapionate to 3-oxo-isoapionate 4-phosphate.
CC       {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoisoapionate + ATP = 3-oxoisoapionate 4-phosphate + ADP +
CC         H(+); Xref=Rhea:RHEA:57068, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:141353, ChEBI:CHEBI:141357, ChEBI:CHEBI:456216;
CC         EC=2.7.1.231; Evidence={ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC       {ECO:0000305}.
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DR   EMBL; ABLD01000025; EDT07588.1; -; Genomic_DNA.
DR   RefSeq; WP_006052126.1; NZ_CADIKA010000024.1.
DR   AlphaFoldDB; B1G889; -.
DR   SMR; B1G889; -.
DR   EnsemblBacteria; EDT07588; EDT07588; BgramDRAFT_5557.
DR   BioCyc; MetaCyc:MON-20965; -.
DR   BRENDA; 2.7.1.231; 12477.
DR   Proteomes; UP000005045; Unassembled WGS sequence.
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   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..470
FT                   /note="3-oxo-isoapionate kinase"
FT                   /id="PRO_0000446040"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q6D0N7"
FT   BINDING         291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         403..406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         451
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ   SEQUENCE   470 AA;  49606 MW;  D30E604EAFBA2FAD CRC64;
     MNGTEPAEPT NGTNATAWPA GLLLAYYGDD FTGSTDAMEA MQAAGVPTVL CLQKPTPELL
     ARFPEVRCVG MAGSSRGRSS AWMDDELPDV LASLAALGAP ILQYKVCSTF DSSPEVGSIG
     RAIDIGVRHM PGNWSPMVIG APRLKRYQMF GNLFAAVDGV GYRLDRHPTM SRHPVTPMNE
     ADLRLHLARQ TARRIELIDM LELRGADVAT RVRALCAPDM PVVLIDVLDE ETLAEAGRLV
     WEQRGEGIFT ASSSGLQYAL AAHWRARGLL PPTPSLPAAD PVQAIAAVSG SCSPVTAAQI
     GWARAHGFHT ERLDLPRALD SRDGAAEIER VVTAATQALT RGISVIVHSA EGPDDPAVTG
     FDAIASAAGF ARHDAARKVG RALAEVMRRL LDSVELTRVV VAGGDSSGEV ASVLGIDALS
     VMAGLVPGAP LCRAWSAEPR RDGLQIVLKG GQIGDATFFG MVREGRLAGA