ID   DENK_HELMI              Reviewed;         439 AA.
AC   B0TBI9;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=D-erythronate kinase {ECO:0000303|PubMed:27402745};
DE            EC=2.7.1.220 {ECO:0000269|PubMed:27402745};
GN   Name=denK {ECO:0000303|PubMed:27402745};
GN   ORFNames=HM1_2673 {ECO:0000312|EMBL:ABZ85202.1};
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 51547 / Ice1;
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 ATP-dependent phosphorylation of D-erythronate
CC       to D-erythronate 4-phosphate. Can also phosphorylate D-threonate and 4-
CC       hydroxy-L-threonine, with lower efficiency.
CC       {ECO:0000269|PubMed:27402745}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-erythronate = 4-phospho-D-erythronate + ADP + H(+);
CC         Xref=Rhea:RHEA:52392, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58766, ChEBI:CHEBI:136591, ChEBI:CHEBI:456216;
CC         EC=2.7.1.220; Evidence={ECO:0000269|PubMed:27402745};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.081 mM for D-erythronate {ECO:0000269|PubMed:27402745};
CC         KM=3.2 mM for D-threonate {ECO:0000269|PubMed:27402745};
CC         KM=44 mM for 4-hydroxy-L-threonine {ECO:0000269|PubMed:27402745};
CC         Note=kcat is 16 sec(-1) with D-erythronate as substrate. kcat is 12
CC         sec(-1) with D-threonate as substrate. kcat is 41 sec(-1) with 4-
CC         hydroxy-L-threonine as substrate. {ECO:0000269|PubMed:27402745};
CC   -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000930; ABZ85202.1; -; Genomic_DNA.
DR   RefSeq; WP_012283687.1; NC_010337.2.
DR   AlphaFoldDB; B0TBI9; -.
DR   SMR; B0TBI9; -.
DR   STRING; 498761.HM1_2673; -.
DR   EnsemblBacteria; ABZ85202; ABZ85202; HM1_2673.
DR   KEGG; hmo:HM1_2673; -.
DR   eggNOG; COG3395; Bacteria.
DR   HOGENOM; CLU_029424_0_1_9; -.
DR   OMA; IASCVPW; -.
DR   OrthoDB; 771666at2; -.
DR   BioCyc; MetaCyc:MON-20186; -.
DR   BRENDA; 2.7.1.220; 12644.
DR   Proteomes; UP000008550; Chromosome.
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   Reference proteome; Transferase.
FT   CHAIN           1..439
FT                   /note="D-erythronate kinase"
FT                   /id="PRO_0000439673"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         366..369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT   BINDING         412
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ   SEQUENCE   439 AA;  46168 MW;  DC2ACE083190EA76 CRC64;
     MSNVVIIADD LTGANATGVL LARKGYKTAT FLQLPQDPLE NGNRFDVISI TTDSRAVAPE
     EAYRRVAEAA RAMLGNKPGL FTKRIDSTLR GNLGPEIDAM LDVLGPDSLA VVVAAFPTSG
     RITVGGYLLV HSIPLEQTDV ARDPKTPVHQ TLVADIVAAQ SKHSVGFIPL ATVLQGSTAV
     MEALGAQKEA GKRIVVMDAA TQKDLDTIAH GAYLSGLSVV AVDPGPFTEA LAAYVLPKPK
     QGRGKKVLMV VGSVTALTRQ QLKAVENAYS TCFTTVDVHA LIDPWRNAEE IERVSGEVLD
     HLDDHQVLGV RTVEEAGQVL DLASVALAYM ISEEEIASRI ADGLAAIARR VLQVSHGEVG
     GLYTSGGDVT VAVCQALAAS GVEVKDEVVP LAAYGRLIGG AFHQTPIITK GGLVGNSDAA
     CTCVDYLLTK ISNETYPAE