OTNK_ACTSZ
ID OTNK_ACTSZ Reviewed; 414 AA.
AC A6VKK5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=Asuc_0122 {ECO:0000312|EMBL:ABR73502.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
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 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 -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000746; ABR73502.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VKK5; -.
DR SMR; A6VKK5; -.
DR STRING; 339671.Asuc_0122; -.
DR EnsemblBacteria; ABR73502; ABR73502; Asuc_0122.
DR KEGG; asu:Asuc_0122; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_6; -.
DR OMA; CSVMTNK; -.
DR Proteomes; UP000001114; 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..414
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000439678"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 355..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ SEQUENCE 414 AA; 44417 MW; B75C850CEFD0AC65 CRC64;
MMLGVIADDF TGASDIASFL VENGLSAVQM NGVPKQPLNS RVDAIVISLK SRSNPANEAV
EQSLNAYNWL QENGCTQFYF KYCSTFDSTA KGNIGPVTDA LLEALNEDFT VITPALPVNG
RTIFNGYLFV GEQLLSESGM KNHPITPMTD ANLMRLMDAQ AKGKTGLVAY ADVIQGAARV
KERFAELKAQ GYRYAVVDAA DNSQLEVLAE AVAGLKLVTG GSGLGAYIAA RLSGGKKGTN
AFTPTKGKTV VLSGSCSVMT NKQVEKYCEK APHFQLDAAQ AINNPNYAEE LYQWVTANLD
APLAPMVYAT VPPEALKAIQ NEFGADKASH AIENTFAQLA AKLKRYGVTN FINAGGETSS
IVVQQLGFSG FHIGKQIAPG VPWLKAVEED IYLALKSGNF GKEDFFEYAQ GMFV
