OTNK_BRUME
ID OTNK_BRUME Reviewed; 436 AA.
AC Q8YB10;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BMEII1091 {ECO:0000312|EMBL:AAL54333.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
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}.
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DR EMBL; AE008918; AAL54333.1; -; Genomic_DNA.
DR PIR; AB3646; AB3646.
DR AlphaFoldDB; Q8YB10; -.
DR SMR; Q8YB10; -.
DR STRING; 224914.BMEII1091; -.
DR EnsemblBacteria; AAL54333; AAL54333; BMEII1091.
DR KEGG; bme:BMEII1091; -.
DR eggNOG; COG3395; Bacteria.
DR OMA; TIYCPAF; -.
DR Proteomes; UP000000419; Chromosome II.
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..436
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000439679"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 372..375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
SQ SEQUENCE 436 AA; 45926 MW; AE329C1B8408BD7B CRC64;
MPASNFPTGV HDMRLGVIAD DFTGATDIAG FLVGNGLRTI QLNGVPADDL AVDADAVVIS
LKARSCPTGQ AIAESLAALK WLQKNNCQQF FFKYCSTFDS TPKGNIGPVT DALLEALGEE
FTVICPALPV NGRTIYNGYL FVNGVLLSET GMRNHPVTPM TDSNIMRVME SQSRGRAGNI
SSTIVDQGSD AVRDALRKLQ SEGIRYAVLD ALNDQHIETL GRAVSQMKLV TGGSGLADGM
ARAWTQLRGK NVAAAEAAGA PVKGRTVILS GSCSQMTNAQ VAAYKAKAPA LAMDVEKAIN
DAAYIDVLAE WVLAQSGDAL PPLVYATMPP EALKAVQERF GGERASAAIE DLFGQLAKRL
EAEGFTRFIV AGGETSGAVT QALAIDGFTI GPQIAPGVPW VRGIGKPLSL ALKSGNFGTE
AFFFEAQKIA NQEGDK
