OTNK_HAEIN
ID OTNK_HAEIN Reviewed; 413 AA.
AC P44093;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=HI_1011;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
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:1YZY}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RA Patskovsky Y., Almo S.C.;
RT "Crystal structure of the Haemophilus influenzae hypothetical protein
RT HI1011.";
RL Submitted (FEB-2005) 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 -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22672.1; -; Genomic_DNA.
DR PIR; C64018; C64018.
DR RefSeq; NP_439172.1; NC_000907.1.
DR RefSeq; WP_005693348.1; NC_000907.1.
DR PDB; 1YZY; X-ray; 2.10 A; A/B=1-413.
DR PDBsum; 1YZY; -.
DR AlphaFoldDB; P44093; -.
DR SMR; P44093; -.
DR STRING; 71421.HI_1011; -.
DR PRIDE; P44093; -.
DR DNASU; 950004; -.
DR EnsemblBacteria; AAC22672; AAC22672; HI_1011.
DR KEGG; hin:HI_1011; -.
DR PATRIC; fig|71421.8.peg.1055; -.
DR eggNOG; COG3395; Bacteria.
DR HOGENOM; CLU_029424_1_0_6; -.
DR OMA; CSVMTNK; -.
DR PhylomeDB; P44093; -.
DR BioCyc; HINF71421:G1GJ1-1051-MON; -.
DR EvolutionaryTrace; P44093; -.
DR Proteomes; UP000000579; 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 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..413
FT /note="3-oxo-tetronate kinase"
FT /id="PRO_0000169314"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 354..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT BINDING 397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q0KBC8"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:1YZY"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:1YZY"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:1YZY"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:1YZY"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 324..345
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 380..389
FT /evidence="ECO:0007829|PDB:1YZY"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:1YZY"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:1YZY"
SQ SEQUENCE 413 AA; 44787 MW; 0639C8DA33D6A6D5 CRC64;
MLGVIADDFT GASDIASFLV ENGLSTVQMN GVPTQSLNSK VDAIVISLKS RSNPVNEAIE
QSLRAYQWLK ENGCTQFYFK YCSTFDSTAK GNIGPVTDAL LDELNEDFTV ITPALPVNGR
TIFNGYLFVG DVLLSESGMK NHPITPMVDA NLMRLMDAQA KGKTGLVAYA DVIKGASRVQ
ECFAELKAQG YRYAVVDAVD NSQLEVLAEA VADFKLVTGG SGLGAYMAAR LSGGKKGTNA
FTPTKGKTVV LSGSCSVMTN KQVEKYREKA PHFQLDVEQA IHNENYIEQL YQWVIANLDS
EFAPMVYATV PPDALKAIQH QFGVDQASHA IENTFAKLAA KLKQYGVTNF ITAGGETSSI
VVQELGFTGF HIGKQIAPGV PWLKAVEEDI FLALKSGNFG KEDFFEYAQG MFL
