ID A0A172ZEV6_9BACL Unreviewed; 299 AA.
AC A0A172ZEV6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=AR543_09320 {ECO:0000313|EMBL:ANF96176.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF96176.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF96176.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF96176.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036647};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family.
CC {ECO:0000256|ARBA:ARBA00006479}.
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DR EMBL; CP013023; ANF96176.1; -; Genomic_DNA.
DR RefSeq; WP_060533798.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZEV6; -.
DR STRING; 1616788.AR543_09320; -.
DR KEGG; pbv:AR543_09320; -.
DR OrthoDB; 9783435at2; -.
DR Proteomes; UP000078148; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR42742:SF5; FRUCTOKINASE-RELATED; 1.
DR PANTHER; PTHR42742; TRANSCRIPTIONAL REPRESSOR MPRA; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01125; ROK; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ANF96176.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078148};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 299 AA; 32045 MW; 447D2CF0DCF4E070 CRC64;
MKKLGAIEAG GTKFVCGIGT EDGQILERAS FPTETPEITM KNVVSFFEGK GIEALGVGSF
GPIDPIPGSP TYGYITTTPK PHWGQYNIIG HLKQHFDVPM SFDTDVNGAA LGEYTWGAAK
GLDSCLYITV GTGIGAGAVV DGKMLHGLSH PEMGHILVRR HLDDTFEGFC PYHGDCLEGM
AAGPALEKRW QVKGSELTPD HPAWEMEAYY LAQALMSYVL ILSPQKIIMG GGVMKQEQLF
PLIREKLQQL LNGYVQHPSL QENLDQYIVS PGLGDNAGLS GAIALAKLAL EGEAGADVV
//
