ID A0A1B8UMB4_9BACL Unreviewed; 291 AA.
AC A0A1B8UMB4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=BBG47_21405 {ECO:0000313|EMBL:OBY77492.1};
OS Paenibacillus sp. KS1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY77492.1, ECO:0000313|Proteomes:UP000092663};
RN [1] {ECO:0000313|EMBL:OBY77492.1, ECO:0000313|Proteomes:UP000092663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|EMBL:OBY77492.1,
RC ECO:0000313|Proteomes:UP000092663};
RA Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT Florida, USA.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBY77492.1}.
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DR EMBL; MAIS01000078; OBY77492.1; -; Genomic_DNA.
DR RefSeq; WP_065293413.1; NZ_MAIS01000078.1.
DR AlphaFoldDB; A0A1B8UMB4; -.
DR OrthoDB; 9783435at2; -.
DR Proteomes; UP000092663; Unassembled WGS sequence.
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:OBY77492.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092663};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 291 AA; 31253 MW; DD181820EAD54941 CRC64;
MKLLGAIEGG GTKFVVAVGT EDGQIQQIES FPTTTPEETM DRTVAFFKDK GISSIGFGSF
GPVDLNSNSP TYGHIAKTPK PHWSGYDVVG HLKRHLNVPV GFDTDVNGAA LGEATFGAAK
GLNSCLYITV GTGIGAGAVV EGKLVHGLLH PEMGHIMVKR HPEDTYEGKC PYHKDCLEGL
AAGPAIEARW GVKAYELGED HKAWELQTFY LAQALMNYIL TISPEKIILG GGVSKQLHLF
PRIREQVKTL LNGYVQHPAI LEVNEDYIVP PALQDRAGIT GALALAVQAL K
//
