ID A0A0Q8XND7_9SPHN Unreviewed; 297 AA.
AC A0A0Q8XND7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=ASE13_13915 {ECO:0000313|EMBL:KRC80113.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC80113.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC80113.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80113.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC80113.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80113.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRC80113.1}.
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DR EMBL; LMIV01000002; KRC80113.1; -; Genomic_DNA.
DR RefSeq; WP_056616907.1; NZ_LMIV01000002.1.
DR AlphaFoldDB; A0A0Q8XND7; -.
DR STRING; 1736501.ASE13_13915; -.
DR OrthoDB; 9783435at2; -.
DR Proteomes; UP000051629; 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:SF3; MANNOSE-6-PHOSPHATE ISOMERASE GMUF-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 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KRC80113.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:KRC80113.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 297 AA; 30094 MW; 103743E8890B52D7 CRC64;
MASTVSLIAG IELGGTKCIA LLGTGPGDVR AQQVIPTTDP ATTLAAIEAV LDDWAFDAIG
VASFGPLQLG TGAPDYGAIT ATTKPGWSGT DLVRRLEARY GKPIGFQTDV NGAALAEGRW
GAARGMVTHA YLTIGTGVGV GLVAGGRPVQ GVAHGEAGHM RVPRAAGDTY AGWCRFHGDC
VEGLISGPAL AERFGCPGKE LPHDGPEWDL FVHDLSGLLH NLVTVAAPER IAIGGGVIAA
REHLFLRLRA RLAESLGGYG SLAGYAAELD ERLGPPGLGP MAGPLGALAV GLGAVGA
//
