ID A0A0T0PWC2_9SPHN Unreviewed; 305 AA.
AC A0A0T0PWC2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=ASG29_04700 {ECO:0000313|EMBL:KQT33363.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT33363.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT33363.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33363.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT33363.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33363.1,
RC ECO:0000313|Proteomes:UP000051178};
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 -!- 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:KQT33363.1}.
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DR EMBL; LMQP01000002; KQT33363.1; -; Genomic_DNA.
DR RefSeq; WP_055981028.1; NZ_LMQP01000002.1.
DR AlphaFoldDB; A0A0T0PWC2; -.
DR STRING; 1736370.ASG29_04700; -.
DR OrthoDB; 9783435at2; -.
DR Proteomes; UP000051178; 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:KQT33363.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 305 AA; 31116 MW; DB71830C6D169E03 CRC64;
MGEAPLVAGV ELGGTKCIAI LASGPDRVLE EVRIPTTTPA ETLPALEAAL DQWRGFAAIG
IASFGPVSID RASVRYGSIT STPKPHWADT DIARRLEARY GVPTGFHSDV VGAALAEARW
GAGRGLSDLA YVTVGTGVGA GLVAHGQPVD GLSHAELGHI RPPRLRGDDW GGICPFHGDC
VEGLAAGPAI AARTGTKGED LTADHPAWDT VVDALAHLFG TLALTGVPRR IVLGGGVLVG
NDFLLPRLRR ATAASLGGYV ALPEVEDMDT FLVPAALGGR AGPLGAIVLG GNALDAARAG
AFTRA
//
