ID A0A0Q7R7Z3_9CAUL Unreviewed; 309 AA.
AC A0A0Q7R7Z3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=ASD25_14555 {ECO:0000313|EMBL:KQY66759.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY66759.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY66759.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY66759.1,
RC ECO:0000313|Proteomes:UP000051815};
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:KQY66759.1}.
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DR EMBL; LMFL01000067; KQY66759.1; -; Genomic_DNA.
DR RefSeq; WP_055831420.1; NZ_LMFL01000067.1.
DR AlphaFoldDB; A0A0Q7R7Z3; -.
DR Proteomes; UP000051815; 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 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; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQY66759.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 309 AA; 31370 MW; BE4A4607BAAF90C2 CRC64;
MSDRGPLLAG VELGGTKCVC LLASGPDDVR EEVRIDTSAP AETLAAIHGV LSRWQDREGF
AAIGVASFGP LELDIGAAGY GCIVNTSKAG WSGADVLALL RGFGAPTGFD TDVNGAALAE
GRWGGARGLD SYAYITVGTG IGVGSVVRGL TLRGLGHSEA GHLRIPRMPG ETWAGVCPFH
GDCVEGLASG PAIQMKAGGP GHGLGPSSPV WNEVVHALAA LLHNLVLTTA PQRILIGGGV
VGGHPFLLPR LREALIHSLN GYGAAPGIVE VIREFVVAPA LADRAGPLGA IALAEDALAD
QVARQGRAT
//
