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Database: UniProt
Entry: A0A095B0E4_9SPHN
LinkDB: A0A095B0E4_9SPHN
Original site: A0A095B0E4_9SPHN 
ID   A0A095B0E4_9SPHN        Unreviewed;       339 AA.
AC   A0A095B0E4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE            EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN   ORFNames=FG95_02637 {ECO:0000313|EMBL:KGB55169.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB55169.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB55169.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB55169.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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:KGB55169.1}.
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DR   EMBL; JNFC01000034; KGB55169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095B0E4; -.
DR   STRING; 1120705.FG95_02637; -.
DR   PATRIC; fig|1120705.3.peg.2658; -.
DR   eggNOG; COG1940; Bacteria.
DR   Proteomes; UP000029625; 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; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGB55169.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   339 AA;  34707 MW;  DF7ECE8FBD417137 CRC64;
     MSREISPDPA TFGLALQRGA RHKPERSGEG VALMDGPVAD RGEVRLFAGI ELGGTKCICT
     LAAGPGEIRD QRTIATTVPS ETLPAILAVL DGWARAPGFC SIGVASFGPI RVDPVKADYG
     RVGATNKPDW EGADLLGPLK SAFPVPIGFD TDVNGAALAE IRWGSGRGLD DFAYVTVGTG
     VGVGLVVHGK PTRGFSHSEI GHILVPRLAG DEVPSVCRFH DDCVEGLASG TALKARLGGR
     SLADVAADDP VWEPIVHTLA SMVHSLACTT GPMRVAMGGG VLAGQPQLLP RINARLEASL
     AGYMQIPGGG AYVIAPELGT MAGPLGAIAL AMDAVGVAA
//
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