ID K2GFB7_9BACI Unreviewed; 291 AA.
AC K2GFB7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN ORFNames=MJ3_00265 {ECO:0000313|EMBL:EKE32887.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32887.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE32887.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE32887.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(2012).
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:EKE32887.1}.
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DR EMBL; AMPQ01000001; EKE32887.1; -; Genomic_DNA.
DR RefSeq; WP_008586941.1; NZ_JAFBFF010000001.1.
DR AlphaFoldDB; K2GFB7; -.
DR STRING; 1230341.AAV35_003055; -.
DR KEGG; sje:AAV35_003055; -.
DR PATRIC; fig|1230341.3.peg.61; -.
DR eggNOG; COG1940; Bacteria.
DR OrthoDB; 9783435at2; -.
DR Proteomes; UP000011746; 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:EKE32887.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 291 AA; 31881 MW; 432B33966D291912 CRC64;
MNLGAIEAGG TKFVLAVGNE EGEILEKKVI PTEHPSITMP AVIDFFRGKD IERLGVGSFG
PIDVNADSAF YGQLQKTPKT EWVDYPLGKE LQDHLLIPVI IDTDVNVAAM SEAKWGDAKD
VDSCLYITVG TGIGAGAYIK GETLRGLSHP EMGHIPVRRH SDDDYAGGCP YHGDCLEGMA
AGPHIEKRWG RPAEELVDRK EVWEMEAYYL AQALVNYIYI VSPERIILGG GVMKQKQLFP
MIRTMVLELL NGYVSSPYLT EDTIDKYIVS PGLTDEAGVK GALYLAMGSR M
//
