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Database: UniProt
Entry: A0A0R1RHC0_9LACO
LinkDB: A0A0R1RHC0_9LACO
Original site: A0A0R1RHC0_9LACO 
ID   A0A0R1RHC0_9LACO        Unreviewed;       290 AA.
AC   A0A0R1RHC0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE            EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN   ORFNames=FD35_GL001484 {ECO:0000313|EMBL:KRL53051.1};
OS   Furfurilactobacillus rossiae DSM 15814.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Furfurilactobacillus.
OX   NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL53051.1, ECO:0000313|Proteomes:UP000051999};
RN   [1] {ECO:0000313|EMBL:KRL53051.1, ECO:0000313|Proteomes:UP000051999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL53051.1,
RC   ECO:0000313|Proteomes:UP000051999};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL53051.1}.
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DR   EMBL; AZFF01000026; KRL53051.1; -; Genomic_DNA.
DR   RefSeq; WP_017261008.1; NZ_AZFF01000026.1.
DR   AlphaFoldDB; A0A0R1RHC0; -.
DR   STRING; 1114972.FD35_GL001484; -.
DR   PATRIC; fig|1114972.6.peg.1507; -.
DR   eggNOG; COG1940; Bacteria.
DR   OrthoDB; 9783435at2; -.
DR   Proteomes; UP000051999; 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:0008483; F:transaminase activity; 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.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KRL53051.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRL53051.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051999};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRL53051.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   290 AA;  31862 MW;  FA555CC8E249107B CRC64;
     MLLGSVEAGG TKFVCAVGDE NYRTKDIVSF PTTTPAETLQ KTIDYFRQFD IKALSVASFG
     PIELRRNDPK YGYITNTPKP NWADTDFIGT LKEAFDIPMF WTTDVNGSAY GEYVMSTLTN
     ERINSLVYYT IGTGVGAGAI IDGDFLGEMG HPEMGHVRLK RHPDDLDFNG ICPFHGDCLE
     GLVAGPTFEA RTGKPGKEVP LTDHVWDIMA YYVAQAALQV TLIMRPGKII FGGGVVSEPF
     LKKVRQQFSE LLNDYVNVGN LDDYIAMPAI KHNGSATLGN FALALRELQA
//
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