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Database: UniProt
Entry: A0A0R1VRY8_9LACO
LinkDB: A0A0R1VRY8_9LACO
Original site: A0A0R1VRY8_9LACO 
ID   A0A0R1VRY8_9LACO        Unreviewed;       290 AA.
AC   A0A0R1VRY8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=fructokinase {ECO:0000256|ARBA:ARBA00038887};
DE            EC=2.7.1.4 {ECO:0000256|ARBA:ARBA00038887};
GN   ORFNames=FC89_GL001313 {ECO:0000313|EMBL:KRM05609.1};
OS   Liquorilactobacillus ghanensis DSM 18630.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM05609.1, ECO:0000313|Proteomes:UP000051451};
RN   [1] {ECO:0000313|EMBL:KRM05609.1, ECO:0000313|Proteomes:UP000051451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM05609.1,
RC   ECO:0000313|Proteomes:UP000051451};
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:KRM05609.1}.
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DR   EMBL; AZGB01000018; KRM05609.1; -; Genomic_DNA.
DR   RefSeq; WP_057872053.1; NZ_AZGB01000018.1.
DR   AlphaFoldDB; A0A0R1VRY8; -.
DR   STRING; 1423750.FC89_GL001313; -.
DR   PATRIC; fig|1423750.3.peg.1346; -.
DR   OrthoDB; 9783435at2; -.
DR   Proteomes; UP000051451; 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:KRM05609.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRM05609.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051451};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRM05609.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   290 AA;  31676 MW;  407AE3AC7135CF94 CRC64;
     MLLGSIEAGG TKFICAVGNE DYRIKDKVQI PTTTPEETLT AVVDYFKQFK LDALGIASFG
     PIEIRKTSPK YGYITTTPKK GWANTDFLGF IKKSINVPIS WTTDVNGSAF GEYTMSTLFN
     EKIESLVYYT IGTGVGAGAV IDGHLVGSAG HPEMGHVLLK RHPDDLNFKG ICPYHHDCLE
     GLVAGPTFEA RTGKKGQDVP LTDKTWDILA YYIAQAAIQV TLILRPNKIV FGGGVTNKVL
     LEKVRSEFKN ILNDYVKVPP LDQYITMPQV ANNGSANIGN FALAENLLLK
//
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