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Database: UniProt
Entry: H8GTA6_DEIGI
LinkDB: H8GTA6_DEIGI
Original site: H8GTA6_DEIGI 
ID   H8GTA6_DEIGI            Unreviewed;       315 AA.
AC   H8GTA6;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=1-phosphofructokinase {ECO:0000256|ARBA:ARBA00013596, ECO:0000256|RuleBase:RU369061};
DE            Short=Fru1PK {ECO:0000256|RuleBase:RU369061};
DE            EC=2.7.1.56 {ECO:0000256|ARBA:ARBA00012131, ECO:0000256|RuleBase:RU369061};
DE   AltName: Full=Fructose 1-phosphate kinase {ECO:0000256|ARBA:ARBA00032802, ECO:0000256|RuleBase:RU369061};
GN   OrderedLocusNames=DGo_CA2631 {ECO:0000313|EMBL:AFD26558.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26558.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD26558.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA   Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT   Deinococcus gobiensis: insights into the extreme environmental
RT   adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC       phosphate to fructose-l,6-bisphosphate.
CC       {ECO:0000256|RuleBase:RU369061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881,
CC         ChEBI:CHEBI:456216; EC=2.7.1.56;
CC         Evidence={ECO:0000256|ARBA:ARBA00000823,
CC         ECO:0000256|RuleBase:RU369061};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|RuleBase:RU369061}.
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DR   EMBL; CP002191; AFD26558.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8GTA6; -.
DR   STRING; 745776.DGo_CA2631; -.
DR   KEGG; dgo:DGo_CA2631; -.
DR   PATRIC; fig|745776.4.peg.2697; -.
DR   eggNOG; COG1105; Bacteria.
DR   HOGENOM; CLU_050013_0_1_0; -.
DR   Proteomes; UP000007575; Chromosome.
DR   GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01164; FruK_PfkB_like; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR022463; 1-PFruKinase.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR   NCBIfam; TIGR03168; 1-PFK; 1.
DR   NCBIfam; TIGR03828; pfkB; 1.
DR   PANTHER; PTHR46566:SF5; 1-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR46566; 1-PHOSPHOFRUCTOKINASE-RELATED; 1.
DR   Pfam; PF00294; PfkB; 1.
DR   PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU369061};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU369061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU369061};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT   DOMAIN          14..297
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   315 AA;  31659 MW;  570D675EAB3BA6ED CRC64;
     MTLTLNPALD MTVRVDGLRL GEVNGGQSLQ TDAGGKGVNV ASFLADWGRD EPGGLDVTAT
     GLLGADNAAP FEALLRGKGI TDAFVRVPGA TRVGVKLSDH AAQETTDINL PGLSAAPEAL
     AEVRARLREL ATGGGVFVLA GSLPPGVPAD LYAELVAELR AAGTYVALDT SGAALTSVLG
     AGVLPQLVKP NIHELEAALG RSLTGEAEVL AAARELLSRG AEVVAVSQGE QGALIVTAAG
     TVRALPPRVQ VVSTVGAGDA MVAGLVASHL AGLSLPDAAR RATSFSVGNI TRLGAHLPPR
     AELDGYAAQV QVSAV
//
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