ID Q9RZP6_DEIRA Unreviewed; 315 AA.
AC Q9RZP6;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 138.
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=DR_B0074 {ECO:0000313|EMBL:AAF12596.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OG Plasmid megaplasmid MP1 {ECO:0000313|Proteomes:UP000002524}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12596.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF12596.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE001826; AAF12596.1; -; Genomic_DNA.
DR PIR; C75626; C75626.
DR RefSeq; NP_051610.1; NC_000958.1.
DR RefSeq; WP_010884013.1; NZ_JMLF01000022.1.
DR AlphaFoldDB; Q9RZP6; -.
DR EnsemblBacteria; AAF12596; AAF12596; DR_B0074.
DR GeneID; 69519324; -.
DR KEGG; dra:DR_B0074; -.
DR PATRIC; fig|243230.17.peg.72; -.
DR HOGENOM; CLU_050013_0_1_0; -.
DR InParanoid; Q9RZP6; -.
DR OrthoDB; 9801219at2; -.
DR Proteomes; UP000002524; Plasmid megaplasmid MP1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
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; PS00583; PFKB_KINASES_1; 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}; Plasmid {ECO:0000313|EMBL:AAF12596.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT DOMAIN 19..298
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 315 AA; 32521 MW; FE48D9535E74E5AA CRC64;
MGTPRVLTLT LNPALDLTVR ADGWRPNTVN SGQTLHLTAG GKGVNVASFL ADWGLPVTAS
GLLGEDNAEV FDALFRTKAI TDAFVRVPGQ TRVGVKIVDH AAQQTTDINL PGLRATPEHL
RELHAQLDAL CESHDAFVLA GSLPPGIAPD FYTELVAKLR GAGKFVALDT SGAALTAALT
ANVLPHLVKP NTHELSAALG RELGTQAELL AAARDLLGRG AELVAISQGE DGALLVTPGA
TVQAKPPHVQ VVSTVGAGDA MVAGLVSAHL DSLPLPDAAR RATSFSVSTI TRLGAHLPAR
DELAGYAAQV TVTPL
//
