K1PF_HALVD
ID K1PF_HALVD Reviewed; 305 AA.
AC D4GYE6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=1-phosphofructokinase {ECO:0000305};
DE EC=2.7.1.56 {ECO:0000269|PubMed:22493022};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000303|PubMed:22493022};
DE Short=Fru1PK {ECO:0000250|UniProtKB:P0AEW9};
GN Name=pfkB; OrderedLocusNames=HVO_1500; ORFNames=C498_11231;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP INDUCTION, DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DS2 / DS70;
RX PubMed=22493022; DOI=10.1128/jb.00200-12;
RA Pickl A., Johnsen U., Schoenheit P.;
RT "Fructose degradation in the haloarchaeon Haloferax volcanii involves a
RT bacterial type phosphoenolpyruvate-dependent phosphotransferase system,
RT fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate
RT aldolase.";
RL J. Bacteriol. 194:3088-3097(2012).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate. Involved in the utilization of
CC fructose as a sole carbon and energy source.
CC {ECO:0000269|PubMed:22493022}.
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:0000269|PubMed:22493022};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for fructose-1-phosphate {ECO:0000269|PubMed:22493022};
CC KM=1.12 mM for fructose-6-phosphate {ECO:0000269|PubMed:22493022};
CC KM=0.08 mM for ATP {ECO:0000269|PubMed:22493022};
CC Vmax=308 umol/min/mg enzyme toward fructose-1-phosphate
CC {ECO:0000269|PubMed:22493022};
CC Vmax=30.7 umol/min/mg enzyme toward fructose-6-phosphate
CC {ECO:0000269|PubMed:22493022};
CC Vmax=200 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:22493022};
CC pH dependence:
CC Optimum pH is between 7.5 and 9. {ECO:0000269|PubMed:22493022};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22493022}.
CC -!- INDUCTION: Expression is highly up-regulated in presence of fructose.
CC {ECO:0000269|PubMed:22493022}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth on fructose. Growth on glucose is
CC not affected. {ECO:0000269|PubMed:22493022}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE02968.1; -; Genomic_DNA.
DR EMBL; AOHU01000090; ELY28262.1; -; Genomic_DNA.
DR RefSeq; WP_004043435.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; D4GYE6; -.
DR SMR; D4GYE6; -.
DR STRING; 309800.C498_11231; -.
DR EnsemblBacteria; ADE02968; ADE02968; HVO_1500.
DR EnsemblBacteria; ELY28262; ELY28262; C498_11231.
DR GeneID; 8926637; -.
DR KEGG; hvo:HVO_1500; -.
DR PATRIC; fig|309800.29.peg.2140; -.
DR eggNOG; arCOG00015; Archaea.
DR HOGENOM; CLU_050013_0_0_2; -.
DR OMA; GETRSNI; -.
DR OrthoDB; 55800at2157; -.
DR BRENDA; 2.7.1.56; 2561.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
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 Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR03168; 1-PFK; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..305
FT /note="1-phosphofructokinase"
FT /id="PRO_0000428980"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 214..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 245..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ SEQUENCE 305 AA; 32003 MW; E5E079577C3988F5 CRC64;
MILTVTPNPA VDHTIHFDEP LQTGVVHRTD DAVFTAGGKG INVAKYASAL DADVTASGFL
GGHFGKFVRD RLDADGIASD FVTVDADTRL NTTVLAADGE YKLNHNGPQI RAADVDELVE
TAQANEPDTL LVGGSLPPGM SLSDVDRLAR AGDWKIAVDM GGEYLAELDA DYYVCKPNRS
ELAAATGRTV ETEADAVEAA EELHARGFEY VLASLGADGA LLVTDDEVLS APALDVEVVD
TVGAGDAVMS GFLAAREHGL SDADALRMGV LTASRVVGVA GTRVPDLEDV LTNETHVEVT
TVRTR
