PFP_XANCB
ID PFP_XANCB Reviewed; 418 AA.
AC B0RP51;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01978};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01978};
DE Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01978};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01978};
GN Name=pfp {ECO:0000255|HAMAP-Rule:MF_01978};
GN OrderedLocusNames=xcc-b100_0891;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=B100;
RX PubMed=24508689; DOI=10.1016/j.abb.2014.01.023;
RA Frese M., Schatschneider S., Voss J., Vorholter F.J., Niehaus K.;
RT "Characterization of the pyrophosphate-dependent 6-phosphofructokinase from
RT Xanthomonas campestris pv. campestris.";
RL Arch. Biochem. Biophys. 546:53-63(2014).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the
CC first committing step of glycolysis. Uses inorganic phosphate (PPi) as
CC phosphoryl donor instead of ATP like common ATP-dependent
CC phosphofructokinases (ATP-PFKs), which renders the reaction reversible,
CC and can thus function both in glycolysis and gluconeogenesis.
CC Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-
CC PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
CC {ECO:0000255|HAMAP-Rule:MF_01978, ECO:0000269|PubMed:24508689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:24508689};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01978};
CC -!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000255|HAMAP-Rule:MF_01978,
CC ECO:0000269|PubMed:24508689}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for phosphate {ECO:0000269|PubMed:24508689};
CC KM=41 uM for diphosphate {ECO:0000269|PubMed:24508689};
CC KM=202 uM for fructose 6-phosphate {ECO:0000269|PubMed:24508689};
CC KM=24 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:24508689};
CC Vmax=58 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:24508689};
CC Vmax=59 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:24508689};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:24508689};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:24508689};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01978}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01978}.
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DR EMBL; AM920689; CAP50236.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RP51; -.
DR SMR; B0RP51; -.
DR KEGG; xca:xcc-b100_0891; -.
DR HOGENOM; CLU_020655_1_1_6; -.
DR OMA; AHDIGYF; -.
DR BRENDA; 2.7.1.90; 9230.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001188; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01978; Phosphofructokinase_II_B2; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR011404; PPi-PFK_XF0274.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF036483; PFK_XF0274; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..418
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase"
FT /id="PRO_0000429699"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 13
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT BINDING 295..298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT SITE 112
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
FT SITE 138
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01978"
SQ SEQUENCE 418 AA; 44647 MW; 77F8CFCB3D61231D CRC64;
MTNGNLLYAQ SGGVTAVINA TAAGVIGEAR ARKIKVLAAR NGILGALREE LIDTSKESAA
AIAALAQTPG GAFGSCRYKL KSLEQDRAKY ERLLEVLRAH DVRWFLYNGG NDSADTALKV
SQLAKAFGYP LHCIGVPKTI DNDLAVTDTC PGFGSAAKYT AVSVREAALD VAAMADTSTK
VFIYEAMGRH AGWLAAAAGL AGQGPDDAPQ IILLPERAFD QAAFLAKVRQ MVERVGWCVV
VASEGIQDAQ GKFVADAGGA TDSFGHAQLG GVASFLAAQV KQELGYKVHW TLPDYLQRSA
RHLASKTDWE QAQAVGKAAV QYALKGMNAV IPVIERVSDA PYRWKIVPAP LHKVANHEKK
MPPSFLRKDG FGITERARRY FAPLIKGEAP LAYGSDGLPK YVSLKNVAVA KKLPAWEG
