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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta (PFP) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-PFK) (Pyrophosphate-dependent 6-phosphofructose-1-kinase)

 V7CAP6_PHAVU            Unreviewed;       568 AA.
V7CAP6;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
27-SEP-2017, entry version 23.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_03185};
Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185};
EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_03185};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185};
AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185};
Name=PFP-BETA {ECO:0000256|HAMAP-Rule:MF_03185};
ORFNames=PHAVU_003G082000g {ECO:0000313|EMBL:ESW25986.1};
Phaseolus vulgaris (Kidney bean) (French bean).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW25986.1, ECO:0000313|Proteomes:UP000000226};
[1] {ECO:0000313|EMBL:ESW25986.1, ECO:0000313|Proteomes:UP000000226}
NUCLEOTIDE SEQUENCE.
Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalytic subunit of pyrophosphate--fructose 6-phosphate
1-phosphotransferase. Catalyzes the phosphorylation of D-fructose
6-phosphate, the first committing step of glycolysis. Uses
inorganic phosphate (PPi) as phosphoryl donor instead of ATP like
common ATP-dependent phosphofructokinases (ATP-PFKs), which
renders the reaction reversible, and can thus function both in
glycolysis and gluconeogenesis. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_03185}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03185};
-!- ENZYME REGULATION: Allosterically activated by fructose 2,6-
bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta
(catalytic) chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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EMBL; CM002290; ESW25986.1; -; Genomic_DNA.
RefSeq; XP_007153992.1; XM_007153930.1.
GeneID; 18634267; -.
KEGG; pvu:PHAVU_003G082000g; -.
KO; K00895; -.
PhylomeDB; V7CAP6; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000226; Chromosome 3.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR011183; PfpB_PPi_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
TIGRFAMs; TIGR02477; PFKA_PPi; 1.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185};
Complete proteome {ECO:0000313|Proteomes:UP000000226};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
Kinase {ECO:0000256|HAMAP-Rule:MF_03185};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03185};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Reference proteome {ECO:0000313|Proteomes:UP000000226};
Transferase {ECO:0000256|HAMAP-Rule:MF_03185}.
DOMAIN 98 463 PFK. {ECO:0000259|Pfam:PF00365}.
REGION 228 230 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 267 268 Substrate binding; shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 275 277 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 441 444 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
ACT_SITE 230 230 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03185}.
METAL 200 200 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03185}.
BINDING 106 106 Diphosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03185}.
BINDING 336 336 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03185}.
SITE 201 201 Important for catalytic activity and
substrate specificity; stabilizes the
transition state when the phosphoryl
donor is PPi; prevents ATP from binding
by mimicking the alpha-phosphate group of
ATP. {ECO:0000256|HAMAP-Rule:MF_03185}.
SITE 227 227 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000256|HAMAP-Rule:MF_03185}.
SEQUENCE 568 AA; 62223 MW; 39DA102562A57A1E CRC64;
MAPSFAINGG FPGTRVTPPS DTGRFAAVYS EVQNSRIDHA LPLPSVLKNP FVIVDGHQST
AAGNPDEIAK LFPNLFGQPS ASLVPSDSHA LHANPKLKIG VVLSGGQAPG GHNVISGIFD
YLQDKAEGST LYGFRGGPAG IMKSKYVELT SDYIYPYRNQ GGFDMIRSGR DKIETPEQFR
QAEETVQKLD LDGLVVIGGD DSNTNACLLA EYFRSKNIKT RVIGCPKTID GDLKCKEVPT
SFGFDTACKI YAEMIGNVMI DARSTGKYYH FVRLMGRAAS HITLECALQT HPNITIIGEE
VATKKMTLKD VTDYIVDIIS KRAEDNYNYG VILIPEGLID FIPEVQHLIA ELNEILAHDT
VDEGGLWKKK LTDQSLNLFE LLPKAIQEQL MLERDPHGNV QVAKIETEKM LIQMVETELE
KRKQQGTYKG GFRGQSHFFG YEGRCGLPTN FDSSYCYALG YGAAALLQSG KTGLISSVAN
LCAPVEEWTV GGTALTSLMD VERRHGKFKP VIKKAMVELE GAPFQKFASL RDEWALKNRY
ISPGPIQFTG PGSDAISQTL LLELDAQA


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