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Multifunctional fusion protein [Includes: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase); Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent) (PPi-dependent phosphofructokinase) (Pyrophosphate-dependent 6-phosphofructose-1-kinase) (PPi-PFK)]

 A0A1F7RHM3_9BACT        Unreviewed;       346 AA.
A0A1F7RHM3;
15-FEB-2017, integrated into UniProtKB/TrEMBL.
15-FEB-2017, sequence version 1.
10-OCT-2018, entry version 16.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|HAMAP-Rule:MF_01976};
Includes:
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01976};
EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01976};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01976};
AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01976};
Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01976};
Includes:
RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339};
Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339};
AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339};
Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339};
Synonyms=pfp {ECO:0000256|HAMAP-Rule:MF_01976};
ORFNames=A2042_09850 {ECO:0000313|EMBL:OGL41033.1};
Candidatus Schekmanbacteria bacterium GWA2_38_11.
Bacteria; Candidatus Schekmanbacteria.
NCBI_TaxID=1817876 {ECO:0000313|EMBL:OGL41033.1};
[1] {ECO:0000313|EMBL:OGL41033.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=27774985; DOI=10.1038/ncomms13219;
Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
"Thousands of microbial genomes shed light on interconnected
biogeochemical processes in an aquifer system.";
Nat. Commun. 7:13219-13219(2016).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis. {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00643164}.
-!- FUNCTION: 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. Consistently, PPi-PFK can replace the enzymes of
both the forward (ATP-PFK) and reverse (fructose-bisphosphatase
(FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01976}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00643168}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_01976}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640094};
-!- ACTIVITY REGULATION: Allosterically activated by ADP and other
diphosphonucleosides, and allosterically inhibited by
phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS01071267}.
-!- ACTIVITY REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
Rule:MF_01976}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00640117}.
-!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
Rule:MF_01976}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00634688}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640112}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. Mixed-substrate PFK group III subfamily.
{ECO:0000256|HAMAP-Rule:MF_01976}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OGL41033.1}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; MGDB01000080; OGL41033.1; -; Genomic_DNA.
UniPathway; UPA00109; UER00182.
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:UniProtKB-KW.
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_00339; Phosphofructokinase_I_B1; 1.
HAMAP; MF_01976; Phosphofructokinase_III; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR012003; ATP_PFK_prok-type.
InterPro; IPR012828; PFKA_ATP_prok.
InterPro; IPR015912; Phosphofructokinase_CS.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR012829; Phosphofructokinase_III.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF000532; ATP_PFK_prok; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
TIGRFAMs; TIGR02483; PFK_mixed; 1.
PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00339};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00643171};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640104};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640111};
Kinase {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640102};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640121};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640110};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00643171};
Transferase {ECO:0000256|HAMAP-Rule:MF_00339,
ECO:0000256|SAAS:SAAS00640102}.
DOMAIN 6 302 PFK. {ECO:0000259|Pfam:PF00365}.
NP_BIND 75 76 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
REGION 24 28 Allosteric activator ADP binding; shared
with dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00339}.
REGION 128 130 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00339}.
REGION 172 174 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00339}.
REGION 188 190 Allosteric activator ADP binding.
{ECO:0000256|HAMAP-Rule:MF_00339}.
REGION 216 218 Allosteric activator ADP binding.
{ECO:0000256|HAMAP-Rule:MF_00339}.
REGION 276 279 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00339}.
ACT_SITE 130 130 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00339}.
METAL 106 106 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_00339}.
BINDING 14 14 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_00339}.
BINDING 14 14 Diphosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01976}.
BINDING 165 165 Substrate; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00339}.
BINDING 214 214 Allosteric activator ADP.
{ECO:0000256|HAMAP-Rule:MF_00339}.
BINDING 225 225 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00339}.
BINDING 270 270 Substrate; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_00339}.
SITE 107 107 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_01976}.
SITE 127 127 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000256|HAMAP-Rule:MF_01976}.
SEQUENCE 346 AA; 37349 MW; 289EABF951222FC6 CRC64;
MKPVKKIGVL TGGGDCPGLN AAIRAVVRRA NSYGYEVIGI KRGWHGLIYG ETEPLTNFSV
SGILHVGGTI IGTSRTNPFK NEEDLQRLLA NYKKFGIDAL ISIGGEDTLG VAYKLSEKGI
PIVGIPKTID NDLSGTDFTF GFDTAVTIVT DAIDRLHSTA ESHDRIMVVE VMGRHTGWIA
TFGGIAGGAD IILIPEVSFD IGEVCTMIKK RHERGKNFSI IVVAEGAKPK DVDKYITSSN
QVDEFGHIKL GGVGNFLGTE IEKRTGYDTR VTVLGHIQRG GSPTANDRVL ATRFGVAAVD
LIKEGKFGRM VALQCNKIVD IDISEPVKKL KTVDPDLYEI AKVFFG


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