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

 F8EX71_TRECH            Unreviewed;       551 AA.
F8EX71;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
25-OCT-2017, entry version 43.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01980};
EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_01980};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_01980};
AltName: Full=PPi-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01980};
Short=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_01980};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_01980};
Name=pfp {ECO:0000256|HAMAP-Rule:MF_01980};
OrderedLocusNames=Spica_0660 {ECO:0000313|EMBL:AEJ18814.1};
Treponema caldarium (strain ATCC 51460 / DSM 7334 / H1) (Spirochaeta
caldaria).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=744872 {ECO:0000313|EMBL:AEJ18814.1, ECO:0000313|Proteomes:UP000000503};
[1] {ECO:0000313|Proteomes:UP000000503}
NUCLEOTIDE SEQUENCE.
STRAIN=ATCC 51460 / DSM 7334 / H1 {ECO:0000313|Proteomes:UP000000503};
PubMed=23961314; DOI=10.4056/sigs.3096473;
Abt B., Goker M., Scheuner C., Han C., Lu M., Misra M., Lapidus A.,
Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R.,
Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N.,
Mavromatis K., Mikhailova N., Huntemann M., Pati A., Chen A.,
Palaniappan K., Land M., Hauser L., Jeffries C.D., Rohde M.,
Spring S., Gronow S., Detter J.C., Bristow J., Eisen J.A.,
Markowitz V., Hugenholtz P., Kyrpides N.C., Woyke T., Klenk H.P.;
"Genome sequence of the thermophilic fresh-water bacterium Spirochaeta
caldaria type strain (H1(T)), reclassification of Spirochaeta
caldaria, Spirochaeta stenostrepta, and Spirochaeta zuelzerae in the
genus Treponema as Treponema caldaria comb. nov., Treponema
stenostrepta comb. nov., and Treponema zuelzerae comb. nov., and
emendation of the genus Treponema.";
Stand. Genomic Sci. 8:88-105(2013).
-!- 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_01980}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_01980}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01980};
-!- ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP-
Rule:MF_01980}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_01980}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01980}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000256|HAMAP-Rule:MF_01980}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01980}.
-----------------------------------------------------------------------
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EMBL; CP002868; AEJ18814.1; -; Genomic_DNA.
RefSeq; WP_013968126.1; NC_015732.1.
STRING; 744872.Spica_0660; -.
EnsemblBacteria; AEJ18814; AEJ18814; Spica_0660.
KEGG; scd:Spica_0660; -.
eggNOG; ENOG4107RJF; Bacteria.
eggNOG; COG0205; LUCA.
KO; K00895; -.
OMA; GGFDMIG; -.
OrthoDB; POG091H01AC; -.
BioCyc; TCAL744872:G12Y1-663-MONOMER; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000503; Chromosome.
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.
InterPro; IPR035966; PKF_sf.
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;
Complete proteome {ECO:0000313|Proteomes:UP000000503};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01980};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_01980};
Kinase {ECO:0000256|HAMAP-Rule:MF_01980};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01980};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01980};
Reference proteome {ECO:0000313|Proteomes:UP000000503};
Transferase {ECO:0000256|HAMAP-Rule:MF_01980}.
DOMAIN 74 362 PFK. {ECO:0000259|Pfam:PF00365}.
REGION 203 205 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01980}.
REGION 242 243 Substrate binding; shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_01980}.
REGION 250 252 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01980}.
REGION 425 428 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01980}.
ACT_SITE 205 205 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01980}.
METAL 175 175 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_01980}.
BINDING 81 81 Diphosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01980}.
BINDING 311 311 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01980}.
SITE 176 176 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_01980}.
SITE 202 202 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000256|HAMAP-Rule:MF_01980}.
SEQUENCE 551 AA; 60027 MW; F200C957EA189320 CRC64;
MEISALQKAR YAYRPKLPVI LTGPVSDIAI EFGTPTESVA DQADLRALFK HSYGKPLARF
VKGKNDKITR RLTVGVILSG GQAPGGHNVI AGLYDGLKKG NKDSKLLGFL GGPSGLIENK
VVEITDAFMD EYRNTGGFDM IGSGRTKIET PEQFAASLET AKKLGLDAVV IIGGDDSNTN
AALLAEYFLE KGEKIQVIGC PKTIDGDLKN EHIETSFGFD TATKTYSELI GNIERDANSA
KKYWHFIKLM GRSASHIALE CALQTQPNIC LISEEVEAKK LSLGQIVDQI CDSIVKRAAN
KENFGVVLIP EGLVEFVPEM KKLIAELNDL MAHYADEFAG LSGFETQAAW LGKKLSAESA
KVFASLPAEI AKQLLMDRDP HGNVQVSRIE TEKLLIGMVE QRLAELKKTG SYTGKFSALA
HFFGYEGRCA FPSNFDADYT YALGFTAFVL IASGLTGYLS SVKNLTAPAD QWVAGGVPLT
MMMNMEQRHG SKKPVIRKAL VELDGKPFKA FAAKRAEWAV KTSFLFPGAI QYYGPSEVCD
QPTKTLILEH S


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