Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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)

 PFP_TREPA               Reviewed;         573 AA.
O83553;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01980};
EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_01980};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000255|HAMAP-Rule:MF_01980};
AltName: Full=PPi-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01980};
Short=PPi-PFK {ECO:0000255|HAMAP-Rule:MF_01980};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000255|HAMAP-Rule:MF_01980};
Name=pfp {ECO:0000255|HAMAP-Rule:MF_01980}; OrderedLocusNames=TP_0542;
ORFNames=TPANIC_0542;
Treponema pallidum (strain Nichols).
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=243276;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=9665876; DOI=10.1126/science.281.5375.375;
Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
Weidman J.F., Smith H.O., Venter J.C.;
"Complete genome sequence of Treponema pallidum, the syphilis
spirochete.";
Science 281:375-388(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nichols;
PubMed=24058545; DOI=10.1371/journal.pone.0074319;
Petrosova H., Pospisilova P., Strouhal M., Cejkova D., Zobanikova M.,
Mikalova L., Sodergren E., Weinstock G.M., Smajs D.;
"Resequencing of Treponema pallidum ssp. pallidum strains Nichols and
SS14: correction of sequencing errors resulted in increased separation
of syphilis treponeme subclusters.";
PLoS ONE 8:E74319-E74319(2013).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, AND SUBUNIT.
PubMed=11164318; DOI=10.1111/j.1574-6968.2001.tb09479.x;
Roberson R.S., Ronimus R.S., Gephard S., Morgan H.W.;
"Biochemical characterization of an active pyrophosphate-dependent
phosphofructokinase from Treponema pallidum.";
FEMS Microbiol. Lett. 194:257-260(2001).
-!- 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:0000255|HAMAP-Rule:MF_01980,
ECO:0000269|PubMed:11164318}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_01980, ECO:0000269|PubMed:11164318}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01980};
-!- ENZYME REGULATION: Non-allosteric. {ECO:0000255|HAMAP-
Rule:MF_01980, ECO:0000269|PubMed:11164318}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.39 mM for phosphate {ECO:0000269|PubMed:11164318};
KM=0.042 mM for diphosphate {ECO:0000269|PubMed:11164318};
KM=0.529 mM for fructose 6-phosphate
{ECO:0000269|PubMed:11164318};
KM=0.267 mM for fructose 1,6-bisphosphate
{ECO:0000269|PubMed:11164318};
Vmax=141 umol/min/mg enzyme for the forward reaction
{ECO:0000269|PubMed:11164318};
Vmax=42.4 umol/min/mg enzyme for the reverse reaction
{ECO:0000269|PubMed:11164318};
pH dependence:
Optimum pH is 8.0 for both the forward and reverse reactions.
{ECO:0000269|PubMed:11164318};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_01980}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01980,
ECO:0000269|PubMed:11164318}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01980}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000255|HAMAP-Rule:MF_01980}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE000520; AAC65526.1; -; Genomic_DNA.
EMBL; CP004010; AGN75729.1; -; Genomic_DNA.
PIR; C71312; C71312.
RefSeq; WP_010881989.1; NC_021490.2.
ProteinModelPortal; O83553; -.
SMR; O83553; -.
IntAct; O83553; 3.
STRING; 243276.TP0542; -.
EnsemblBacteria; AAC65526; AAC65526; TP_0542.
EnsemblBacteria; AGN75729; AGN75729; TPANIC_0542.
KEGG; tpa:TP_0542; -.
KEGG; tpw:TPANIC_0542; -.
PATRIC; fig|243276.9.peg.538; -.
eggNOG; ENOG4107RJF; Bacteria.
eggNOG; COG0205; LUCA.
KO; K00895; -.
OMA; GGFDMIG; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000811; Chromosome.
Proteomes; UP000014259; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
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.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Glycolysis; Kinase; Magnesium;
Metal-binding; Reference proteome; Transferase.
CHAIN 1 573 Pyrophosphate--fructose 6-phosphate 1-
phosphotransferase.
/FTId=PRO_0000429711.
REGION 212 214 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01980}.
REGION 251 252 Substrate binding; shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_01980}.
REGION 259 261 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01980}.
REGION 434 437 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_01980}.
ACT_SITE 214 214 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01980}.
METAL 184 184 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_01980}.
BINDING 90 90 Diphosphate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01980}.
BINDING 320 320 Substrate. {ECO:0000255|HAMAP-
Rule:MF_01980}.
SITE 185 185 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:0000255|HAMAP-Rule:MF_01980}.
SITE 211 211 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000255|HAMAP-Rule:MF_01980}.
SEQUENCE 573 AA; 62427 MW; 3A9A95B01CBC134E CRC64;
MSISLLQQER HRYLPKVPDL LRGDFRRVCA RRGLSTTAVA DYDALRSLFA RTYGQPLVNF
VNASEKNEDS PMETAPEPRG LRVAIVLSGG QAPGGHNVIA GLFDGLKRWH ADSVLIGFLG
GPAGVLSGDH IEICADRVDA YRNTGGFDLI GSGRTKIESE SQFAAAAQTV TRMALDALVV
VGGDDSNTNA ALLAEHFVNS GISTKVIGVP KTIDGDLKNE AIETSFGFDT ATKTYSELIG
NIARDACSAR KYWHFIKLMG RSASHIALEC ALKTQPNVCL ISEEVAAQSL TLAQIVQSLC
DTIATRAQHG EHFGIVLVPE GLIEFIPEMK ALITELNEVM ARRAQEFEAL DTPDAQRVWI
EQALSASARA VFNALPAEIS TQLLADRDPH GNVQVSRIDT ERLLILQVTE RLAQMKQEGT
YTGVFSSIAH FFGYEGRCAF PSNFDADYCY TLGLTACLLA VHRFTGYVAS VRNLTSSVAE
WAVGGVPLTM LMNMERRHGS QKPVIKKALV DLEGMPFRVF SRRRASWALK TSYVYPGAVQ
YYGPPAVCDE PSVTIRLERP APAANSSFGH RSS


Related products :

Catalog number Product name Quantity
EIAAB32529 Homo sapiens,Human,Phosphoribosyl pyrophosphate synthase 1-like 1,Phosphoribosyl pyrophosphate synthase III,PRPS1L1,PRPS1-like 1,PRPS3,PRPSL,PRS-III,Ribose-phosphate pyrophosphokinase 3
7722-88-5 Tetrasodium pyrophosphate Sodium pyrophosphate 1g
E0717p ELISA kit 6-phosphofructokinase, muscle type,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Pig,Sus scrofa 96T
U0717p CLIA 6-phosphofructokinase, muscle type,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Pig,Sus scrofa 96T
E0717p ELISA 6-phosphofructokinase, muscle type,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Pig,Sus scrofa 96T
E0717r ELISA 6-phosphofructokinase, muscle type,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rat,Rattus norvegicus 96T
E0717b ELISA 6-phosphofructokinase, muscle type,Bos taurus,Bovine,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
U0717r CLIA 6-phosphofructokinase, muscle type,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rat,Rattus norvegicus 96T
E0717r ELISA kit 6-phosphofructokinase, muscle type,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rat,Rattus norvegicus 96T
U0717b CLIA 6-phosphofructokinase, muscle type,Bos taurus,Bovine,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
E0717b ELISA kit 6-phosphofructokinase, muscle type,Bos taurus,Bovine,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
E0717m ELISA 6-phosphofructokinase, muscle type,Mouse,Mus musculus,Pfka,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
E0717Rb ELISA 6-phosphofructokinase, muscle type,Oryctolagus cuniculus,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rabbit 96T
U0717m CLIA 6-phosphofructokinase, muscle type,Mouse,Mus musculus,Pfka,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
U0717Rb CLIA 6-phosphofructokinase, muscle type,Oryctolagus cuniculus,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rabbit 96T
E0717m ELISA kit 6-phosphofructokinase, muscle type,Mouse,Mus musculus,Pfka,PFK-A,Pfkm,Pfk-m,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
E0717Rb ELISA kit 6-phosphofructokinase, muscle type,Oryctolagus cuniculus,PFK-A,PFKM,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase,Rabbit 96T
E0717h ELISA kit 6-phosphofructokinase, muscle type,Homo sapiens,Human,PFK-A,PFKM,PFKX,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
E0717h ELISA 6-phosphofructokinase, muscle type,Homo sapiens,Human,PFK-A,PFKM,PFKX,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
U0717h CLIA 6-phosphofructokinase, muscle type,Homo sapiens,Human,PFK-A,PFKM,PFKX,Phosphofructo-1-kinase isozyme A,Phosphofructokinase 1,Phosphofructokinase-M,Phosphohexokinase 96T
YSGKAMCC107E Cyclin Dependent Kinase 2 (cdk2), Cyclin Dependent Kinase 5 (cdk5), NO X w_Cyclin Dependent Kinase (cdk)1, ~33kD, Clone 8A12, Mab anti_Human, Mouse; WB 100 µg.
EIAAB06559 CDI1,CDK2-associated dual-specificity phosphatase,CDKN3,CIP2,Cyclin-dependent kinase inhibitor 3,Cyclin-dependent kinase interactor 1,Cyclin-dependent kinase-interacting protein 2,Homo sapiens,Human,K
18-783-77631 GOAT ANTI LAPINE FRUCTOSE-6-PHOSPHATE KINASE - PfkB; EC 2.7.1.11; EC 2.7.1.56; 1-PHOSPHOFRUCTOKINASE PROTEIN Polyclonal 1 ml
E1745h ELISA kit 6-phosphofructokinase type C,6-phosphofructokinase, platelet type,Homo sapiens,Human,PFK-C,PFKF,PFKP,Phosphofructo-1-kinase isozyme C,Phosphofructokinase 1,Phosphohexokinase 96T
E1745h ELISA 6-phosphofructokinase type C,6-phosphofructokinase, platelet type,Homo sapiens,Human,PFK-C,PFKF,PFKP,Phosphofructo-1-kinase isozyme C,Phosphofructokinase 1,Phosphohexokinase 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur