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

HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr(Ser) kinase/phosphorylase)

 F8DJC0_STREP            Unreviewed;       310 AA.
F8DJC0;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
22-NOV-2017, entry version 49.
RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00720482};
Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00720486};
EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00720478};
AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000313|EMBL:AEH55916.1};
OrderedLocusNames=HMPREF0833_10885 {ECO:0000313|EMBL:AEH55916.1};
Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372
/ LMG 14537).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH55916.1, ECO:0000313|Proteomes:UP000001502};
[1] {ECO:0000313|Proteomes:UP000001502}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
{ECO:0000313|Proteomes:UP000001502};
Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G.,
Hawes A., Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W.,
Liu X., Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J.,
Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D.,
Johnson A., Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A.,
Song B.-B., Dinh H., Thornton R., Coyle M., Francisco L., Jackson L.,
Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R.,
Nguyen L., Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
Petrosino J., Highlander S., Gibbs R.;
"Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-
dependent phosphorylation of a specific serine residue in HPr, a
phosphocarrier protein of the phosphoenolpyruvate-dependent sugar
phosphotransferase system (PTS). HprK/P also catalyzes the
pyrophosphate-producing, inorganic phosphate-dependent
dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-
Ser-HPr). The two antagonistic activities of HprK/P are regulated
by several intracellular metabolites, which change their
concentration in response to the absence or presence of rapidly
metabolisable carbon sources (glucose, fructose, etc.) in the
growth medium. Therefore, by controlling the phosphorylation state
of HPr, HPrK/P is a sensor enzyme that plays a major role in the
regulation of carbon metabolism and sugar transport: it mediates
carbon catabolite repression (CCR), and regulates PTS-catalyzed
carbohydrate uptake and inducer exclusion. {ECO:0000256|HAMAP-
Rule:MF_01249}.
-!- CATALYTIC ACTIVITY: ATP + HPr = ADP + P-Ser-HPr.
{ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00720469}.
-!- CATALYTIC ACTIVITY: P-Ser-HPr + phosphate = HPr + diphosphate.
{ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00720473}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720456};
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720461}.
-!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
{ECO:0000256|HAMAP-Rule:MF_01249}.
-!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
out by the same active site and suggest a common mechanism for
both reactions. {ECO:0000256|HAMAP-Rule:MF_01249}.
-!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000256|HAMAP-
Rule:MF_01249, ECO:0000256|SAAS:SAAS00720471}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP002843; AEH55916.1; -; Genomic_DNA.
RefSeq; WP_013903893.1; NC_015678.1.
EnsemblBacteria; AEH55916; AEH55916; HMPREF0833_10885.
GeneID; 10835384; -.
KEGG; scp:HMPREF0833_10885; -.
KO; K06023; -.
Proteomes; UP000001502; Chromosome.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
CDD; cd01918; HprK_C; 1.
Gene3D; 3.40.1390.20; -; 1.
HAMAP; MF_01249; HPr_kinase; 1.
InterPro; IPR003755; HPr(Ser)_kin/Pase.
InterPro; IPR011104; Hpr_kin/Pase_C.
InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
PANTHER; PTHR30305:SF1; PTHR30305:SF1; 1.
Pfam; PF07475; Hpr_kinase_C; 1.
Pfam; PF02603; Hpr_kinase_N; 1.
SUPFAM; SSF75138; SSF75138; 1.
TIGRFAMs; TIGR00679; hpr-ser; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720483};
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01249};
Complete proteome {ECO:0000313|Proteomes:UP000001502};
Kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720472};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720484};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720477};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720481};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720483};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720472};
Transferase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00720472}.
DOMAIN 3 127 Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.
DOMAIN 130 298 Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
NP_BIND 153 160 ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
REGION 201 210 Important for the catalytic mechanism of
both phosphorylation and
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
REGION 264 269 Important for the catalytic mechanism of
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
ACT_SITE 138 138 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 159 159 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 177 177 Proton acceptor; for phosphorylation
activity. Proton donor; for
dephosphorylation activity.
{ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 243 243 {ECO:0000256|HAMAP-Rule:MF_01249}.
METAL 160 160 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
METAL 202 202 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
SEQUENCE 310 AA; 34807 MW; E51CE318CFC4894B CRC64;
MAVTVRDIQE KLRLSVVYGN DSLLSKEITT ADISRPGLEM TGYFDYYTPE RIQLVGMKEW
SYLVKMSSHN RHQVLRKMFQ PETPVIIVAR NLEIPEEMLR AAEEKQLAIL KSNVATSRLS
GELSSYLDSR LAERTSVHGV LMDIYGMGVL IQGDSGIGKS ETGLELVKRG HRLVADDRVD
IYARDEMTLW GEPAEILRHL LEIRGVGIID VMSLYGASAV KDSSQVQIAV YLENYAKDQV
YDRLGNNAEE LEIGGVTIPR IRIPVKTGRN ISVVIEAAAM NVRAKEMGYD ATKTFEERLS
QLISQNEVKE


Related products :

Catalog number Product name Quantity
EIAAB30892 Homo sapiens,Human,PHKG2,PHK-gamma-T,Phosphorylase b kinase gamma catalytic chain, testis_liver isoform,Phosphorylase kinase subunit gamma-2,PSK-C3,Serine_threonine-protein kinase PHKG2
EIAAB30887 Phkg,Phkg1,Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform,Phosphorylase kinase subunit gamma-1,Rat,Rattus norvegicus
EIAAB30888 Mouse,Mus musculus,Phkg,Phkg1,Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform,Phosphorylase kinase subunit gamma-1
EIAAB30889 Oryctolagus cuniculus,PHKG,PHKG1,Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform,Phosphorylase kinase subunit gamma-1,Rabbit
EIAAB30890 Homo sapiens,Human,PHKG,PHKG1,Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform,Phosphorylase kinase subunit gamma-1
EIAAB30894 Mouse,Mus musculus,Phkg2,PHK-gamma-T,Phosphorylase b kinase gamma catalytic chain, testis_liver isoform,Phosphorylase kinase subunit gamma-2,Serine_threonine-protein kinase PHKG2
EIAAB30893 Phkg2,PHK-gamma-T,Phosphorylase b kinase gamma catalytic chain, testis_liver isoform,Phosphorylase kinase subunit gamma-2,Rat,Rattus norvegicus,Serine_threonine-protein kinase PHKG2
EIAAB30891 Bos taurus,Bovine,PHKG2,PHK-gamma-T,Phosphorylase b kinase gamma catalytic chain, testis_liver isoform,Phosphorylase kinase subunit gamma-2,Serine_threonine-protein kinase PHKG2
18-003-42332 Phosphorylase b kinase gamma catalytic chain. testis_liver isoform - EC 2.7.11.19; PHK-gamma-T; Phosphorylase kinase subunit gamma 2; PSK-C3 Polyclonal 0.05 mg Aff Pur
EIAAB25616 5'-methylthioadenosine phosphorylase,Mouse,MTA phosphorylase,Mtap,MTAPase,Mus musculus,S-methyl-5'-thioadenosine phosphorylase
EIAAB25617 5'-methylthioadenosine phosphorylase,Homo sapiens,Human,MSAP,MTA phosphorylase,MTAP,MTAPase,S-methyl-5'-thioadenosine phosphorylase
orb71878 Phosphorylase Kinase b-Subunit Fragment (420-436) peptide This is Phosphorylase Kinase b-Subunit Fragment (420-436) peptide. For research use only. 1 mg
SP2904a Phosphorylase Kinase b-Subunit (420-436) 0.5 mg
SP2904b Phosphorylase Kinase b-Subunit (420-436) 1 mg
SP2904a Phosphorylase Kinase b-Subunit (420-436)
SP2904b Phosphorylase Kinase b-Subunit (420-436)
SP2904b Phosphorylase Kinase b_Subunit (420_436) 1.0 mg
SP2904a Phosphorylase Kinase b_Subunit (420_436) 0.5 mg
ARP33072_P050 PHKG2 (phosphorylase kinase, gamma 2 (testis)) 50 µg
E12088h Human Phosphorylase Kinase, Beta ELISA Kit 96T
SP-102107-1 Phosphorylase Kinase b-Subunit Fragment (420-436) (AA: Lys-Arg-Asn-Pro-Gly-Ser-Gln-Lys-Arg-Phe-Pro-Ser-Asn-Cys-Gly-Arg-Asp) (MW: 1946.2) 1 mg
E12087h Human Phosphorylase Kinase, Alpha 2 ELISA Kit 96T
GTX107878 Phosphorylase kinase subunit beta antibody 0.1 mg
9001-88-1 Phosphorylase kinase EC 2.7.1.38 from rabbit muscle lyop 1g
E9824h Human Phosphorylase Kinase, Alpha 1 ELISA Kit 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