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)

 A0A1L8N360_9SPIO        Unreviewed;       329 AA.
A0A1L8N360;
15-MAR-2017, integrated into UniProtKB/TrEMBL.
15-MAR-2017, sequence version 1.
05-DEC-2018, entry version 9.
RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754002};
Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754007};
EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754021};
AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249};
ORFNames=BKP49_02740 {ECO:0000313|EMBL:OJF77398.1};
Treponema sp. CETP13.
Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
NCBI_TaxID=1908540 {ECO:0000313|EMBL:OJF77398.1, ECO:0000313|Proteomes:UP000183349};
[1] {ECO:0000313|EMBL:OJF77398.1, ECO:0000313|Proteomes:UP000183349}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Nathani N.M., Tikariha H., Hinsu A.T., Purohit H.J., Joshi C.G.;
"Candidatus Treponema sp. CETP13 genome retrieved from CETP activated
sludge metagenomes.";
Submitted (OCT-2016) 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). {ECO:0000256|HAMAP-Rule:MF_01249}.
-!- CATALYTIC ACTIVITY:
Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754017};
-!- CATALYTIC ACTIVITY:
Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate =
[HPr protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604,
Rhea:RHEA-COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
ChEBI:CHEBI:83421; Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754013};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754019};
-!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754027}.
-!- 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:SAAS00754005}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OJF77398.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; MLPZ01000002; OJF77398.1; -; Genomic_DNA.
Proteomes; UP000183349; Unassembled WGS sequence.
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: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:SAAS00754014};
Complete proteome {ECO:0000313|Proteomes:UP000183349};
Kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754024};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754029};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754025};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754014};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023};
Transferase {ECO:0000256|HAMAP-Rule:MF_01249,
ECO:0000256|SAAS:SAAS00754023}.
DOMAIN 21 134 Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.
DOMAIN 140 308 Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
NP_BIND 162 169 ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
REGION 211 220 Important for the catalytic mechanism of
both phosphorylation and
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
REGION 274 279 Important for the catalytic mechanism of
dephosphorylation. {ECO:0000256|HAMAP-
Rule:MF_01249}.
ACT_SITE 147 147 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 168 168 {ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 186 186 Proton acceptor; for phosphorylation
activity. Proton donor; for
dephosphorylation activity.
{ECO:0000256|HAMAP-Rule:MF_01249}.
ACT_SITE 253 253 {ECO:0000256|HAMAP-Rule:MF_01249}.
METAL 169 169 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
METAL 212 212 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01249}.
SEQUENCE 329 AA; 36864 MW; 70428AAF81958093 CRC64;
MASKSFTVLD LLDLELKGHN SLNLKCVSGR RGLSRKITIP DVNRPGLALS GFYDSFAHQR
VQLFGRGENA YLSKIIKEKN LDTIRQLFSY SIPCCVFTHG FIPPSEFISI SEDSGCPVLL
TDLESTEFST RLLRAFSDIF ALRKSMHGVF VEVYGLGILI LGSSGVGKSE TALELIERGH
RLVADDIVEI RCVNGNMVLG QGPNKMISHH MEIRGLGIIN IQQLYGVGAI REQKQVQLVV
KLEEWDAQKV YDRLGTEENT MDLLGVKIPM LEIPVKPGRN IPIILETAAM NERLKTMGYF
SAREFNQNVL KWIESTEAES TYYGNDDIY


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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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