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

Bifunctional protein HldE [Includes: D-beta-D-heptose 7-phosphate kinase (EC 2.7.1.167) (D-beta-D-heptose 7-phosphotransferase) (D-glycero-beta-D-manno-heptose-7-phosphate kinase); D-beta-D-heptose 1-phosphate adenylyltransferase (EC 2.7.7.70) (D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase)]

 HLDE_ECOLI              Reviewed;         477 AA.
P76658; Q2M9F3; Q6J1J5;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-MAR-2018, entry version 134.
RecName: Full=Bifunctional protein HldE;
Includes:
RecName: Full=D-beta-D-heptose 7-phosphate kinase;
EC=2.7.1.167;
AltName: Full=D-beta-D-heptose 7-phosphotransferase;
AltName: Full=D-glycero-beta-D-manno-heptose-7-phosphate kinase;
Includes:
RecName: Full=D-beta-D-heptose 1-phosphate adenylyltransferase;
EC=2.7.7.70;
AltName: Full=D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase;
Name=hldE; Synonyms=rfaE, waaE, yqiF; OrderedLocusNames=b3052, JW3024;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-477.
STRAIN=K12 / MG1655 / ATCC 47076;
Perna N.T.;
"Escherichia coli K-12 MG1655 genomic sequence correction.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
DOMAINS.
STRAIN=K12 / W1485;
PubMed=10629197; DOI=10.1128/JB.182.2.488-497.2000;
Valvano M.A., Marolda C.L., Bittner M., Glaskin-Clay M., Simon T.L.,
Klena J.D.;
"The rfaE gene from Escherichia coli encodes a bifunctional protein
involved in the biosynthesis of the lipopolysaccharide core precursor
ADP-L-glycero-D-manno-heptose.";
J. Bacteriol. 182:488-497(2000).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND ADP-L-BETA-D-HEPTOSE BIOSYNTHESIS
PATHWAY.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=11751812; DOI=10.1128/JB.184.2.363-369.2002;
Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F.,
Kosma P., Valvano M.A., Messner P.;
"Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in
Escherichia coli.";
J. Bacteriol. 184:363-369(2002).
[6]
MUTAGENESIS OF ASN-195; GLU-198 AND ASP-264, AND SUBUNIT.
PubMed=16030223; DOI=10.1128/JB.187.15.5292-5300.2005;
McArthur F., Andersson C.E., Loutet S., Mowbray S.L., Valvano M.A.;
"Functional analysis of the glycero-manno-heptose 7-phosphate kinase
domain from the bifunctional HldE protein, which is involved in ADP-L-
glycero-D-manno-heptose biosynthesis.";
J. Bacteriol. 187:5292-5300(2005).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
-!- FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-
heptose 7-phosphate at the C-1 position to selectively form D-
glycero-beta-D-manno-heptose-1,7-bisphosphate.
{ECO:0000269|PubMed:11751812}.
-!- FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-
manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-
heptose. {ECO:0000269|PubMed:11751812}.
-!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 7-phosphate +
ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP.
{ECO:0000269|PubMed:11751812}.
-!- CATALYTIC ACTIVITY: D-glycero-beta-D-manno-heptose 1-phosphate +
ATP = ADP-D-glycero-beta-D-manno-heptose + diphosphate.
{ECO:0000269|PubMed:11751812}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4.
-!- PATHWAY: Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-
manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose
from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4.
-!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16030223}.
-!- MISCELLANEOUS: In both reactions the enzyme functions only with
beta anomers.
-!- MISCELLANEOUS: The function of the domain II is independent from
the activity mediated by domain I.
-!- SIMILARITY: In the N-terminal section; belongs to the carbohydrate
kinase PfkB family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
cytidylyltransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U00096; AAC76088.1; -; Genomic_DNA.
EMBL; AP009048; BAE77103.1; -; Genomic_DNA.
EMBL; AY605712; AAT28329.1; -; Genomic_DNA.
PIR; B65093; B65093.
RefSeq; NP_417524.1; NC_000913.3.
RefSeq; WP_000869178.1; NZ_LN832404.1.
ProteinModelPortal; P76658; -.
SMR; P76658; -.
BioGrid; 4261504; 430.
DIP; DIP-10666N; -.
IntAct; P76658; 6.
STRING; 316385.ECDH10B_3227; -.
iPTMnet; P76658; -.
EPD; P76658; -.
PaxDb; P76658; -.
PRIDE; P76658; -.
EnsemblBacteria; AAC76088; AAC76088; b3052.
EnsemblBacteria; BAE77103; BAE77103; BAE77103.
GeneID; 947548; -.
KEGG; ecj:JW3024; -.
KEGG; eco:b3052; -.
PATRIC; fig|1411691.4.peg.3679; -.
EchoBASE; EB3192; -.
EcoGene; EG13416; hldE.
eggNOG; ENOG4105DW0; Bacteria.
eggNOG; COG2870; LUCA.
HOGENOM; HOG000237584; -.
InParanoid; P76658; -.
KO; K03272; -.
OMA; CDPKGKD; -.
PhylomeDB; P76658; -.
BioCyc; EcoCyc:G7590-MONOMER; -.
BioCyc; MetaCyc:G7590-MONOMER; -.
BRENDA; 2.7.1.167; 2026.
BRENDA; 2.7.7.70; 2026.
UniPathway; UPA00356; UER00437.
UniPathway; UPA00356; UER00439.
UniPathway; UPA00958; -.
PRO; PR:P76658; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0033785; F:heptose 7-phosphate kinase activity; IDA:EcoCyc.
GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IDA:EcoCyc.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
GO; GO:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd01172; RfaE_like; 1.
Gene3D; 3.40.1190.20; -; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_01603; HldE; 1.
InterPro; IPR023030; Bifunc_HldE.
InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR011611; PfkB_dom.
InterPro; IPR011913; RfaE_dom_I.
InterPro; IPR011914; RfaE_dom_II.
InterPro; IPR029056; Ribokinase-like.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
Pfam; PF00294; PfkB; 1.
SUPFAM; SSF53613; SSF53613; 1.
TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
TIGRFAMs; TIGR02198; rfaE_dom_I; 1.
TIGRFAMs; TIGR02199; rfaE_dom_II; 1.
PROSITE; PS00583; PFKB_KINASES_1; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Carbohydrate metabolism; Complete proteome;
Kinase; Lipopolysaccharide biosynthesis; Multifunctional enzyme;
Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
Transferase.
CHAIN 1 477 Bifunctional protein HldE.
/FTId=PRO_0000080107.
NP_BIND 195 198 ATP. {ECO:0000255}.
REGION 1 318 Ribokinase.
REGION 344 477 Cytidylyltransferase.
ACT_SITE 264 264 {ECO:0000255}.
MOD_RES 179 179 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 195 195 N->D: Loss of activity.
{ECO:0000269|PubMed:16030223}.
MUTAGEN 198 198 E->D: Loss of activity.
{ECO:0000269|PubMed:16030223}.
MUTAGEN 264 264 D->E: Loss of activity.
{ECO:0000269|PubMed:16030223}.
MUTAGEN 264 264 D->N: Loss of activity.
{ECO:0000269|PubMed:16030223}.
SEQUENCE 477 AA; 51051 MW; 0F03CBE160B95389 CRC64;
MKVTLPEFER AGVMVVGDVM LDRYWYGPTS RISPEAPVPV VKVNTIEERP GGAANVAMNI
ASLGANARLV GLTGIDDAAR ALSKSLADVN VKCDFVSVPT HPTITKLRVL SRNQQLIRLD
FEEGFEGVDP QPLHERINQA LSSIGALVLS DYAKGALASV QQMIQLARKA GVPVLIDPKG
TDFERYRGAT LLTPNLSEFE AVVGKCKTEE EIVERGMKLI ADYELSALLV TRSEQGMSLL
QPGKAPLHMP TQAQEVYDVT GAGDTVIGVL AATLAAGNSL EEACFFANAA AGVVVGKLGT
STVSPIELEN AVRGRADTGF GVMTEEELKL AVAAARKRGE KVVMTNGVFD ILHAGHVSYL
ANARKLGDRL IVAVNSDAST KRLKGDSRPV NPLEQRMIVL GALEAVDWVV SFEEDTPQRL
IAGILPDLLV KGGDYKPEEI AGSKEVWANG GEVLVLNFED GCSTTNIIKK IQQDKKG


Related products :

Catalog number Product name Quantity
EIAAB31019 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,Protein STM-7,PtdIns(4)P-5-kinase 1 beta,S
EIAAB30999 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Homo sapiens,Human,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase
EIAAB31001 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Mouse,Mus musculus,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase
EIAAB31016 Chicken,Gallus gallus,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,PtdIns(4)P-5-kinase 1 beta,RCJMB04_20j1
EIAAB31017 Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,Pip5k1a,Pip5k1b,PIP5K1-beta,PIP5KIalp
EIAAB31000 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase type-2 beta,Phospha
EIAAB31018 Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,Pip5k1a,Pip5k1b,PI
EIAAB29520 C2-PI3K,Homo sapiens,Human,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit beta,Phosphoinositide 3-kinase-C2-beta,PI3K-C2-beta,PIK3C2B,PtdIns-3-kinase C2 subunit beta
EIAAB31420 1-acylglycerol-3-phosphate O-acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta,1-AGP acyltransferase 2,1-AGPAT 2,Agpat2,LPAAT-beta,Lysophosphatidic acid acyltransferase beta,Mouse,
EIAAB31014 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase,Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinos
EIAAB31419 1-acylglycerol-3-phosphate O-acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta,1-AGP acyltransferase 2,1-AGPAT 2,AGPAT2,Homo sapiens,Human,LPAAT-beta,Lysophosphatidic acid acyltran
S-08125 SODIUM -B-GLYCERO PHOSPHATE 99 percent AR (B-Glycero Phosphate Sodium Salt) CAS: 13408-09-8 500 gm
S-08125 SODIUM -B-GLYCERO PHOSPHATE 99 percent AR (B-Glycero Phosphate Sodium Salt) CAS: 13408-09-8 100 gm
S-08125 SODIUM -B-GLYCERO PHOSPHATE 99 percent AR (B-Glycero Phosphate Sodium Salt) CAS: 13408-09-8 25 gm
PI42B_RAT Rat ELISA Kit FOR Phosphatidylinositol-5-phosphate 4-kinase type-2 beta 96T
pka-053 Recombinant Human Phosphatidylinositol-5-Phosphate 4-Kinase, Type II, Beta 10
pka-053 Recombinant Human Phosphatidylinositol-5-Phosphate 4-Kinase, Type II, Beta 2
RPK-053 Recombinant Human Phosphatidylinositol-5-Phosphate 4-Kinase, Type II, Beta 2
pka-053 Recombinant Human Phosphatidylinositol-5-Phosphate 4-Kinase, Type II, Beta 1mg
942-90 BETA-NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE (beta-NADP), Oxidized Form Powder 1 g
943-30 BETA-NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE (beta-NADPH), Reduced Form Lyophilized 1 g
943-30 BETA-NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE (beta-NADPH), Reduced Form Lyophilized 50 mg
943-30 BETA-NICOTINAMIDE-ADENINE DINUCLEOTIDE PHOSPHATE (beta-NADPH), Reduced Form Lyophilized 100 mg
943-10 BETA-NICOTINAMIDE-ADENINE DINUCLEOTIDE 2-PHOSPHATE (beta-NADP-K), Oxidized Form Lyophilized 1 g
SPCS3_RAT Human ELISA Kit FOR Phosphatidylinositol-4-phosphate 5-kinase type-1 beta 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