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

Isoprenyl transferase (EC 2.5.1.-)

 B3U4U2_9BACT            Unreviewed;       261 AA.
B3U4U2;
02-SEP-2008, integrated into UniProtKB/TrEMBL.
02-SEP-2008, sequence version 1.
28-FEB-2018, entry version 64.
RecName: Full=Isoprenyl transferase {ECO:0000256|HAMAP-Rule:MF_01139};
EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01139};
Name=ispU {ECO:0000313|EMBL:ACE75659.1};
Synonyms=uppS {ECO:0000313|EMBL:CBK41253.1};
ORFNames=NIDE1513 {ECO:0000313|EMBL:CBK41253.1};
Nitrospira defluvii.
Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
NCBI_TaxID=330214 {ECO:0000313|EMBL:ACE75659.1};
[1] {ECO:0000313|EMBL:ACE75659.1}
NUCLEOTIDE SEQUENCE.
PubMed=18459973; DOI=10.1111/j.1462-2920.2008.01646.x;
Maixner F., Wagner M., Lucker S., Pelletier E., Schmitz-Esser S.,
Hace K., Spieck E., Konrat R., Le Paslier D., Daims H.;
"Environmental genomics reveals a functional chlorite dismutase in the
nitrite-oxidizing bacterium 'Candidatus Nitrospira defluvii'.";
Environ. Microbiol. 10:3043-3056(2008).
[2] {ECO:0000313|EMBL:CBK41253.1, ECO:0000313|Proteomes:UP000001660}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.1003860107;
Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
"A Nitrospira metagenome illuminates the physiology and evolution of
globally important nitrite-oxidizing bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010).
[3] {ECO:0000313|EMBL:CBK41253.1}
NUCLEOTIDE SEQUENCE.
Genoscope - CEA;
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate
(IPP) with allylic pyrophosphates generating different type of
terpenoids. {ECO:0000256|HAMAP-Rule:MF_01139}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01139};
Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_01139};
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
-!- SIMILARITY: Belongs to the UPP synthase family.
{ECO:0000256|HAMAP-Rule:MF_01139}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; EU559167; ACE75659.1; -; Genomic_DNA.
EMBL; FP929003; CBK41253.1; -; Genomic_DNA.
RefSeq; WP_013248077.1; NC_014355.1.
STRING; 330214.NIDE1513; -.
EnsemblBacteria; CBK41253; CBK41253; NIDE1513.
KEGG; nde:NIDE1513; -.
eggNOG; ENOG4105CR3; Bacteria.
eggNOG; COG0020; LUCA.
HOGENOM; HOG000006055; -.
KO; K00806; -.
OrthoDB; POG091H00BZ; -.
BioCyc; CNIT330214:G1GVO-1406-MONOMER; -.
Proteomes; UP000001660; Chromosome.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
CDD; cd00475; Cis_IPPS; 1.
Gene3D; 3.40.1180.10; -; 1.
HAMAP; MF_01139; ISPT; 1.
InterPro; IPR001441; UPP_synth-like.
InterPro; IPR018520; UPP_synth-like_CS.
InterPro; IPR036424; UPP_synth-like_sf.
PANTHER; PTHR10291; PTHR10291; 1.
Pfam; PF01255; Prenyltransf; 1.
SUPFAM; SSF64005; SSF64005; 1.
TIGRFAMs; TIGR00055; uppS; 1.
PROSITE; PS01066; UPP_SYNTHASE; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000001660};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
Reference proteome {ECO:0000313|Proteomes:UP000001660};
Transferase {ECO:0000256|HAMAP-Rule:MF_01139,
ECO:0000313|EMBL:ACE75659.1}.
REGION 36 39 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01139}.
REGION 80 82 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01139}.
REGION 209 211 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01139}.
ACT_SITE 35 35 {ECO:0000256|HAMAP-Rule:MF_01139}.
ACT_SITE 83 83 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01139}.
METAL 35 35 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01139}.
METAL 222 222 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 40 40 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 48 48 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 52 52 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 84 84 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 86 86 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
BINDING 203 203 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01139}.
SEQUENCE 261 AA; 29645 MW; E2857822EC5E8CEF CRC64;
MNDSRSRDIE PAPDSDLLSQ LEPDLLPKHL AVIMDGNGRW AELRGLPRIA GHQEGIKSVR
ELISLSLELG IKVLTIYAFS QENWNRPAQE ITALMGLLEH YLSTERSSLV EKGVRFQTIG
RVTALPPSAL QWVRTTEQET AHLDKLILNV ALSYGGRAEL VDAAKELARA VQSGRLSPDQ
IDEQAMQRAL YTHNLPDPDL LIRTSGETRI SNFLLWQLAY TELYFTPTLW PDFRRRETLV
ALIEYQRRER RFGRVLSSVS S


Related products :

Catalog number Product name Quantity
70024-64-5 Isoprenyl aluminium 75 percent in Hexane 1g
U0609m CLIA Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
E0609m ELISA Glutathione S-transferase A1,Glutathione S-transferase Ya,Glutathione S-transferase Ya1,GST class-alpha member 1,Gsta,Gsta1,Gstya,Mouse,Mus musculus 96T
U0609m CLIA Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
E0609m ELISA Glutathione S-transferase A3,Glutathione S-transferase Ya3,Glutathione S-transferase Yc,GST class-alpha member 3,Gsta3,Gstyc,Mouse,Mus musculus 96T
EIAAB37659 3-oxoacid-CoA transferase 2A,FKSG25,Homo sapiens,Human,OXCT2,SCOT-t,Succinyl-CoA 3-ketoacid-coenzyme A transferase 2, mitochondrial,Testis-specific succinyl-CoA 3-oxoacid CoA-transferase
EIAAB37651 3-oxoacid-CoA transferase 2B,Mouse,Mus musculus,Oxct2b,SCOT-t2,Succinyl-CoA 3-ketoacid-coenzyme A transferase 2B, mitochondrial,Testis-specific succinyl-CoA 3-oxoacid CoA-transferase 2
EIAAB37650 3-oxoacid-CoA transferase 2A,Mouse,Mus musculus,Oxct2a,SCOT-t1,Succinyl-CoA 3-ketoacid-coenzyme A transferase 2A, mitochondrial,Testis-specific succinyl-CoA 3-oxoacid CoA-transferase 1
EIAAB37649 3-oxoacid-CoA transferase 2A,Oxct2a,Rat,Rattus norvegicus,SCOT-t1,Succinyl-CoA 3-ketoacid-coenzyme A transferase 2A, mitochondrial,Testis-specific succinyl-CoA 3-oxoacid CoA-transferase 1
EIAAB37657 3-oxoacid-CoA transferase 1,Homo sapiens,Human,OXCT,OXCT1,SCOT,SCOT-s,Somatic-type succinyl-CoA 3-oxoacid-CoA-transferase,Succinyl-CoA 3-ketoacid-coenzyme A transferase 1, mitochondrial
EIAAB37656 3-oxoacid-CoA transferase 1,Oxct,Oxct1,Rat,Rattus norvegicus,Scot,SCOT-s,Somatic-type succinyl-CoA 3-oxoacid CoA-transferase,Succinyl-CoA 3-ketoacid-coenzyme A transferase 1, mitochondrial
EIAAB37658 3-oxoacid-CoA transferase 1,Mouse,Mus musculus,Oxct,Oxct1,Scot,SCOT-s,Somatic-type succinyl-CoA 3-oxoacid CoA-transferase,Succinyl-CoA 3-ketoacid-coenzyme A transferase 1, mitochondrial
EIAAB37655 3-oxoacid-CoA transferase 1,OXCT,OXCT1,Pig,SCOT,SCOT-s,Somatic-type succinyl-CoA 3-oxoacid CoA-transferase,Succinyl-CoA 3-ketoacid-coenzyme A transferase 1, mitochondrial,Sus scrofa
U0609h CLIA Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
U0609m CLIA Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
U0609h CLIA Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
E0609h ELISA kit Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
U0609h CLIA Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609m ELISA Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
E0609h ELISA kit Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
E0609h ELISA kit Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609h ELISA Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 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