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

Unplaced genomic scaffold supercont1.17, whole genome shotgun sequence

 A0A0D0TRE9_9TREE        Unreviewed;      1606 AA.
A0A0D0TRE9;
29-APR-2015, integrated into UniProtKB/TrEMBL.
29-APR-2015, sequence version 1.
20-JUN-2018, entry version 35.
RecName: Full=Pentafunctional AROM polypeptide {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=DHQS {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.3.4 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-dehydroquinate dehydratase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=3-dehydroquinase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=4.2.1.10 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=1.1.1.25 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=Shikimate kinase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=SK {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.7.1.71 {ECO:0000256|HAMAP-Rule:MF_03143};
Includes:
RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_03143};
EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_03143};
AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_03143};
Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_03143};
ORFNames=I313_06048 {ECO:0000313|EMBL:KIR38053.1};
Cryptococcus gattii VGII Ram5.
Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
Cryptococcus gattii species complex.
NCBI_TaxID=1296110 {ECO:0000313|EMBL:KIR38053.1, ECO:0000313|Proteomes:UP000053392};
[1] {ECO:0000313|EMBL:KIR38053.1, ECO:0000313|Proteomes:UP000053392}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ram5 {ECO:0000313|EMBL:KIR38053.1,
ECO:0000313|Proteomes:UP000053392};
The Broad Institute Genomics Platform;
Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
Dromer F., Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L.,
Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S.,
Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C., Naylor J.,
Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
Wortman J., Nusbaum C., Birren B.;
"The Genome Sequence of Cryptococcus gattii Ram5.";
Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic
reactions in prechorismate polyaromatic amino acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712173}.
-!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712185}.
-!- CATALYTIC ACTIVITY: 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate
= 3-dehydroquinate + phosphate. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858949}.
-!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629607}.
-!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712174}.
-!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate +
NADPH. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712180}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514};
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 2/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858971}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 3/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712175}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 4/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712177}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 5/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629576}.
-!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
biosynthesis; chorismate from D-erythrose 4-phosphate and
phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712169}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712187}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629599}.
-!- SIMILARITY: In the 2nd section; belongs to the EPSP synthase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712186}.
-!- SIMILARITY: In the 3rd section; belongs to the shikimate kinase
family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712182}.
-!- SIMILARITY: In the 4th section; belongs to the type-I 3-
dehydroquinase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712184}.
-!- SIMILARITY: In the C-terminal section; belongs to the shikimate
dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712181}.
-!- SIMILARITY: In the N-terminal section; belongs to the
dehydroquinate synthase family. {ECO:0000256|PIRNR:PIRNR000514}.
-!- SIMILARITY: In the N-terminal section; belongs to the sugar
phosphate cyclases superfamily. Dehydroquinate synthase family.
{ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00858969}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03143}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; KN847912; KIR38053.1; -; Genomic_DNA.
EnsemblFungi; KIR38053; KIR38053; I313_06048.
UniPathway; UPA00053; UER00085.
UniPathway; UPA00053; UER00086.
UniPathway; UPA00053; UER00087.
UniPathway; UPA00053; UER00088.
UniPathway; UPA00053; UER00089.
Proteomes; UP000053392; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-UniRule.
GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00502; DHQase_I; 1.
CDD; cd01556; EPSP_synthase; 1.
CDD; cd00464; SK; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.65.10.10; -; 2.
HAMAP; MF_00210; EPSP_synth; 1.
HAMAP; MF_03143; Pentafunct_AroM; 1.
HAMAP; MF_00109; Shikimate_kinase; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016037; DHQ_synth_AroB.
InterPro; IPR030960; DHQS/DOIS.
InterPro; IPR001381; DHquinase_I.
InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
InterPro; IPR006264; EPSP_synthase.
InterPro; IPR023193; EPSP_synthase_CS.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR008289; Pentafunct_AroM.
InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
InterPro; IPR031322; Shikimate/glucono_kinase.
InterPro; IPR013708; Shikimate_DH-bd_N.
InterPro; IPR010110; Shikimate_DH_AroM-type.
InterPro; IPR000623; Shikimate_kinase/TSH1.
InterPro; IPR023000; Shikimate_kinase_CS.
Pfam; PF01761; DHQ_synthase; 1.
Pfam; PF01487; DHquinase_I; 1.
Pfam; PF00275; EPSP_synthase; 1.
Pfam; PF08501; Shikimate_dh_N; 1.
Pfam; PF01202; SKI; 1.
PIRSF; PIRSF000514; Pentafunct_AroM; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF55205; SSF55205; 1.
TIGRFAMs; TIGR01356; aroA; 1.
TIGRFAMs; TIGR01357; aroB; 1.
TIGRFAMs; TIGR01093; aroD; 1.
TIGRFAMs; TIGR01809; Shik-DH-AROM; 1.
PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
PROSITE; PS01128; SHIKIMATE_KINASE; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00858978};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Complete proteome {ECO:0000313|Proteomes:UP000053392};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629621};
Kinase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Lyase {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00629772}; Membrane {ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00727050};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629584};
NADP {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|SAAS:SAAS00712176};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|SAAS:SAAS00629580};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00712172};
Transferase {ECO:0000256|HAMAP-Rule:MF_03143,
ECO:0000256|PIRNR:PIRNR000514, ECO:0000256|SAAS:SAAS00629577};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius};
Zinc {ECO:0000256|HAMAP-Rule:MF_03143, ECO:0000256|PIRNR:PIRNR000514,
ECO:0000256|SAAS:SAAS00712179}.
TRANSMEM 109 133 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 78 380 DHQ_synthase. {ECO:0000259|Pfam:PF01761}.
DOMAIN 432 853 EPSP_synthase.
{ECO:0000259|Pfam:PF00275}.
DOMAIN 1332 1413 Shikimate_dh_N.
{ECO:0000259|Pfam:PF08501}.
NP_BIND 47 49 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 84 87 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 115 117 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 158 159 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 198 201 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
NP_BIND 895 902 ATP. {ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 1 406 3-dehydroquinate synthase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
REGION 286 290 Substrate binding 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
REGION 1327 1606 Shikimate dehydrogenase.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 282 282 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 297 297 Proton acceptor; for 3-dehydroquinate
synthase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 841 841 For EPSP synthase activity.
{ECO:0000256|HAMAP-Rule:MF_03143}.
ACT_SITE 1216 1216 Proton acceptor; for 3-dehydroquinate
dehydratase activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
ACT_SITE 1244 1244 Schiff-base intermediate with substrate;
for 3-dehydroquinate dehydratase
activity. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 213 213 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 293 293 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
METAL 309 309 Zinc; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 120 120 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 149 149 Substrate 1. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 165 165 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 171 171 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 180 180 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 181 181 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 209 209 NAD. {ECO:0000256|HAMAP-Rule:MF_03143}.
BINDING 272 272 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 293 293 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 309 309 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
BINDING 378 378 Substrate 2. {ECO:0000256|HAMAP-
Rule:MF_03143}.
SEQUENCE 1606 AA; 172639 MW; 760EB3136E8E944C CRC64;
MSSSSADVLK ISILGNESIH VGFHLLPYIF ETVVTTLPSS TYVLITDTNL SAIYLNDLKV
SFEEAATRAS NKARFLVYEV APGEGAKSRK VKGEIEDWML DNKCTRDTVI LAFGGGVIGD
LAGFVAATLW VAYFGSKRVA LILGLDSMRG VKFVQIPTTL LAMVDSSVGG KTAIDTPHGK
NLIGAFWQPS YIFVDLAFLT TLPTREVSNG MAETAAIWKD DDFALLESRS AEISLAASTR
PTGSPTAGRF ASDRSHAQSL LLTVVSGSIY VKAHIVTIDE RETGLRNLVN FGHTIGHAIE
AVLTPAMLHG ECVSVGIILE AEVARQLGVL SQVAVGRLTR CLQAYGLPVS LSDRRITALP
ASSQLSVDRL LDIMKIDKKN SGPAKKIVLL SRIGKTYEEK ASVVADDVIR KVLCESVTVK
AAIPTKSPIT MATPGSKSIS NRALVLAALG KGTCRVRNLL HSDDTAVMMN ALVELKGAVF
SWEDGGDTIV VEGGGGILCT PAKGKELYLG NAGTASRFLT TVCAMVSGSA SSERSTIITG
NARMKQRPIG PLVDALTANG AKVKYLESIG CLPLDIETDG FRGGHIQLAA SVSSQYVSSI
LLCAPYAAEQ VTLELTGGQV ISQPYIDMTI AMMEQFGATC TYVNPPEYSV ESDASSATYP
LAIAAITGTT CTISNIGSSS LQGDARFAKE VLEPMGCTVE QTLTSTKVTG PPVGTLRALG
NVDMEPMTDA FLTASVLAAV AVKPCLPERK VEGLPETASR IFGIANQRVK ECNRIQAMRD
QLAKFSVETD EFDDGIIIFG KPEASLFRGA SVHCYDDHRV AMAFAVLSCI VDKTIVEEKR
CVEKTWPNFW DDLQNKIGVA VEGVELETHN RASTSAKPTA AIDRSQSDRP IFLIGMRGAG
KTYVGRMAAD ILSGQFTDAD DVFAEETRQS VSEFVAANGW DEFRKKETEI LSKFAEEHRG
NHVIALGGGI VETETAREIL KAHVAKGGHV VHVTRALEDI EAYLDSIGNT AVRPNWGETF
ADVFKRREPW YQACSSHEFY NVLEAIGCQS LEEHTKAMRA ECGRFFKFIT GRESNRPRLS
VENPTSFLSL TFPDVTPALV HLDELAEGAD AVEFRVDLLS TTGQAPTGPA LPPISFVAKQ
LASLRLATTL PIVFSVRSKD QGGMVPSDNA EAYGALVRLG LRSACEYVDL EVCWPVQVLN
SIVRLKRESH IIASWHDWTG DMAWDGEEMK AKHVLCEKYG DVAKIVGTAK SGLDNAKLAL
FVGEVRGRPE AKPLLAINMG AAGQLSRVLN PILTPVTHDA LPSRAAPGQL TAREILQARV
LIGFLPAKKF VLFGSPIAHS VSPLLHNTGF ATLGLPHKYG LHESEKVDQD VLELIRSSDF
GGASVTIPLK LDIIPHLDSV SEDAKIIGAV NTVIPRGGKL HGENTDWQAI RQAAAQNLDA
GALSDGSSTA LVIGAGGTCR AAIYAMHKLR FKTIYLFNRT PENAAKVKAS FPESYGIIVV
TSLPLPEAPA VVVSTVPGNS LTLDTSSEGI YFPSEVLSRP SGVAIDLAYK PHMTALLQAA
EKKEGWKVVP GVEILCLQGF RQFEEWTGKR APAKKMRKAV LDKYFA


Related products :

Catalog number Product name Quantity
28-673 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-702 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
29-197 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science Laboratory in RIKEN. 0.1 mg
28-655 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.1 mg
28-654 cDNA library was prepared and sequenced in Mouse Genome Encyclopedia Project of Genome Exploration Research Group in Riken Genomic Sciences Center and Genome Science laboratory in RIKEN. 0.05 mg
XGC-Roche-MetaSeq-500K Deep Sequencing of whole Metagenome: shotgun library preparation, data generation using long read (upto1 Kb read length) shotgun approach on Roche GSFLX (Minimum 2 Sample) Sample
XGC-Roche-MetaSeq-250K Deep Sequencing of whole Metagenome: shotgun library preparation, data generation using long read (upto1 Kb read length) shotgun approach on Roche GSFLX (Minimum 4 Sample) Sample
26-764 PIP5KL1 may act as a scaffold to localize and regulate type I PI (4)P 5-kinases to specific compartments within the cell, where they generate PI (4,5)P2 for actin nucleation, signaling and scaffold pr 0.05 mg
28-711 The amino acid sequence of 1110033M05Rik is derived from an annotated genomic sequence (NT_039589) using gene prediction method GNOMON, supported by mRNA and EST evidence. 0.05 mg
30-678 The amino acid sequence of hCG_1646157 is derived from an annotated genomic sequence (NT_024477) using gene prediction method GNOMON, supported by mRNA and EST evidence. The exact function of hCG_164 0.05 mg
26-571 The amino acid sequence of hCG_1646157 is derived from an annotated genomic sequence (NT_024477) using gene prediction method GNOMON, supported by mRNA and EST evidence. The exact function of hCG_164 0.05 mg
30-696 The sequence of LOC442049 is derived from an annotated genomic sequence (NW_921562) using gene prediction method GNOMON. The exact function of LOC442049 remains unknown. 0.05 mg
30-520 The sequence of LOC652559 is derived from an annotated genomic sequence (NW_922352) using gene prediction method GNOMON. The exact function of LOC652559 remains unknown. 0.05 mg
30-519 The sequence of LOC650515 is derived from an annotated genomic sequence (NW_922073) using gene prediction method GNOMON, supported by EST evidence. The exact function of LOC650515 remains unknown. 0.05 mg
30-700 The sequence of LOC641765 is derived from an annotated genomic sequence (NT_079593) using gene prediction method GNOMON, supported by EST evidence. The exact function of LOC641765 remains unknown. 0.05 mg
LF-MA41029 anti-Scaffold Attachment Factor B (6F7), Mouse monoclonal to Scaffold Attachment Factor B, Isotype IgG1, Host Mouse 50 ug
27-465 ZFP57 is a protein similar to zinc finger protein 57. It is derived from an annotated genomic sequence (NT_007592) using gene prediction method. 0.05 mg
29-191 ZFP57 is a protein similar to zinc finger protein 57. It is derived from an annotated genomic sequence (NT_007592) using gene prediction method. 0.1 mg
AB1I144 Polyclonal Antibodies: Anti-CrPV Genome polyprotein Polyclonal Antibody; Specificity: Anti-CrPV Genome polyprotein Polyclonal Antibody ; Application: IHC 0.1mg
XGC-Roche-Trans-250K Deep Sequencing of Whole Transcriptome: Shotgun Library Prep, data generation using long read(up to 1kb read length) on Roche GSFLX (Minimum 4 sample) Sample
XGC-Roche-Trans-500K Deep Sequencing of Whole Transcriptome: Shotgun Library Prep, data generation using long read(up to 1kb read length) on Roche GSFLX (Minimum 2 Sample) Sample
XGC-Roche-16SMetaG48 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 48 samples
XGC-Roche-16SMetaG24 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 24 samples
XGC-Roche-16SMetaG12 Deep Sequencing of 16S amplicon Metagenome: Library preparation using V3-V4 region-400-500bp (customized region), data generation using long read shotgun approach on Roche GSFLX 12 samples
GE-102 Equine Skeletal Muscles Genomic DNA Species: Horse Tissue Genomic DNA 0.1mg


 

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