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

Archaeosine synthase (EC 2.6.1.-) (Ammonium:preQ0-tRNA aminotransferase) (QueF-like amidinotransferase) (QueF-L)

 QUEFL_PYRCJ             Reviewed;         109 AA.
A3MSP1;
25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 1.
28-FEB-2018, entry version 53.
RecName: Full=Archaeosine synthase {ECO:0000303|PubMed:28383498};
EC=2.6.1.- {ECO:0000269|PubMed:28383498};
AltName: Full=Ammonium:preQ0-tRNA aminotransferase {ECO:0000305|PubMed:28383498};
AltName: Full=QueF-like amidinotransferase {ECO:0000303|PubMed:28383498};
Short=QueF-L {ECO:0000303|PubMed:28383498};
Name=queF-L {ECO:0000303|PubMed:28383498};
OrderedLocusNames=Pcal_0221 {ECO:0000312|EMBL:ABO07658.1};
Pyrobaculum calidifontis (strain JCM 11548 / VA1).
Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
Thermoproteaceae; Pyrobaculum.
NCBI_TaxID=410359;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=JCM 11548 / VA1;
US DOE Joint Genome Institute;
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
Lowe T.M., Richardson P.;
"Complete sequence of Pyrobaculum calidifontis JCM 11548.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, AND PATHWAY.
PubMed=22032275; DOI=10.1021/cb200361w;
Phillips G., Swairjo M.A., Gaston K.W., Bailly M., Limbach P.A.,
Iwata-Reuyl D., de Crecy-Lagard V.;
"Diversity of archaeosine synthesis in Crenarchaeota.";
ACS Chem. Biol. 7:300-305(2012).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, REACTION
MECHANISM, AND ACTIVE SITE.
PubMed=28383498; DOI=10.3390/biom7020036;
Bon Ramos A., Bao L., Turner B., de Crecy-Lagard V., Iwata-Reuyl D.;
"QueF-like, a non-homologous archaeosine synthase from the
Crenarchaeota.";
Biomolecules 7:0-0(2017).
[4] {ECO:0000244|PDB:5JYX, ECO:0000244|PDB:5K0P}
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH PREQ0 VIA A COVALENT THIOIMIDE LINKAGE, REACTION MECHANISM,
ACTIVE SITE, AND SUBUNIT.
PubMed=27802572; DOI=10.1002/prot.25202;
Mei X., Alvarez J., Bon Ramos A., Samanta U., Iwata-Reuyl D.,
Swairjo M.A.;
"Crystal structure of the archaeosine synthase QueF-like-Insights into
amidino transfer and tRNA recognition by the tunnel fold.";
Proteins 85:103-116(2017).
-!- FUNCTION: Is responsible for the final step in the biosynthesis of
archaeosine, a modified nucleoside present in the dihydrouridine
loop (D-loop) of archaeal tRNA (PubMed:28383498, PubMed:22032275).
Catalyzes the conversion of 7-cyano-7-deazaguanine (preQ0)-
modified tRNA to archaeosine-tRNA, transforming a nitrile group to
a formamidine group. Can use neither glutamine nor asparagine as
amino donor in vitro, is only able to utilize free ammonium
(PubMed:28383498). However, the enzyme might function in vivo with
a partner that serves to generate ammonium.
{ECO:0000269|PubMed:22032275, ECO:0000269|PubMed:28383498}.
-!- CATALYTIC ACTIVITY: NH(4)(+) + 7-cyano-7-carbaguanine(15) in tRNA
= archaeosine(15) in tRNA. {ECO:0000269|PubMed:28383498}.
-!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
{ECO:0000269|PubMed:22032275}.
-!- SUBUNIT: Forms a symmetric tunnel-fold (T-fold) homodecamer of two
head-to-head facing pentameric subunits, with 10 active sites at
the intermonomer interfaces. {ECO:0000269|PubMed:27802572}.
-!- SIMILARITY: Belongs to the archaeosine synthase type 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP000561; ABO07658.1; -; Genomic_DNA.
PDB; 5JYX; X-ray; 2.74 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-109.
PDB; 5K0P; X-ray; 1.94 A; A/B/C/D/E/F/G/H/I/J=1-109.
PDBsum; 5JYX; -.
PDBsum; 5K0P; -.
SMR; A3MSP1; -.
STRING; 410359.Pcal_0221; -.
EnsemblBacteria; ABO07658; ABO07658; Pcal_0221.
KEGG; pcl:Pcal_0221; -.
eggNOG; arCOG04210; Archaea.
eggNOG; COG0780; LUCA.
HOGENOM; HOG000223114; -.
OMA; VNPPYVK; -.
OrthoDB; POG093Z0INE; -.
BioCyc; MetaCyc:MONOMER-20299; -.
BioCyc; PCAL410359:GIX2-219-MONOMER; -.
UniPathway; UPA00393; -.
Proteomes; UP000001431; Chromosome.
GO; GO:0033739; F:preQ1 synthase activity; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008616; P:queuosine biosynthetic process; IEA:InterPro.
GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
InterPro; IPR029500; QueF.
Pfam; PF14489; QueF; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Transferase; tRNA processing.
CHAIN 1 109 Archaeosine synthase.
/FTId=PRO_0000442193.
REGION 43 46 Substrate binding; shared with adjacent
subunit. {ECO:0000269|PubMed:27802572}.
REGION 62 63 Substrate binding.
{ECO:0000269|PubMed:27802572}.
ACT_SITE 21 21 Thioimide intermediate.
{ECO:0000269|PubMed:27802572,
ECO:0000269|PubMed:28383498}.
ACT_SITE 28 28 Proton donor/acceptor.
{ECO:0000305|PubMed:27802572}.
BINDING 28 28 Substrate. {ECO:0000269|PubMed:27802572}.
STRAND 9 20 {ECO:0000244|PDB:5K0P}.
TURN 22 24 {ECO:0000244|PDB:5K0P}.
STRAND 26 37 {ECO:0000244|PDB:5K0P}.
STRAND 39 42 {ECO:0000244|PDB:5JYX}.
HELIX 45 53 {ECO:0000244|PDB:5K0P}.
TURN 54 57 {ECO:0000244|PDB:5K0P}.
HELIX 62 77 {ECO:0000244|PDB:5K0P}.
STRAND 80 90 {ECO:0000244|PDB:5K0P}.
STRAND 93 102 {ECO:0000244|PDB:5K0P}.
SEQUENCE 109 AA; 12055 MW; 7918C03F02536C60 CRC64;
MLKVSKSPSL VRLKTRGESV CPISKTVDSF EVSVEYIPRG AVLAIEEFKK MVDSYRGREI
LHEELAVDLL EKVKAAVNPP YVKVTVKSYY IGVEVEVVAE SGGVPPVYI


Related products :

Catalog number Product name Quantity
U1045m CLIA D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthase,UGA 96T
E1045m ELISA D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthase,UGA 96T
EIAAB33196 Ccdc139,Coiled-coil domain-containing protein 139,Mouse,Mus musculus,Psi55 synthase,Pus10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,tRNA-u
E1045m ELISA kit D5Ertd135e,Mouse,Mus musculus,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,Sepsecs,Sep-tRNA Sec-tRNA synthas 96T
EIAAB44136 Homo sapiens,Human,PP8985,PUS1,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB44137 MNCb-0873,Mouse,Mus musculus,Pus1,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB44135 Pus1,Rat,Rattus norvegicus,tRNA pseudouridine synthase A, mitochondrial,tRNA pseudouridine(38-40) synthase,tRNA pseudouridylate synthase I,tRNA-uridine isomerase I
EIAAB33197 CCDC139,Coiled-coil domain-containing protein 139,DOBI,Homo sapiens,Human,Psi55 synthase,PUS10,Putative tRNA pseudouridine synthase Pus10,tRNA pseudouridine 55 synthase,tRNA pseudouridylate synthase,t
E1045h ELISA kit Homo sapiens,Human,Liver-pancreas antigen,LP,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,SEPSECS,Sep-tRNA S 96T
E1045h ELISA Homo sapiens,Human,Liver-pancreas antigen,LP,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,SEPSECS,Sep-tRNA Sec-tR 96T
U1045h CLIA Homo sapiens,Human,Liver-pancreas antigen,LP,O-phosphoseryl-tRNA(Sec) selenium transferase,Sec synthase,Selenocysteine synthase,Selenocysteinyl-tRNA(Sec) synthase,SepSecS,SEPSECS,Sep-tRNA Sec-tRN 96T
EIAAB33200 FKSG32,Homo sapiens,Human,PUS3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
EIAAB33206 Homo sapiens,Human,PUSL1,tRNA pseudouridine synthase-like 1,tRNA pseudouridylate synthase-like 1,tRNA-uridine isomerase-like 1
EIAAB33199 Bos taurus,Bovine,PUS3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
EIAAB33198 Mouse,Mus musculus,Pus3,tRNA pseudouridine synthase 3,tRNA pseudouridylate synthase 3,tRNA-uridine isomerase 3
EIAAB33205 Mouse,Mus musculus,Pusl1,tRNA pseudouridine synthase-like 1,tRNA pseudouridylate synthase-like 1,tRNA-uridine isomerase-like 1
18-003-43159 tRNA pseudouridine synthase A - EC 5.4.99.12; tRNA-uridine isomerase I; tRNA pseudouridylate synthase I Polyclonal 0.05 mg Aff Pur
201-20-5185 SEPSECS{Sep (O-phosphoserine) tRNA Sec (selenocysteine) tRNA synthase}rabbit.pAb 0.2ml
gen14261 SPCS_MOUSE Sep-tRNA Sec-tRNA synthase ELISA tesk kit 1
gen14246 SPCS_HUMAN Sep-tRNA Sec-tRNA synthase ELISA tesk kit 1
EIAAB11992 C20orf88,DTD1,D-tyrosyl-tRNA(Tyr) deacylase 1,HARS2,Histidyl-tRNA synthase-related,Homo sapiens,Human
CSB-EL009284PI Pig glycine amidinotransferase (L-arginine glycine amidinotransferase) (GATM) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL009284RA Rat glycine amidinotransferase (L-arginine glycine amidinotransferase) (GATM) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL021019MO Mouse Sep (O-phosphoserine) tRNA Sec (selenocysteine) tRNA synthase (SEPSECS) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021019HU Human Sep (O-phosphoserine) tRNA Sec (selenocysteine) tRNA synthase (SEPSECS) ELISA kit, Species Human, Sample Type serum, plasma 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