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

CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)

 U4KSG2_ACHPJ            Unreviewed;       537 AA.
U4KSG2;
11-DEC-2013, integrated into UniProtKB/TrEMBL.
11-DEC-2013, sequence version 1.
20-JUN-2018, entry version 34.
RecName: Full=CTP synthase {ECO:0000256|HAMAP-Rule:MF_01227};
EC=6.3.4.2 {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=Cytidine triphosphate synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
Short=CTP synthetase {ECO:0000256|HAMAP-Rule:MF_01227};
Short=CTPS {ECO:0000256|HAMAP-Rule:MF_01227};
AltName: Full=UTP--ammonia ligase {ECO:0000256|HAMAP-Rule:MF_01227};
Name=pyrG {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000313|EMBL:CCV64981.1};
ORFNames=BN85414040 {ECO:0000313|EMBL:CCV64981.1};
Acholeplasma palmae (strain ATCC 49389 / J233).
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=1318466 {ECO:0000313|EMBL:CCV64981.1, ECO:0000313|Proteomes:UP000032740};
[1] {ECO:0000313|EMBL:CCV64981.1, ECO:0000313|Proteomes:UP000032740}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J233 {ECO:0000313|EMBL:CCV64981.1,
ECO:0000313|Proteomes:UP000032740};
PubMed=24158107; DOI=10.1159/000354322;
Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
"Analysis of the Complete Genomes of Acholeplasma brassicae , A.
palmae and A. laidlawii and Their Comparison to the Obligate Parasites
from ' Candidatus Phytoplasma'.";
J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
-!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
either L-glutamine or ammonia as the source of nitrogen. Regulates
intracellular CTP levels through interactions with the four
ribonucleotide triphosphates. {ECO:0000256|HAMAP-Rule:MF_01227}.
-!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate +
CTP + L-glutamate. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710710}.
-!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine
is the substrate; GTP has no effect on the reaction when ammonia
is the substrate. The allosteric effector GTP functions by
stabilizing the protein conformation that binds the tetrahedral
intermediate(s) formed during glutamine hydrolysis. Inhibited by
the product CTP, via allosteric rather than competitive
inhibition. {ECO:0000256|HAMAP-Rule:MF_01227}.
-!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
pathway; CTP from UDP: step 2/2. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710815}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710816}.
-!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for
distinguishing between UTP and CTP. The overlapping regions of the
product feedback inhibitory and substrate sites recognize a common
feature in both compounds, the triphosphate moiety. To
differentiate isosteric substrate and product pyrimidine rings, an
additional pocket far from the expected kinase/ligase catalytic
site, specifically recognizes the cytosine and ribose portions of
the product inhibitor. {ECO:0000256|HAMAP-Rule:MF_01227}.
-!- SIMILARITY: Belongs to the CTP synthase family.
{ECO:0000256|HAMAP-Rule:MF_01227, ECO:0000256|SAAS:SAAS00710794}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01227}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; FO681347; CCV64981.1; -; Genomic_DNA.
RefSeq; WP_030003864.1; NC_022538.1.
EnsemblBacteria; CCV64981; CCV64981; BN85414040.
KEGG; apal:BN85414040; -.
KO; K01937; -.
BioCyc; APAL1318466:G1HMZ-1464-MONOMER; -.
UniPathway; UPA00159; UER00277.
Proteomes; UP000032740; Chromosome Acholeplasma palmae.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
CDD; cd01746; GATase1_CTP_Synthase; 1.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_01227; PyrG; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR004468; CTP_synthase.
InterPro; IPR017456; CTP_synthase_N.
InterPro; IPR017926; GATASE.
InterPro; IPR033828; GATase1_CTP_Synthase.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11550; PTHR11550; 1.
Pfam; PF06418; CTP_synth_N; 1.
Pfam; PF00117; GATase; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00337; PyrG; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710699};
Complete proteome {ECO:0000313|Proteomes:UP000032740};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|PROSITE-ProRule:PRU00605, ECO:0000256|SAAS:SAAS00710676};
Ligase {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710762, ECO:0000313|EMBL:CCV64981.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710689};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710675};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710699};
Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|SAAS:SAAS00710748};
Reference proteome {ECO:0000313|Proteomes:UP000032740}.
DOMAIN 294 534 Glutamine amidotransferase type-1.
{ECO:0000259|PROSITE:PS51273}.
NP_BIND 15 20 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 149 151 Allosteric inhibitor CTP.
{ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 189 194 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
NP_BIND 189 194 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
REGION 1 268 Amidoligase domain. {ECO:0000256|HAMAP-
Rule:MF_01227}.
REGION 384 387 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01227}.
ACT_SITE 383 383 Nucleophile. {ECO:0000256|PROSITE-
ProRule:PRU00605}.
ACT_SITE 383 383 Nucleophile; for glutamine hydrolysis.
{ECO:0000256|HAMAP-Rule:MF_01227}.
ACT_SITE 507 507 {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|PROSITE-ProRule:PRU00605}.
ACT_SITE 509 509 {ECO:0000256|HAMAP-Rule:MF_01227,
ECO:0000256|PROSITE-ProRule:PRU00605}.
METAL 72 72 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01227}.
METAL 142 142 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 14 14 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 14 14 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 55 55 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 72 72 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 225 225 Allosteric inhibitor CTP; alternate.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 225 225 UTP; alternate. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 243 243 ATP. {ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 356 356 L-glutamine; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01227}.
BINDING 407 407 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01227}.
BINDING 461 461 L-glutamine; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01227}.
SEQUENCE 537 AA; 60002 MW; 3793DAACEF759D2A CRC64;
MSTKFIFVTG GVVSSLGKGI TASSIGQILK SRGLKVFMQK FDPYINVDPG TMSPYQHGEV
FVTDDGAETD LDLGHYERFI DENLSKDSSI TTGKIYQTVI DRERKGGYLG ATIQVIPHIT
DEIKSKLKAA AESSLADVVI TEIGGTVGDI ESLPYLEAIR QARRDYGYEN TLYLHNTLIP
YLKAANEIKT KPTQHSVKEL RSLGIQPDMI VLRSEVEIPK HVKEKIALFC DVNENAVFES
LDVEVLYQSI LNLEKQGIDD FILDHFKFNN LPKANLSEWE NLISKIKGLK EAITIGLVGK
YVSLHDAYLS ISEALKHAGY AHDVSIKIKW LSAEKINPEN VGEALADCDG ILVPGGFGKR
ATEGKIAAIQ YARENNVPMF GICYGMQLSV IEYARNVLGI KNANSTEIDP KTDAPIITKK
IKDSKLGGTL RLGLYESILK ENTKTFKAYN KGVIAERHRH RYEVNPEYVE ILEKDANFII
TGVEKTSKLV ESIELNNHPW FIAVQYHPEF VSRPLRPHPL FKDFVFAAKQ NKKGKLL


Related products :

Catalog number Product name Quantity
EIAAB33278 CTP synthase 1,CTP synthetase 1,Ctps,Mouse,Mus musculus,UTP--ammonia ligase 1
EIAAB33279 CTP synthase 1,CTP synthetase 1,CTPS,Homo sapiens,Human,UTP--ammonia ligase 1
E12899h Human Cytidine Triphosphate Synthase ELISA Kit 96T
E12898h Human Cytidine Triphosphate Synthase 2 ELISA Kit 96T
30-148 The catalytic conversion of UTP to CTP is accomplished by the enzyme cytidine-5-prime-triphosphate synthetase. The enzyme is important in the biosynthesis of phospholipids and nucleic acids, and plays 0.1 mg
30-149 The catalytic conversion of UTP to CTP is accomplished by the enzyme cytidine-5-prime-triphosphate synthetase. The enzyme is important in the biosynthesis of phospholipids and nucleic acids, and plays 0.1 mg
EIAAB33282 Bos taurus,Bovine,CTP synthase 2,CTP synthetase 2,CTPS2,UTP--ammonia ligase 2
EIAAB33280 CTP synthase 2,CTP synthetase 2,Ctps2,Rat,Rattus norvegicus,UTP--ammonia ligase 2
EIAAB33284 CTP synthase 2,CTP synthetase 2,CTPS2,Homo sapiens,Human,UTP--ammonia ligase 2
EIAAB33281 CTP synthase 2,CTP synthetase 2,Ctps2,CTPsH,Mouse,Mus musculus,UTP--ammonia ligase 2
NU-1170L Ara-cytidine-5'-triphosphate (ara-CTP), L pack Cytarabine triphosphate, Sodium salt 500Units
NU-1170S Ara-cytidine-5'-triphosphate (ara-CTP), S pack Cytarabine triphosphate, Sodium salt 100Units
NU-1170S Nucleic acids: Ara-cytidine-5'-triphosphate (ara-CTP), S pack Cytarabine triphosphate, Sodium salt 100Units
NU-1170L Nucleic acids: Ara-cytidine-5'-triphosphate (ara-CTP), L pack Cytarabine triphosphate, Sodium salt 500Units
EIAAB33283 Chicken,CTP synthase 2,CTP synthetase 2,CTPS2,Gallus gallus,RCJMB04_4c5,UTP--ammonia ligase 2
40390000-1 CTP (Cytidine-5'-triphosphate) Disodium 50 mg
NU-1170L Ara-cytidine-5'-triphosphate (ara-CTP), L pack 500Units
NU-1170L ara-Cytidine-5'-triphosphate (ara-CTP), L pack 5 x 100Units
NU-1170S Ara-cytidine-5'-triphosphate (ara-CTP), S pack 100Units
40390000-2 CTP (Cytidine-5'-triphosphate) Disodium 100 mg
NU-1170S ara-Cytidine-5'-triphosphate (ara-CTP), S pack 100
NU-1170L ara-Cytidine-5'-triphosphate (ara-CTP), L pack 5 x 100
NU-10507-C-10 2'-Fluoro-2'-deoxy-ara-cytidine-5'-triphosphate, 10 10
CD0134T Cytidine-5'-triphosphate (CTP), trisodium salt 500mg
CD0134T Cytidine-5'-triphosphate (CTP), trisodium salt 100mg


 

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