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

Multifunctional fusion protein [Includes: UDP-N-acetylenolpyruvoylglucosamine reductase (EC 1.3.1.98) (UDP-N-acetylmuramate dehydrogenase); UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); UDP-N-acetylmuramyl-tripeptide synthetase (EC 6.3.2.-) (UDP-MurNAc-tripeptide synthetase)]

 A0A0G1C4S4_9BACT        Unreviewed;      1220 AA.
A0A0G1C4S4;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
23-MAY-2018, entry version 31.
SubName: Full=UDP-N-acetylmuramate-L-alanine ligase {ECO:0000313|EMBL:KKS80449.1};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
Synonyms=murB {ECO:0000256|HAMAP-Rule:MF_00037},
murC {ECO:0000256|HAMAP-Rule:MF_00046};
ORFNames=UV56_C0017G0004 {ECO:0000313|EMBL:KKS80449.1};
Candidatus Woesebacteria bacterium GW2011_GWC1_43_10b.
Bacteria; Candidatus Woesebacteria.
NCBI_TaxID=1618585 {ECO:0000313|EMBL:KKS80449.1, ECO:0000313|Proteomes:UP000034611};
[1] {ECO:0000313|EMBL:KKS80449.1, ECO:0000313|Proteomes:UP000034611}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
Wilkins M.J., Williams K.H., Banfield J.F.;
"rRNA introns, odd ribosomes, and small enigmatic genomes across a
large radiation of phyla.";
Nature 0:0-0(2015).
-!- FUNCTION: Catalyzes the addition of an amino acid to the
nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
(UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00812040}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L-
alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
alanine. {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00650646}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-
N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH.
{ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00098041}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00174316};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00650633}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650638}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurB family. {ECO:0000256|HAMAP-
Rule:MF_00037, ECO:0000256|SAAS:SAAS00558987}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KKS80449.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; LCEY01000017; KKS80449.1; -; Genomic_DNA.
EnsemblBacteria; KKS80449; KKS80449; UV56_C0017G0004.
PATRIC; fig|1618585.3.peg.224; -.
UniPathway; UPA00219; -.
Proteomes; UP000034611; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0008763; F:UDP-N-acetylmuramate-L-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.40.1190.10; -; 2.
Gene3D; 3.90.190.20; -; 2.
Gene3D; 3.90.78.10; -; 1.
HAMAP; MF_00037; MurB; 1.
HAMAP; MF_00046; MurC; 1.
HAMAP; MF_00208; MurE; 1.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR000713; Mur_ligase_N.
InterPro; IPR003170; MurB.
InterPro; IPR011601; MurB_C.
InterPro; IPR036635; MurB_C_sf.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC.
Pfam; PF01565; FAD_binding_4; 1.
Pfam; PF01225; Mur_ligase; 2.
Pfam; PF02875; Mur_ligase_C; 2.
Pfam; PF08245; Mur_ligase_M; 2.
Pfam; PF02873; MurB_C; 1.
SUPFAM; SSF53244; SSF53244; 2.
SUPFAM; SSF53623; SSF53623; 2.
SUPFAM; SSF56176; SSF56176; 1.
SUPFAM; SSF56194; SSF56194; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR00179; murB; 1.
TIGRFAMs; TIGR01082; murC; 1.
PROSITE; PS51387; FAD_PCMH; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00650652};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650620};
Cell division {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650620};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650625};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650655};
Complete proteome {ECO:0000313|Proteomes:UP000034611};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650657};
FAD {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00990849};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00990849};
Ligase {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00650635, ECO:0000313|EMBL:KKS80449.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
NADP {ECO:0000256|HAMAP-Rule:MF_00037, ECO:0000256|SAAS:SAAS00057124};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00046,
ECO:0000256|SAAS:SAAS00650652};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00057181};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00037,
ECO:0000256|SAAS:SAAS00650625};
Reference proteome {ECO:0000313|Proteomes:UP000034611}.
DOMAIN 927 1090 FAD-binding PCMH-type.
{ECO:0000259|PROSITE:PS51387}.
NP_BIND 98 104 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
NP_BIND 547 553 ATP. {ECO:0000256|HAMAP-Rule:MF_00046}.
ACT_SITE 1069 1069 {ECO:0000256|HAMAP-Rule:MF_00037}.
ACT_SITE 1120 1120 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_00037}.
ACT_SITE 1210 1210 {ECO:0000256|HAMAP-Rule:MF_00037}.
BINDING 20 20 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 169 169 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 175 175 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 177 177 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOD_RES 209 209 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 1220 AA; 134331 MW; 33C075245BBD9AE3 CRC64;
MQLEELLQKI GNYSGITDDS RKVMKNYIFV AIRGIKNDGH DFISDALKNG AGVVVGEEEI
KISIPYLKVL DSREALGKLA SHFFGNPSNR LKVIGVTGTD GKTTTANLIY FMLETAGKRV
GLISTLGAKI DKEEVDTGLH VTNPDPISLQ KILSEFVLKG AEFAVVEVTS HGLDQKRVAG
VKFDMGVLTN ITREHLDYHK TFEAYVKAKS KLFAGVRISV LNKNDSSYKK IKPLIPKGIK
IIEYPMALSG PLVEATNGRF PEDYNKLNTQ AAIAAVRVFV DFAHTPNALQ NALFELRKKV
GRKGKIISVF GSAGERDRAK RSIMGEISAR LADVSVFTAE DPRSEDVEGI IDQLVEGTKK
VKGEPKYYRI SERGEAIWFA VNKLAGSEDI VAIFGKGHEK SMAYGVKEYP WSDQEAVYEA
LKGRIKLVEK GFDFDRLKNV HFTGIKGVGM ASLALCFDDL GIKVSGSDTN EVFVTDETLE
KRKISWRVGF SGKNVSRKCD LLITTGAHGG LTNPEVLEAK KRGIATITHA EGLAKIGAGK
EVIAVSGVGG KSTTSSIISH LLEKAGLEPS FAIGVGNIFP LGTPGKFNSK GKHFICEADE
FAISPGINDN PRFSLLSPKI LVATNIEHDH PDIYPRLSDT KETFKEFFKK VPEDGWLVVN
VDNKNIRDVI SDVDVPKATY GFSPDADWKI FDVSYSPGST LFSLIHRGDI VKNMKINIPG
QYNVQNATAA FVVATLLGIS PKKVKDGLNS FVGVKRRFEF VGEVGGMLIY DDYAHHPLEI
KAVLKAARQW FPDRRVVAVF QPHTYSRTKA LFGQFAESFK GANVSAFMDI YSSAREKKDP
NVSSERLAQE TKKYVKNSYY IGSHKEATYW LKKNLRSGDL LLTLGAGDIF YLHEDLLGKT
KAINEPKSIF GDKVLSQEPL ENHTTLGLGG PASFFIKADS EDELISIVKK ANSLGVKNMV
IGDGSDLLVS EKGFPGLVIK NNIQGIKTSN YKFMVKCGTS LQSLVDRSIM EGCQGMEKMT
GIPGTVGGAV YGNAGAYGQV VSDNLTRVRA FDGKKVRWVP KKLCQFGYRE SIFKKNKWVL
LEVEFLFKSK VSPAQLKKEA ADTLTLRLKK YKPGLKCPGS FFKNIEVKDL TREQLIKIPK
EKIVYGKIPA GYLLEEVGAK GKRLGKILIA DFHANLFINT GGGNPTDFYK LAKTYTKKVE
EKFGIKLEPE VQLVGFSQNV


Related products :

Catalog number Product name Quantity
EIAAB40743 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Mouse,Mus musculus
EIAAB40744 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Rat,Rattus norvegicus
EIAAB40742 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,GARS,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Homo sapiens,Human
EIAAB40674 Aars,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Rat,Rattus norvegicus
EIAAB40675 Aars,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Mouse,Mus musculus
EIAAB40678 Aars2,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Rat,Rattus norvegicus,rCG_43500
EIAAB40676 Aars2,Aarsl,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Gm89,Kiaa1270,Mouse,Mus musculus
EIAAB40677 AARS2,AARSL,Alanine--tRNA ligase,Alanyl-tRNA synthetase, mitochondrial,AlaRS,Homo sapiens,Human,KIAA1270
EIAAB40673 AARS,Alanine--tRNA ligase,Alanyl-tRNA synthetase, cytoplasmic,AlaRS,Homo sapiens,Human,Renal carcinoma antigen NY-REN-42
EIAAB33185 Adenylosuccinate synthetase isozyme 1,Adenylosuccinate synthetase, basic isozyme,Adenylosuccinate synthetase, muscle isozyme,AdSS 1,ADSS1,ADSSL1,AMPSase 1,Homo sapiens,Human,IMP--aspartate ligase 1,M-
EIAAB33183 Adenylosuccinate synthetase isozyme 1,Adenylosuccinate synthetase, basic isozyme,Adenylosuccinate synthetase, muscle isozyme,AdSS 1,Adss1,Adssl1,AMPSase 1,IMP--aspartate ligase 1,Mouse,M-type adenylos
EIAAB31988 Coab,Mouse,Mus musculus,Phosphopantothenate--cysteine ligase,Phosphopantothenoylcysteine synthetase,PPC synthetase,Ppcs
EIAAB33182 Adenylosuccinate synthetase isozyme 1,Adenylosuccinate synthetase, basic isozyme,Adenylosuccinate synthetase, muscle isozyme,AdSS 1,ADSS1,ADSSL1,AMPSase 1,IMP--aspartate ligase 1,M-type adenylosuccina
EIAAB33184 Adenylosuccinate synthetase isozyme 1,Adenylosuccinate synthetase, basic isozyme,Adenylosuccinate synthetase, muscle isozyme,AdSS 1,ADSS1,ADSSL1,AMPSase 1,Bos taurus,Bovine,IMP--aspartate ligase 1,M-t
EIAAB31989 COAB,Homo sapiens,Human,Phosphopantothenate--cysteine ligase,Phosphopantothenoylcysteine synthetase,PPC synthetase,PPCS
15-288-22064F 2'-5'-oligoadenylate synthetase 1 - EC 2.7.7.-; (2-5')oligo(A) synthetase 1; 2-5A synthetase 1; p46_p42 OAS; E18_E16 Polyclonal 0.05 mg
15-288-22064F 2'-5'-oligoadenylate synthetase 1 - EC 2.7.7.-; (2-5')oligo(A) synthetase 1; 2-5A synthetase 1; p46_p42 OAS; E18_E16 Polyclonal 0.1 mg
10-288-22064F 2'-5'-oligoadenylate synthetase 1 - EC 2.7.7.-; (2-5')oligo(A) synthetase 1; 2-5A synthetase 1; p46_p42 OAS; E18_E16 0.05 mg
10-288-22064F 2'-5'-oligoadenylate synthetase 1 - EC 2.7.7.-; (2-5')oligo(A) synthetase 1; 2-5A synthetase 1; p46_p42 OAS; E18_E16 0.1 mg
EIAAB33190 Adenylosuccinate synthetase isozyme 2,Adenylosuccinate synthetase, acidic isozyme,Adenylosuccinate synthetase, liver isozyme,ADSS,AdSS 2,ADSS2,AMPSase 2,Homo sapiens,Human,IMP--aspartate ligase 2,L-ty
EIAAB33189 Adenylosuccinate synthetase isozyme 2,Adenylosuccinate synthetase, acidic isozyme,Adenylosuccinate synthetase, liver isozyme,ADSS,AdSS 2,ADSS2,AMPSase 2,Bos taurus,Bovine,IMP--aspartate ligase 2,L-typ
EIAAB26266 Glutamine-dependent NAD(+) synthetase,Mouse,Mus musculus,NAD(+) synthase [glutamine-hydrolyzing],NAD(+) synthetase,Nadsyn1,NH3-dependent NAD(+) synthetase-like protein
EIAAB33186 Adenylosuccinate synthetase isozyme 2,Adenylosuccinate synthetase, acidic isozyme,Adenylosuccinate synthetase, liver isozyme,Adss,AdSS 2,Adss2,AMPSase 2,IMP--aspartate ligase 2,L-type adenylosuccinate
EIAAB33188 Adenylosuccinate synthetase isozyme 2,Adenylosuccinate synthetase, acidic isozyme,Adenylosuccinate synthetase, liver isozyme,ADSS,AdSS 2,ADSS2,AMPSase 2,IMP--aspartate ligase 2,L-type adenylosuccinate
EIAAB40912 Homo sapiens,Human,Probable threonyl-tRNA synthetase 2, cytoplasmic,TARSL2,Threonine--tRNA ligase,Threonyl-tRNA synthetase-like protein 2,ThrRS


 

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