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

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase)

 C3TQQ2_ECOLX            Unreviewed;       495 AA.
C3TQQ2;
16-JUN-2009, integrated into UniProtKB/TrEMBL.
16-JUN-2009, sequence version 1.
12-SEP-2018, entry version 68.
RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000313|EMBL:AMW44319.1};
ORFNames=ARC77_19765 {ECO:0000313|EMBL:AMW44319.1},
AU473_26385 {ECO:0000313|EMBL:APA44197.1},
BTQ04_13960 {ECO:0000313|EMBL:PAU13640.1},
BWP17_03930 {ECO:0000313|EMBL:OOC84694.1},
CVH05_28530 {ECO:0000313|EMBL:PJG30332.1},
ECs0089 {ECO:0000313|EMBL:ACI71604.1};
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562 {ECO:0000313|EMBL:ACI71604.1};
[1] {ECO:0000313|EMBL:ACI71604.1}
NUCLEOTIDE SEQUENCE.
STRAIN=493/89 {ECO:0000313|EMBL:ACI71604.1},
86-24 {ECO:0000313|EMBL:ACI71605.1},
87-14 {ECO:0000313|EMBL:ACI71606.1}, and
TW14359 {ECO:0000313|EMBL:ACI71608.1};
PubMed=19439656; DOI=10.1073/pnas.0812949106;
Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
Sawyer S.A., Whittam T.S., Tarr P.I.;
"A precise reconstruction of the emergence and constrained radiations
of Escherichia coli O157 portrayed by backbone concatenomic
analysis.";
Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
[2] {ECO:0000313|EMBL:AMW44319.1, ECO:0000313|Proteomes:UP000076266}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=28RC1 {ECO:0000313|EMBL:AMW44319.1,
ECO:0000313|Proteomes:UP000076266};
Baranzoni G.M., Fratamico P., Reichenberger E., Kim G.-H., Breidt F.,
Kay K.;
"Complete Genome Sequences of Escherichia coli O157:H7 strains SRCC
1675 and 28RC.";
Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:APA44197.1, ECO:0000313|Proteomes:UP000177471}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PA20 {ECO:0000313|EMBL:APA44197.1,
ECO:0000313|Proteomes:UP000177471};
Uhlich G.A., Chen C.-Y., Paoli G.;
"E. coli O157:H7 PA20.";
Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:PAU13640.1, ECO:0000313|Proteomes:UP000218692}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=STEC 621S1 {ECO:0000313|EMBL:PAU13640.1,
ECO:0000313|Proteomes:UP000218692};
Ferdous M., Moran-Gilad J., Rossen J.W., Gdalevich M.;
"Real-Time Genomic Investigation Underlying the Public Health Response
to a Shiga Toxin-Producing Escherichia Coli O26:H11 Outbreak in a
Nursery.";
Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:OOC84694.1, ECO:0000313|Proteomes:UP000188999}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=EDL 933 {ECO:0000313|EMBL:OOC84694.1,
ECO:0000313|Proteomes:UP000188999};
Kozyreva V.K., Truong C.-L., Greninger A.L., Mukhopadhyay R.,
Crandall J., Chaturvedi V.;
"Validation and Implementation of CLIA-Compliant Whole Genome
Sequencing (WGS) in Public Health Laboratory.";
Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:PJG30332.1, ECO:0000313|Proteomes:UP000231208}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KCJ4029 {ECO:0000313|EMBL:PJG30332.1,
ECO:0000313|Proteomes:UP000231208};
Han C.G.;
Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the addition of meso-diaminopimelic 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}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate +
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-
diaminoheptanedioate. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- 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_00208, ECO:0000256|RuleBase:RU004135,
ECO:0000256|SAAS:SAAS00951514}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
-!- 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 MurCDEF family. MurE subfamily.
{ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; EU906490; ACI71604.1; -; Genomic_DNA.
EMBL; EU906491; ACI71605.1; -; Genomic_DNA.
EMBL; EU906492; ACI71606.1; -; Genomic_DNA.
EMBL; EU906494; ACI71608.1; -; Genomic_DNA.
EMBL; CP015020; AMW44319.1; -; Genomic_DNA.
EMBL; CP017669; APA44197.1; -; Genomic_DNA.
EMBL; MTFS01000003; OOC84694.1; -; Genomic_DNA.
EMBL; MRVX01000041; PAU13640.1; -; Genomic_DNA.
EMBL; PGUD01000371; PJG30332.1; -; Genomic_DNA.
RefSeq; WP_000785149.1; NZ_PYPR01000045.1.
EnsemblBacteria; AMW44319; AMW44319; ARC77_19765.
EnsemblBacteria; OEG64945; OEG64945; A7H95_14470.
PATRIC; fig|562.7073.peg.592; -.
eggNOG; ENOG4107EEN; Bacteria.
eggNOG; COG0769; LUCA.
HOGENOM; HOG000268118; -.
UniPathway; UPA00219; -.
Proteomes; UP000076266; Chromosome.
Proteomes; UP000177471; Chromosome.
Proteomes; UP000188999; Unassembled WGS sequence.
Proteomes; UP000218692; Unassembled WGS sequence.
Proteomes; UP000231208; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00208; MurE; 1.
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; IPR035911; MurE/MurF_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR01085; murE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951530};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
Complete proteome {ECO:0000313|Proteomes:UP000076266,
ECO:0000313|Proteomes:UP000177471, ECO:0000313|Proteomes:UP000188999,
ECO:0000313|Proteomes:UP000218692};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951519};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:AMW44319.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951530};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}.
DOMAIN 25 102 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 114 318 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 339 425 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 116 122 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 44 46 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 158 159 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 414 417 Meso-diaminopimelate binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 414 417 Meso-diaminopimelate recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 27 27 UDP-MurNAc-L-Ala-D-Glu; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 29 29 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 157 157 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 185 185 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 191 191 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 193 193 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 390 390 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 465 465 Meso-diaminopimelate; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 469 469 Meso-diaminopimelate. {ECO:0000256|HAMAP-
Rule:MF_00208}.
MOD_RES 225 225 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 495 AA; 53390 MW; 17BEAB408DCF1BEB CRC64;
MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR YIPQAIAQGV
AAIIAEAKGE ATDGEIREMH GVPVIYLSQL NERLSALAGR FYHEPSDNLR LVGVTGTNGK
TTTTQLLAQW SQLLGETSAV MGTVGNGLLG KVIPTENTTG SAVDVQHELA GLVDQDATFC
AMEVSSHGLV QHRVAALKFA ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN
ADDEVGRRWL AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE
SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG KPTVVVDYAH
TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA IAEEFADVAV VTDDNPRTEE
PRAIINDILA GMLDAGHAKV MEDRAEAVTC AVMQAKENDV VLVAGKGHED YQIVGNQRLD
YSDRVTVARL LGVIA


Related products :

Catalog number Product name Quantity
14531-04 meso‐Erythritol 〔meso‐Erythrite〕 5G
14531-04 meso‐Erythritol 〔meso‐Erythrite〕 CAS: 149-32-6 5G
26-904 Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase, is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit a 0.05 mg
39174-47-5 Tetrasodium-meso-tetra(4-sulfonatophe Tetrasodium-meso-tetr 1g
14074-80-7 Zinc meso-tetraphenylporphine Zinc meso-tetraphenylp 1g
14172-92-0 Nickel(II)meso-tetraphenylporphine nickel(II)meso-tetraphe 1g
39050-26-5 tetrasodium-meso-tetra(4-sulfonatophen tetrasodium-meso-tetra 1g
EIAAB44058 CCA tRNA nucleotidyltransferase 1, mitochondrial,CGI-47,Homo sapiens,Human,Mitochondrial tRNA nucleotidyl transferase, CCA-adding,mt CCA-adding enzyme,mt tRNA adenylyltransferase,mt tRNA CCA-diphospho
EIAAB44057 CCA tRNA nucleotidyltransferase 1, mitochondrial,mitochondrial tRNA nucleotidyl transferase, CCA-adding,Mouse,mt CCA-adding enzyme,mt tRNA adenylyltransferase,mt tRNA CCA-diphosphorylase,mt tRNA CCA-p
M59821074 meso-Erythritol CAS: [149-32-6] 25 g
CPL-161-10 In-Meso Crystallization Plate 10pcs.
CPL-161-2 In-Meso Crystallization Plate 2pcs.
E02095 meso-Erythritol 100 G
E02095 meso-Erythritol 500 G
E02095 meso-Erythritol 25 G
E0162p ELISA kit GLNS,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS,Pig,Sus scrofa 96T
E0162p ELISA GLNS,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS,Pig,Sus scrofa 96T
E0162b ELISA Bos taurus,Bovine,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS 96T
U0162p CLIA GLNS,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS,Pig,Sus scrofa 96T
U0162b CLIA Bos taurus,Bovine,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS 96T
E0162b ELISA kit Bos taurus,Bovine,GLUL,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS 96T
EIAAB40744 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Rat,Rattus norvegicus
EIAAB40743 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,Gars,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Mouse,Mus musculus
EIAAB40742 AP-4-A synthetase,Diadenosine tetraphosphate synthetase,GARS,Glycine--tRNA ligase,Glycyl-tRNA synthetase,GlyRS,Homo sapiens,Human
E0162r ELISA Glns,Glul,Glutamate decarboxylase,Glutamate--ammonia ligase,Glutamine synthetase,GS,Rat,Rattus norvegicus 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