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

Bifunctional enzyme MurC/Ddl [Includes: UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase); D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanylalanine synthetase)]

 MUDD_CHLMU              Reviewed;         802 AA.
Q9PLG1;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
10-OCT-2018, entry version 127.
RecName: Full=Bifunctional enzyme MurC/Ddl;
Includes:
RecName: Full=UDP-N-acetylmuramate--L-alanine ligase;
EC=6.3.2.8;
AltName: Full=UDP-N-acetylmuramoyl-L-alanine synthetase;
Includes:
RecName: Full=D-alanine--D-alanine ligase;
EC=6.3.2.4;
AltName: Full=D-Ala-D-Ala ligase;
AltName: Full=D-alanylalanine synthetase;
Name=murC/ddl; OrderedLocusNames=TC_0143;
Chlamydia muridarum (strain MoPn / Nigg).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=243161;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
PubMed=10684935; DOI=10.1093/nar/28.6.1397;
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).
-!- FUNCTION: Cell wall formation. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramate + L-
alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
alanine.
-!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
alanyl-D-alanine.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the MurCDEF
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the D-alanine--
D-alanine ligase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF39021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AE002160; AAF39021.1; ALT_INIT; Genomic_DNA.
PIR; B81737; B81737.
RefSeq; WP_010229511.1; NZ_CP027217.1.
ProteinModelPortal; Q9PLG1; -.
SMR; Q9PLG1; -.
STRING; 243161.CmurN_010100000718; -.
PRIDE; Q9PLG1; -.
EnsemblBacteria; AAF39021; AAF39021; TC_0143.
GeneID; 1245677; -.
KEGG; cmu:TC_0143; -.
eggNOG; ENOG4105DFU; Bacteria.
eggNOG; COG0773; LUCA.
eggNOG; COG1181; LUCA.
KO; K01921; -.
KO; K01924; -.
UniPathway; UPA00219; -.
Proteomes; UP000000800; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.1490.20; -; 1.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00047; Dala_Dala_lig; 1.
HAMAP; MF_00046; MurC; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000291; D-Ala_lig_Van_CS.
InterPro; IPR005905; D_ala_D_ala.
InterPro; IPR011095; Dala_Dala_lig_C.
InterPro; IPR011127; Dala_Dala_lig_N.
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; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR005758; UDP-N-AcMur_Ala_ligase_murC.
Pfam; PF07478; Dala_Dala_lig_C; 1.
Pfam; PF01820; Dala_Dala_lig_N; 1.
Pfam; PF01225; Mur_ligase; 1.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF52440; SSF52440; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
TIGRFAMs; TIGR01082; murC; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Ligase; Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
Nucleotide-binding; Peptidoglycan synthesis.
CHAIN 1 802 Bifunctional enzyme MurC/Ddl.
/FTId=PRO_0000177914.
DOMAIN 566 777 ATP-grasp.
NP_BIND 110 116 ATP. {ECO:0000255}.
NP_BIND 599 654 ATP. {ECO:0000250}.
REGION 1 445 UDP-N-acetylmuramate--alanine ligase.
REGION 446 802 D-alanine--D-alanine ligase.
METAL 731 731 Magnesium or manganese 1. {ECO:0000250}.
METAL 744 744 Magnesium or manganese 1. {ECO:0000250}.
METAL 744 744 Magnesium or manganese 2. {ECO:0000250}.
METAL 746 746 Magnesium or manganese 2. {ECO:0000250}.
SEQUENCE 802 AA; 88744 MW; 3FAF071C3CB78F96 CRC64;
MKSLCYHFIG IGGIGMSALA HILLDRGYSV SGSDLSEGKI VETLKNKGVK FFLGNQEEHV
PEESVVVYGS GISKNNPEFL AALNKGNRLI HRAELLAELT KEQISIFVTG SHGKTTVSSL
ITVILQEAGK TPSFAIGGLN GEGINGSSGS EYFVAEADES DGSIRNYSPE FSVITNIDDE
HLSNFGGDRE RLLASLQDFS TKTRQICWYN GDCSRLRSCL VGHTFGFTSS CDLHILTYRQ
EGWRSFFTVR YQNVLYEDVE VRLVGEHNVM NAAAAMGVAL SLGIDEDTIR DALQRFPGVQ
RRLQRKNSSE VFLFLEDYAH HPSEIACTLQ AVRSAVGSRR VLAICQPHRF SRLKECMGCF
PSAFKGADEV LLTDVYSAGE AEEDVSYKEL AQSISRESLV TCAYVPFSEL QGFLEKHIRV
HDVCVALGAG DIEVLGESLR DFEPKKLSLG LICGGRSCEH DISILSAQNI AKYLSHSFYE
VQYFLITREG LWKTGSSLEL SEETGKTIFD PEIAGKLSKV DVILPILHGP YGEDGAMQGF
LETIGKPYTG PSLVFAAIGM NKVLTKRFMS DLGIPVVPYL PLTLKGWKQD QEKCLAQIKA
AFSFPMFVKS VHLGSSIGVF EVHDTNELRD AINEAFVRDD DVFIEESRLG CREIEVSFLG
DGSGVFFVAG MHERRGRGGF IDYQEKYGLS GRASAQIVFD VDLSKETREQ LLGVAEKIYR
LLQGKGSCRI DFFVDNEGSF WLSEINPIPG MTTASPFLAA FVRKGWNREQ IVHQLVIDGL
QRFDQRQRLI STPLIDQALA AR


Related products :

Catalog number Product name Quantity
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 0.02 mg
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 0.005 mg
10-663-45328 Alanine tRNA Ligase (PL-12) Human - EC 6.1.1.7; Alanine--tRNA ligase; AlaRS; NY-REN-42 antigen N_A 1 mg
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
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody 100 ul
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody Antibodies 100 ul
70-600 anti-AlaRS (Alanine-tRNA Ligase) antibody Antibodies DNA Repair_Recombination 100 ul
30-489 GPT and GPT2 (EC 2.6.1.2), also known as alanine transaminases, are pyridoxal enzymes that catalyze the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. By 0.05 mg
26-367 GPT and GPT2 (EC 2.6.1.2), also known as alanine transaminases, are pyridoxal enzymes that catalyze the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. By 0.05 mg
9000-86-6 Alanine aminotransferase Alanine aminotransfera 1g
7764-95-6 N-tert-Butoxycarbonyl-D-alanine BOC-D-Alanine 1g
125814-23-5 Z-L-Alanine N-carboxyanhydride Z-L-Alanine N-carboxya 1g
EIAAB36858 ACSB,ACSVL6,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,FACVL3,FATP5,FATP-5,Fatty acid transport protein 5,Fatty-acid-coenzyme A ligase, very long-chain 3,
EALA-100 EnzyChrom™ L-Alanine Assay Kit, Quantitative assay of L-Alanine by colorimetric (570nm) or fluorimetric (530nm_590nm) methods 100Tests
EALT-100 EnzyChrom™ Alanine Transaminase Assay Kit, Quantitative determination of Alanine transaminase activity at 340nm 100Tests
orb62010 D-Alanine D-Alanine For research use only. 400 g
EH1717 N-acetylmuramoyl-L-alanine amidase Elisa Kit 96T
EALA-100 EnzyChrom™ L-Alanine Assay Kit, Quantitative assay of L-Alanine by colorimetric (570nm) or fluorimetric (530nm_590nm) methods. Procedure 60 min. Kit size 100 tests. Detection limit 0.4 µM. Shelf li 100tests
EALT-100 EnzyChrom™ Alanine Transaminase Assay Kit, Quantitative determination of Alanine transaminase activity at 340nm. Procedure 10 min. Kit size 100 tests. Detection limit 2 U_L. Shelf life 3 months. S 100tests
3403-35-6 D_Phenyl alanine tert_butyl ester hydroch D_Phenyl alanine tert_b 1g


 

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