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

N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase)

 MURQ_HAEIN              Reviewed;         303 AA.
P44862;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
28-FEB-2018, entry version 122.
RecName: Full=N-acetylmuramic acid 6-phosphate etherase;
Short=MurNAc-6-P etherase;
EC=4.2.1.126;
AltName: Full=N-acetylmuramic acid 6-phosphate hydrolase;
AltName: Full=N-acetylmuramic acid 6-phosphate lyase;
Name=murQ; OrderedLocusNames=HI_0754;
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
Pasteurellaceae; Haemophilus.
NCBI_TaxID=71421;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800; DOI=10.1126/science.7542800;
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae
Rd.";
Science 269:496-512(1995).
[2]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Midwest center for structural genomics (MCSG);
"Crystal structure of hypothetical protein HI0754 from Haemophilus
influenzae.";
Submitted (JAN-2005) to the PDB data bank.
-!- FUNCTION: Specifically catalyzes the cleavage of the D-lactyl
ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-
phosphate and D-lactate. Together with AnmK, is also required for
the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either
imported from the medium or derived from its own cell wall murein,
and thus plays a role in cell wall recycling (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: (R)-lactate + N-acetyl-D-glucosamine 6-
phosphate = N-acetylmuramate 6-phosphate + H(2)O.
-!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
degradation.
-!- PATHWAY: Amino-sugar metabolism; N-acetylmuramate degradation.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- MISCELLANEOUS: A lyase-type mechanism (elimination/hydration) is
suggested for the cleavage of the lactyl ether bond of MurNAc 6-
phosphate, with the formation of an alpha,beta-unsaturated
aldehyde intermediate with (E)-stereochemistry, followed by the
syn addition of water to give product. {ECO:0000250}.
-!- SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L42023; AAC22413.1; -; Genomic_DNA.
PIR; I64090; I64090.
RefSeq; NP_438913.1; NC_000907.1.
RefSeq; WP_005693153.1; NC_000907.1.
PDB; 1NRI; X-ray; 1.90 A; A=1-303.
PDB; 4LZJ; X-ray; 2.40 A; A/B/C/D=1-303.
PDB; 4M0D; X-ray; 2.58 A; A/B/C/D=1-303.
PDBsum; 1NRI; -.
PDBsum; 4LZJ; -.
PDBsum; 4M0D; -.
ProteinModelPortal; P44862; -.
SMR; P44862; -.
STRING; 71421.HI0754; -.
EnsemblBacteria; AAC22413; AAC22413; HI_0754.
GeneID; 949804; -.
KEGG; hin:HI0754; -.
PATRIC; fig|71421.8.peg.792; -.
eggNOG; ENOG4105E15; Bacteria.
eggNOG; COG2103; LUCA.
KO; K07106; -.
OMA; CPPTFNT; -.
PhylomeDB; P44862; -.
BioCyc; HINF71421:G1GJ1-792-MONOMER; -.
UniPathway; UPA00342; -.
UniPathway; UPA00343; -.
UniPathway; UPA00544; -.
EvolutionaryTrace; P44862; -.
Proteomes; UP000000579; Chromosome.
GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:InterPro.
GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0097173; P:N-acetylmuramic acid catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
CDD; cd05007; SIS_Etherase; 1.
HAMAP; MF_00068; MurQ; 1.
InterPro; IPR005488; Etherase_MurQ.
InterPro; IPR005486; Glucokinase_regulatory_CS.
InterPro; IPR001347; SIS.
PANTHER; PTHR10088:SF5; PTHR10088:SF5; 1.
Pfam; PF01380; SIS; 1.
TIGRFAMs; TIGR00274; TIGR00274; 1.
PROSITE; PS01272; GCKR; 1.
PROSITE; PS51464; SIS; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Complete proteome; Lyase;
Reference proteome.
CHAIN 1 303 N-acetylmuramic acid 6-phosphate
etherase.
/FTId=PRO_0000214836.
DOMAIN 61 224 SIS.
ACT_SITE 89 89 Proton donor. {ECO:0000250}.
ACT_SITE 120 120 {ECO:0000250}.
HELIX 4 10 {ECO:0000244|PDB:4LZJ}.
HELIX 13 15 {ECO:0000244|PDB:1NRI}.
HELIX 19 21 {ECO:0000244|PDB:1NRI}.
HELIX 24 26 {ECO:0000244|PDB:1NRI}.
HELIX 29 40 {ECO:0000244|PDB:1NRI}.
HELIX 42 66 {ECO:0000244|PDB:1NRI}.
STRAND 71 76 {ECO:0000244|PDB:1NRI}.
HELIX 77 94 {ECO:0000244|PDB:1NRI}.
STRAND 100 105 {ECO:0000244|PDB:1NRI}.
HELIX 109 112 {ECO:0000244|PDB:1NRI}.
HELIX 119 121 {ECO:0000244|PDB:1NRI}.
HELIX 125 132 {ECO:0000244|PDB:1NRI}.
STRAND 139 144 {ECO:0000244|PDB:1NRI}.
HELIX 151 163 {ECO:0000244|PDB:1NRI}.
STRAND 166 173 {ECO:0000244|PDB:1NRI}.
HELIX 177 181 {ECO:0000244|PDB:1NRI}.
STRAND 182 187 {ECO:0000244|PDB:1NRI}.
TURN 199 201 {ECO:0000244|PDB:1NRI}.
HELIX 202 221 {ECO:0000244|PDB:1NRI}.
STRAND 224 226 {ECO:0000244|PDB:4LZJ}.
HELIX 238 251 {ECO:0000244|PDB:1NRI}.
HELIX 256 265 {ECO:0000244|PDB:4LZJ}.
TURN 266 268 {ECO:0000244|PDB:4LZJ}.
HELIX 270 279 {ECO:0000244|PDB:4LZJ}.
HELIX 283 292 {ECO:0000244|PDB:4LZJ}.
TURN 293 295 {ECO:0000244|PDB:4LZJ}.
HELIX 297 302 {ECO:0000244|PDB:4LZJ}.
SEQUENCE 303 AA; 32532 MW; 789297C871248BD6 CRC64;
MNDIILKSLS TLITEQRNPN SVDIDRQSTL EIVRLMNEED KLVPLAIESC LPQISLAVEQ
IVQAFQQGGR LIYIGAGTSG RLGVLDASEC PPTFGVSTEM VKGIIAGGEC AIRHPVEGAE
DNTKAVLNDL QSIHFSKNDV LVGIAASGRT PYVIAGLQYA KSLGALTISI ASNPKSEMAE
IADIAIETIV GPEILTGSSR LKSGTAQKMV LNMLTTASMI LLGKCYENLM VDVQASNEKL
KARAVRIVMQ ATDCNKTLAE QTLLEADQNA KLAIMMILST LSKSEAKVLL ERHQGKLRNA
LSK


Related products :

Catalog number Product name Quantity
10597-89-4 n-Acetylmuramic acid n-Acetylmuramic acid 1g
A178230 N-Acetyl-D-glucosaminyl-(1-4)-N-acetylmuramic Acid C19H32N2O13 CAS: 41137-10-4 1 mg
CSS-161 Biochemicals: Citrate_ Phosphate pH 4.4, 1 M 1M di-Potassium hydrogen Phosphate adjusted with Citric acid 100ml
CSS-161 Citrate_ Phosphate pH 4.4, 1 M 1M di_Potassium hydrogen Phosphate adjusted with Citric acid 100ml
CSS-341 Citrate_ Phosphate pH 5.0, 1 M 1M di_Potassium hydrogen Phosphate adjusted with Citric acid 100ml
CSS-341 Citrate_ Phosphate pH 5.0, 1 M 1M di_Potassium hydrogen Phosphate adjusted with Citric acid 100 ml
CSS-161 Citrate_ Phosphate pH 4.4, 1 M 1M di_Potassium hydrogen Phosphate adjusted with Citric acid 100 ml
EIAAB38426 Homo sapiens,Human,N-acetylneuraminate synthase,N-acetylneuraminate-9-phosphate synthase,N-acetylneuraminic acid phosphate synthase,N-acetylneuraminic acid synthase,NANS,SAS,Sialic acid synthase
orb61182 Etoposide 4'-Phosphate, Free Acid Etoposide 4'-Phosphate, Free Acid For research use only. 25 mg
EIAAB38151 Homo sapiens,hSPL,Human,KIAA1252,S1PL,SGPL1,Sphingosine-1-phosphate aldolase,Sphingosine-1-phosphate lyase 1,SPL 1,SP-lyase 1
EIAAB38150 Mouse,mSPL,Mus musculus,S1PL,Sgpl1,Sphingosine-1-phosphate aldolase,Sphingosine-1-phosphate lyase 1,SPL 1,SP-lyase 1
5116-94-9 Tridecyl acid phosphate Tridecyl acid phosphate 1g
EIAAB38152 Rat,Rattus norvegicus,S1PL,Sgpl1,Sphingosine-1-phosphate aldolase,Sphingosine-1-phosphate lyase 1,SPL,Spl,SPL 1,SP-lyase 1
31-341 AGPAT2 is a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. The protein is located within the endoplasmic reticulum membrane and converts lysophosphatidic acid to phosphatidic acid, 0.1 mg
EIAAB31452 1-acylglycerol-3-phosphate O-acyltransferase 5,1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon,1-AGP acyltransferase 5,1-AGPAT 5,AGPAT5,Homo sapiens,Human,LPAAT-epsilon,Lysophosphatidic acid ac
EIAAB31438 1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,AGPAT4,Bos taurus,Bovine,LPAAT-delta,Lysophosphatidic acid acyltra
EIAAB31417 1-acylglycerol-3-phosphate O-acyltransferase 1,1-acyl-sn-glycerol-3-phosphate acyltransferase alpha,1-AGP acyltransferase 1,1-AGPAT 1,AGPAT1,Bos taurus,Bovine,LPAAT-alpha,Lysophosphatidic acid acyltra
EIAAB31418 1-acylglycerol-3-phosphate O-acyltransferase 1,1-acyl-sn-glycerol-3-phosphate acyltransferase alpha,1-AGP acyltransferase 1,1-AGPAT 1,AGPAT1,G15,Homo sapiens,Human,LPAAT-alpha,Lysophosphatidic acid ac
EIAAB31451 1-acylglycerol-3-phosphate O-acyltransferase 5,1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon,1-AGP acyltransferase 5,1-AGPAT 5,Agpat5,D8Ertd319e,LPAAT-epsilon,Lysophosphatidic acid acyltransf
EIAAB31436 1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,AGPAT4,Homo sapiens,Human,LPAAT-delta,Lysophosphatidic acid acyltr
EIAAB31419 1-acylglycerol-3-phosphate O-acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta,1-AGP acyltransferase 2,1-AGPAT 2,AGPAT2,Homo sapiens,Human,LPAAT-beta,Lysophosphatidic acid acyltran
EIAAB31434 1-acylglycerol-3-phosphate O-acyltransferase 3,1-acyl-sn-glycerol-3-phosphate acyltransferase gamma,1-AGP acyltransferase 3,1-AGPAT 3,AGPAT3,Homo sapiens,Human,LPAAT-gamma,Lysophosphatidic acid acyltr
EIAAB31420 1-acylglycerol-3-phosphate O-acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta,1-AGP acyltransferase 2,1-AGPAT 2,Agpat2,LPAAT-beta,Lysophosphatidic acid acyltransferase beta,Mouse,
EIAAB31435 1-acylglycerol-3-phosphate O-acyltransferase 3,1-acyl-sn-glycerol-3-phosphate acyltransferase gamma,1-AGP acyltransferase 3,1-AGPAT 3,Agpat3,LPAAT-gamma,Lysophosphatidic acid acyltransferase gamma,Mou
EIAAB31439 1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,Agpat4,LPAAT-delta,Lysophosphatidic acid acyltransferase delta,Rat


 

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