Sequence of GLMU_HAEIN
EC Number:2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 2
EC Number:2.3.1.157
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
glucosamine-1-phosphate N-acetyltransferase
P43889
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
456
49287
Reaction
acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Other sequences found for EC No. 2.3.1.157
EC Number:2.7.7.23
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
UDP-N-acetylglucosamine diphosphorylase
P43889
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
456
49287
Reaction
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Other sequences found for EC No. 2.7.7.23
General information:
Sequence
0 MTKKALSAVI LAAGKGTRMY SDLPKVLHTI AGKPMVKHVI DTAHQLGSEN IHLIYGHGGD
60 LMRTHLANEQ VNWVLQTEQL GTAHAVQQAA PFFKDNENIV VLYGDAPLIT KETLEKLIEA
120 KPENGIALLT VNLDNPTGYG RIIRENGNVV AIVEQKDANA EQLNIKEVNT GVMVSDGASF
180 KKWLARVGNN NAQGEYYLTD LIALANQDNC QVVAVQATDV MEVEGANNRL QLAALERYFQ
240 NKQASKLLLE GVMIYDPARF DLRGTLEHGK DVEIDVNVII EGNVKLGDRV KIGTGCVLKN
300 VVIGNDVEIK PYSVLEDSIV GEKAAIGPFS RLRPGAELAA ETHVGNFVEI KKSTVGKGSK
360 VNHLTYVGDS EIGSNCNIGA GVITCNYDGA NKFKTIIGDD VFVGSDTQLV APVKVANGAT
420 IGAGTTITRD VGENELVITR VAQRHIQGWQ RPIKKK
Download this sequence
Download all sequences for 2.7.7.23
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1063239
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
1063240
Mochalkin I.,Lightle S.,Zhu Y.,Ohren J.F.,Spessard C.,Chirgadze N.Y.,Banotai C.,Melnick M.,McDowell L.
Characterization of substrate binding and catalysis in the potential antibacterial target N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
Protein Sci.
16
2657-2666
2007
1063241
Mochalkin I.,Lightle S.,Narasimhan L.,Bornemeier D.,Melnick M.,Vanderroest S.,McDowell L.
Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site.
Protein Sci.
17
577-582
2008
1063243
Larsen N.A.,Nash T.J.,Morningstar M.,Shapiro A.B.,Joubran C.,Blackett C.J.,Patten A.D.,Boriack-Sjodin P.A.,Doig P.
An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.
Biochem. J.
446
405-413
2012
1063244
Doig P.,Boriack-Sjodin P.A.,Dumas J.,Hu J.,Itoh K.,Johnson K.,Kazmirski S.,Kinoshita T.,Kuroda S.,Sato T.O.,Sugimoto K.,Tohyama K.,Aoi H.,Wakamatsu K.,Wang H.
Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping.
Bioorg. Med. Chem.
22
6256-6269
2014