Any feedback?
Please rate this page
(sequences.php)
(0/150)

BRENDA support

Sequence of ALGC_PSEAE

EC Number:5.4.2.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)
P26276
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
463
50296
Reaction
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
Other sequences found for EC No. 5.4.2.2

General information:

Sequence
show sequence in fasta format
  0 MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC VAVGRDGRLS
 60 GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK SGVMLTGSHN PPDYNGFKIV
120 VAGETLANEQ IQALRERIEK NDLASGVGSV EQVDILPRYF KQIRDDIAMA KPMKVVVDCG
180 NGVAGVIAPQ LIEALGCSVI PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA
240 FDGDGDRVGV VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR
300 PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL EILSQDQRDS
360 EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE GNITTLDGVR VDYPKGWGLV
420 RASNTTPVLV LRFEADTEEE LERIKTVFRN QLKAVDSSLP VPF
Download this sequence
in fasta format
Download all sequences for 5.4.2.2
in fasta format
in csv (Excel, OpenOffice) format
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
3897
Zielinski N.A.,Chakrabarty A.M.,Berry A.
Characterization and regulation of the Pseudomonas aeruginosa algC gene encoding phosphomannomutase.
J. Biol. Chem.
266
9754-9763
1991
3898
Stover C.K.,Pham X.-Q.T.,Erwin A.L.,Mizoguchi S.D.,Warrener P.,Hickey M.J.,Brinkman F.S.L.,Hufnagle W.O.,Kowalik D.J.,Lagrou M.,Garber R.L.,Goltry L.,Tolentino E.,Westbrock-Wadman S.,Yuan Y.,Brody L.L.,Coulter S.N.,Folger K.R.,Kas A.,Larbig K.,Lim R.M.,Smith K.A.,Spencer D.H.,Wong G.K.-S.,Wu Z.,Paulsen I.T.,Reizer J.,Saier M.H. Jr.,Hancock R.E.W.,Lory S.,Olson M.V.
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.
Nature
406
959-964
2000
3899
Coyne M.J. Jr.,Russell K.S.,Coyle C.L.,Goldberg J.B.
The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core.
J. Bacteriol.
176
3500-3507
1994
3900
Ye R.W.,Zielinski N.A.,Chakrabarty A.M.
Purification and characterization of phosphomannomutase/phosphoglucomutase from Pseudomonas aeruginosa involved in biosynthesis of both alginate and lipopolysaccharide.
J. Bacteriol.
176
4851-4857
1994
3901
Olvera C.,Goldberg J.B.,Sanchez R.,Soberon-Chavez G.
The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis.
FEMS Microbiol. Lett.
179
85-90
1999
3902
Naught L.E.,Tipton P.A.
Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
Arch. Biochem. Biophys.
396
111-118
2001
3903
Regni C.,Tipton P.A.,Beamer L.J.
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
Structure
10
269-279
2002
3904
Regni C.,Naught L.,Tipton P.A.,Beamer L.J.
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
Structure
12
55-63
2004
3905
Regni C.,Shackelford G.S.,Beamer L.J.
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Acta Crystallogr. F
62
722-726
2006
3906
Regni C.,Schramm A.M.,Beamer L.J.
The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.
J. Biol. Chem.
281
15564-15571
2006
3907
Schramm A.M.,Mehra-Chaudhary R.,Furdui C.M.,Beamer L.J.
Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa.
Biochemistry
47
9154-9162
2008
3908
Sarma A.V.,Anbanandam A.,Kelm A.,Mehra-Chaudhary R.,Wei Y.,Qin P.,Lee Y.,Berjanskii M.V.,Mick J.A.,Beamer L.J.,Van Doren S.R.
Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.
Biochemistry
51
807-819
2012
3909
Lee Y.,Mehra-Chaudhary R.,Furdui C.,Beamer L.J.
Identification of an essential active-site residue in the alpha-D-phosphohexomutase enzyme superfamily.
FEBS J.
280
2622-2632
2013
3910
Lee Y.,Villar M.T.,Artigues A.,Beamer L.J.
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase.
J. Biol. Chem.
289
4674-4682
2014