Sequence of GLCDH_HALMT
EC Number:1.1.1.47
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
glucose 1-dehydrogenase [NAD(P)+]
Q977U7
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
357
39242
Reaction
D-glucose + NAD(P)+ = D-glucono-1,5-lactone + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.47
EC Number:1.1.1.113
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-xylose 1-dehydrogenase
Q977U7
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
357
39242
Reaction
L-xylose + NADP+ = L-xylono-1,4-lactone + NADPH + H+
Other sequences found for EC No. 1.1.1.113
EC Number:1.1.1.119
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
glucose 1-dehydrogenase (NADP+)
Q977U7
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
357
39242
Reaction
D-glucose + NADP+ = D-glucono-1,5-lactone + NADPH + H+
Other sequences found for EC No. 1.1.1.119
EC Number:1.1.1.175
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
D-xylose 1-dehydrogenase
Q977U7
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
357
39242
Reaction
D-xylose + NAD+ = D-xylonolactone + NADH + H+
Other sequences found for EC No. 1.1.1.175
General information:
Sequence
0 MKAIAVKRGE DRPVVIEKPR PEPESGEALV RTLRVGVDGT DHEVIAGGHG GFPEGEDHLV
60 LGHEAVGVVV DPNDTELEEG DIVVPTVRRP PASGTNEYFE RDQPDMAPDG MYFERGIVGA
120 HGYMSEFFTS PEKYLVRIPR SQAELGFLIE PISITEKALE HAYASRSAFD WDPSSAFVLG
180 NGSLGLLTLA MLKVDDKGYE NLYCLGRRDR PDPTIDIIEE LDATYVDSRQ TPVEDVPDVY
240 EQMDFIYEAT GFPKHAIQSV QALAPNGVGA LLGVPSDWAF EVDAGAFHRE MVLHNKALVG
300 SVNSHVEHFE AATVTFTKLP KWFLEDLVTG VHPLSEFEAA FDDDDTTIKT AIEFSTV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
932394
Pire C.,Esclapez J.,Ferrer J.,Bonete M.J.
Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family.
FEMS Microbiol. Lett.
200
221-227
2001
932395
Han J.,Zhang F.,Hou J.,Liu X.,Li M.,Liu H.,Cai L.,Zhang B.,Chen Y.,Zhou J.,Hu S.,Xiang H.
Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer.
J. Bacteriol.
194
4463-4464
2012
932396
Bonete M.J.,Pire C.,Llorca F.I.,Camacho M.L.
Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence.
FEBS Lett.
383
227-229
1996
932398
Ferrer J.,Fisher M.,Burke J.,Sedelnikova S.E.,Baker P.J.,Gilmour D.J.,Bonete M.J.,Pire C.,Esclapez J.,Rice D.W.
Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Haloferax mediterranei.
Acta Crystallogr. D
57
1887-1889
2001
932399
Esclapez J.,Britton K.L.,Baker P.J.,Fisher M.,Pire C.,Ferrer J.,Bonete M.J.,Rice D.W.
Crystallization and preliminary X-ray analysis of binary and ternary complexes of Haloferax mediterranei glucose dehydrogenase.
Acta Crystallogr. F
61
743-746
2005
932400
Esclapez J.,Pire C.,Bautista V.,Martinez-Espinosa R.M.,Ferrer J.,Bonete M.J.
Analysis of acidic surface of Haloferax mediterranei glucose dehydrogenase by site-directed mutagenesis.
FEBS Lett.
581
837-842
2007
932401
Britton K.L.,Baker P.J.,Fisher M.,Ruzheinikov S.,Gilmour D.J.,Bonete M.J.,Ferrer J.,Pire C.,Esclapez J.,Rice D.W.
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei.
Proc. Natl. Acad. Sci. U.S.A.
103
4846-4851
2006
932402
Baker P.J.,Britton K.L.,Fisher M.,Esclapez J.,Pire C.,Bonete M.J.,Ferrer J.,Rice D.W.
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.
Proc. Natl. Acad. Sci. U.S.A.
106
779-784
2009
