Sequence of ALADH_ARCFU
EC Number:1.4.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
alanine dehydrogenase
O28608
Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
322
34829
Reaction
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
Other sequences found for EC No. 1.4.1.1
General information:
Sequence
0 METLILTQEE VESLISMDEA MNAVEEAFRL YALGKAQMPP KVYLEFEKGD LRAMPAHLMG
60 YAGLKWVNSH PGNPDKGLPT VMALMILNSP ETGFPLAVMD ATYTTSLRTG AAGGIAAKYL
120 ARKNSSVFGF IGCGTQAYFQ LEALRRVFDI GEVKAYDVRE KAAKKFVSYC EDRGISASVQ
180 PAEEASRCDV LVTTTPSRKP VVKAEWVEEG THINAIGADG PGKQELDVEI LKKAKIVVDD
240 LEQAKHGGEI NVAVSKGVIG VEDVHATIGE VIAGLKDGRE SDEEITIFDS TGLAIQDVAV
300 AKVVYENALS KNVGSKIKFF RI
Download this sequence
Download all sequences for 1.4.1.1
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
896700
Klenk H.-P.,Clayton R.A.,Tomb J.-F.,White O.,Nelson K.E.,Ketchum K.A.,Dodson R.J.,Gwinn M.L.,Hickey E.K.,Peterson J.D.,Richardson D.L.,Kerlavage A.R.,Graham D.E.,Kyrpides N.C.,Fleischmann R.D.,Quackenbush J.,Lee N.H.,Sutton G.G.,Gill S.R.,Kirkness E.F.,Dougherty B.A.,McKenney K.,Adams M.D.,Loftus B.J.,Peterson S.N.,Reich C.I.,McNeil L.K.,Badger J.H.,Glodek A.,Zhou L.,Overbeek R.,Gocayne J.D.,Weidman J.F.,McDonald L.A.,Utterback T.R.,Cotton M.D.,Spriggs T.,Artiach P.,Kaine B.P.,Sykes S.M.,Sadow P.W.,D'Andrea K.P.,Bowman C.,Fujii C.,Garland S.A.,Mason T.M.,Olsen G.J.,Fraser C.M.,Smith H.O.,Woese C.R.,Venter J.C.
The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.
Nature
390
364-370
1997
896701
Schroder I.,Vadas A.,Johnson E.,Lim S.,Monbouquette H.G.
A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin.
J. Bacteriol.
186
7680-7689
2004
896702
Gallagher D.T.,Monbouquette H.G.,Schroder I.,Robinson H.,Holden M.J.,Smith N.N.
Structure of alanine dehydrogenase from Archaeoglobus: active site analysis and relation to bacterial cyclodeaminases and mammalian mu crystallin.
J. Mol. Biol.
342
119-130
2004