Sequence of CUTC_OLEA2
EC Number:4.3.99.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
choline trimethylamine-lyase
Q30W70
Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
846
94640
Reaction
choline = trimethylamine + acetaldehyde
Other sequences found for EC No. 4.3.99.4
General information:
Sequence
0 MDLQDFSHKL AEATKNLTPA ERASLKKIFE GVSAEVFSQP APVSAVATGA ESGIPDGPTP
60 RHVKLKENFL KQVPSITVQR AVAITKIAKE NPGLPKPLLR AKTFRYCCET APLVIQDHEL
120 IVGSPNGAPR AGAFSPEVAW RWLQDELDTI GSRPQDPFYI SEEDKKVLRE EVFPFWQNKS
180 VDEFCEGQYR EADLWEMSGE SFVSDCSYHA VNGGGDSNPG YDVILMKKGM LDIQREAREK
240 LEQLDYANPE DIDKIYFYKS VIETAEGVMI YARRLSAYAA ELAARETDPR RKAELQKISE
300 VNARVPAHAP SNFWEAIQAV WTVESLLVVE ENQTGMSIGR VDQYMYPFYR ADIDSGRLTE
360 YEAFDLAGCM LVKMSEMMWI TSEGASKFFA GYQPFVNMCV GGVTREGHDA TNDLTYMLMD
420 AVRHVRIYQP TLATRVHNKS PQKYLKKIVD VIRSGMGFPA VHFDDAHIKM MLAKGVSIED
480 ARDYCLMGCV EPQKSGRLYQ WTSTGYTQWP ICIELVLNHG VPLWYGKKVT PDMGDLSQYD
540 TYEKFEAAVK EQIRWITKNT SVATVISQRA HRELAPKPLM SLMYEGCMES GRDVSAGGAM
600 YNFGPGVVWS GLATYVDSMA AIKKLVYDDR KYTLAQLNEA LKADFAGYDQ ILADCLAAPK
660 YGNDDDYADM IAADLVHFTE TEHRKYKTLY SVLSHGTLSI SNNTPFGQLL GASANGRRAW
720 MPLSDGISPT QGADYKGPTA IIKSVSKMAN DNMNIGMVHN FKLMSGLLDT PEGENGLITL
780 IRTACMLGNG EMQFNYLDNE LLLDAQKHPE KYRDLVVRVA GYSAFFVELC KDVQDEIISR
840 TMLHGF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
786194
Hauser L.J.,Land M.L.,Brown S.D.,Larimer F.,Keller K.L.,Rapp-Giles B.J.,Price M.N.,Lin M.,Bruce D.C.,Detter J.C.,Tapia R.,Han C.S.,Goodwin L.A.,Cheng J.F.,Pitluck S.,Copeland A.,Lucas S.,Nolan M.,Lapidus A.L.,Palumbo A.V.,Wall J.D.
Complete genome sequence and updated annotation of Desulfovibrio alaskensis G20.
J. Bacteriol.
193
4268-4269
2011
786195
Craciun S.,Balskus E.P.
Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme.
Proc. Natl. Acad. Sci. U.S.A.
109
21307-21312
2012
786196
Craciun S.,Marks J.A.,Balskus E.P.
Characterization of choline trimethylamine-lyase expands the chemistry of glycyl radical enzymes.
ACS Chem. Biol.
9
1408-1413
2014
