Sequence of MUTA_PROFR
EC Number:5.4.99.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(R)-methylmalonyl-CoA = succinyl-CoA
Other sequences found for EC No. 5.4.99.2
General information:
Sequence
0 MSSTDQGTNP ADTDDLTPTT LSLAGDFPKA TEEQWEREVE KVLNRGRPPE KQLTFAECLK
60 RLTVHTVDGI DIVPMYRPKD APKKLGYPGV APFTRGTTVR NGDMDAWDVR ALHEDPDEKF
120 TRKAILEGLE RGVTSLLLRV DPDAIAPEHL DEVLSDVLLE MTKVEVFSRY DQGAAAEALV
180 SVYERSDKPA KDLALNLGLD PIAFAALQGT EPDLTVLGDW VRRLAKFSPD SRAVTIDANI
240 YHNAGAGDVA ELAWALATGA EYVRALVEQG FTATEAFDTI NFRVTATHDQ FLTIARLRAL
300 REAWARIGEV FGVDEDKRGA RQNAITSWRD VTREDPYVNI LRGSIATFSA SVGGAESITT
360 LPFTQALGLP EDDFPLRIAR NTGIVLAEEV NIGRVNDPAG GSYYVESLTR SLADAAWKEF
420 QEVEKLGGMS KAVMTEHVTK VLDACNAERA KRLANRKQPI TAVSEFPMIG ARSIETKPFP
480 AAPARKGLAW HRDSEVFEQL MDRSTSVSER PKVFLACLGT RRDFGGREGF SSPVWHIAGI
540 DTPQVEGGTT AEIVEAFKKS GAQVADLCSS AKVYAQQGLE VAKALKAAGA KALYLSGAFK
600 EFGDDAAEAE KLIDGRLFMG MDVVDTLSST LDILGVAK
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
192205
Marsh E.N.,McKie N.,Davis N.K.,Leadlay P.F.
Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii.
Biochem. J.
260
345-352
1989
192206
Marsh E.N.,Leadlay P.F.
Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues.
Biochem. J.
260
339-343
1989
192207
Mancia F.,Keep N.H.,Nakagawa A.,Leadlay P.F.,McSweeney S.,Rasmussen B.,Bosecke P.,Diat O.,Evans P.R.
How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2-A resolution.
Structure
4
339-350
1996
192208
Mancia F.,Evans P.R.
Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism.
Structure
6
711-720
1998
