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Sequence of MUTB_PROFR

EC Number:5.4.99.2

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
methylmalonyl-CoA mutase
P11653
Propionibacterium freudenreichii subsp. shermanii
728
80178
Reaction
(R)-methylmalonyl-CoA = succinyl-CoA
Other sequences found for EC No. 5.4.99.2

General information:

Sequence
show sequence in fasta format
  0 MSTLPRFDSV DLGNAPVPAD AARRFEELAA KAGTGEAWET AEQIPVGTLF NEDVYKDMDW
 60 LDTYAGIPPF VHGPYATMYA FRPWTIRQYA GFSTAKESNA FYRRNLAAGQ KGLSVAFDLP
120 THRGYDSDNP RVAGDVGMAG VAIDSIYDMR ELFAGIPLDQ MSVSMTMNGA VLPILALYVV
180 TAEEQGVKPE QLAGTIQNDI LKEFMVRNTY IYPPQPSMRI ISEIFAYTSA NMPKWNSISI
240 SGYHMQEAGA TADIEMAYTL ADGVDYIRAG ESVGLNVDQF APRLSFFWGI GMNFFMEVAK
300 LRAARMLWAK LVHQFGPKNP KSMSLRTHSQ TSGWSLTAQD VYNNVVRTCI EAMAATQGHT
360 QSLHTNSLDE AIALPTDFSA RIARNTQLFL QQESGTTRVI DPWSGSAYVE ELTWDLARKA
420 WGHIQEVEKV GGMAKAIEKG IPKMRIEEAA ARTQARIDSG RQPLIGVNKY RLEHEPPLDV
480 LKVDNSTVLA EQKAKLVKLR AERDPEKVKA ALDKITWAAG NPDDKDPDRN LLKLCIDAGR
540 AMATVGEMSD ALEKVFGRYT AQIRTISGVY SKEVKNTPEV EEARELVEEF EQAEGRRPRI
600 LLAKMGQDGH DRGQKVIATA YADLGFDVDV GPLFQTPEET ARQAVEADVH VVGVSSLAGG
660 HLTLVPALRK ELDKLGRPDI LITVGGVIPE QDFDELRKDG AVEIYTPGTV IPESAISLVK
720 KLRASLDA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
192217
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
192218
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
192219
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
192220
Thoma N.H.,Meier T.W.,Evans P.R.,Leadlay P.F.
Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase.
Biochemistry
37
14386-14393
1998
192221
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
192222
Mancia F.,Smith G.A.,Evans P.R.
Crystal structure of substrate complexes of methylmalonyl-CoA mutase.
Biochemistry
38
7999-8005
1999