3BIC,1REQ


Conserved Protein Domain Family
acid_CoA_mut_C

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TIGR00640: acid_CoA_mut_C 
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methylmalonyl-CoA mutase C-terminal domain
Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a reversible isomerization between L-methylmalonyl-CoA and succinyl-CoA. The enzyme uses an adenosylcobalamin cofactor. It may be a homodimer, as in mitochondrion, or a heterodimer with partially homologous beta chain that does not bind the adenosylcobalamin cofactor, as in Propionibacterium freudenreichii. The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. This model describes the C-terminal domain subfamily. In a neighbor-joining tree (methylaspartate mutase S chain as the outgroup), AF2219 branches with a coenzyme B12-dependent enzyme known not to be 5.4.99.2.
Statistics
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PSSM-Id: 129726
View PSSM: TIGR00640
Aligned: 8 rows
Threshold Bit Score: 203.028
Threshold Setting Gi: 499186832
Created: 7-Oct-2014
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
3BIC_A       603 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLAAGHKTLVPELIKELNSL 682 human
CAA33090     596 RRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKL 675 Propionibacteri...
P22033       613 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSL 692 human
WP_000317235 356 RRPRILIAKMGQDGHDRGAKVIASAYSDLGFDVDLSPMFSTPEEIARLAVENDVHVVGASSLAAGHKTLIPELVEALKKW 435 Escherichia coli
WP_010879708  10 RKIRVIVAKPGLDGHDRGAKVVARALRDAGFEVIYTGIRRTPEEIAETALQEDADVVGLSILSGAHLELTPMVIEELRKR 89  Archaeoglobus f...
WP_010884372   8 SKVRVLVAKPGLDGHDRGAKVVARALRDAGYEVIYTGIRQTPEQIVEAVIEEDVDVLGISILSGAHMVLIPKILKLLEEK 87  Pyrococcus hori...
P71774       615 RRPRILIAKMGQDGHDRGQKVIATAFADIGFDVDVGSLFSTPEEVARQAADNDVHVIGVSSLAAGHLTLVPALRDALAQV 694 Mycobacterium t...
1REQ_A       595 RRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKL 674 Propionibacteri...
3BIC_A       683 GR---P---DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 734 human
CAA33090     676 GR---P---DILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLD 727 Propionibacterium freudenreichii subs...
P22033       693 GR---P---DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744 human
WP_000317235 436 GR---E---DICVVAGGVIPPQDYAFLQERGVAAIYGPGTPMLDSVRDVLNLISQHHD 487 Escherichia coli
WP_010879708  90 GL---EpnrDVLVIVGGIVPEEDVPKLKEMGVAKVFGPGTPLNEIIDFIRAEVPKLKR 144 Archaeoglobus fulgidus
WP_010884372  88 GIkvnE---DVLVVAGGIIPPDDAEELKKMGVAEVFGPGTPLREIIEFIDKNVGKLKK 142 Pyrococcus horikoshii
P71774       695 GR---P---DIMIVVGGVIPPGDFDELYAAGATAIFPPGTVIADAAIDLLHRLAERLG 746 Mycobacterium tuberculosis
1REQ_A       675 GR---P---DILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLD 726 Propionibacterium freudenreichii subs...
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