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: 14590199
Created: 7-Oct-2014
Updated: 23-Jan-2015
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:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3BIC_A       603 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGVSTLAAGHKTLVPELIKELNSL 682
gi 581476    596 RRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKL 675
gi 317373575 613 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSL 692
gi 446239380 356 RRPRILIAKMGQDGHDRGAKVIASAYSDLGFDVDLSPMFSTPEEIARLAVENDVHVVGASSLAAGHKTLIPELVEALKKW 435
gi 499182168  10 RKIRVIVAKPGLDGHDRGAKVVARALRDAGFEVIYTGIRRTPEEIAETALQEDADVVGLSILSGAHLELTPMVIEELRKR 89
gi 499186832   8 SKVRVLVAKPGLDGHDRGAKVVARALRDAGYEVIYTGIRQTPEQIVEAVIEEDVDVLGISILSGAHMVLIPKILKLLEEK 87
gi 2829565   615 RRPRILIAKMGQDGHDRGQKVIATAFADIGFDVDVGSLFSTPEEVARQAADNDVHVIGVSSLAAGHLTLVPALRDALAQV 694
1REQ_A       595 RRPRILLAKMGQDGHDRGQKVIATAYADLGFDVDVGPLFQTPEETARQAVEADVHVVGVSSLAGGHLTLVPALRKELDKL 674
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
3BIC_A       683 GR---P---DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 734
gi 581476    676 GR---P---DILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLD 727
gi 317373575 693 GR---P---DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
gi 446239380 436 GR---E---DICVVAGGVIPPQDYAFLQERGVAAIYGPGTPMLDSVRDVLNLISQHHD 487
gi 499182168  90 GL---EpnrDVLVIVGGIVPEEDVPKLKEMGVAKVFGPGTPLNEIIDFIRAEVPKLKR 144
gi 499186832  88 GIkvnE---DVLVVAGGIIPPDDAEELKKMGVAEVFGPGTPLREIIEFIDKNVGKLKK 142
gi 2829565   695 GR---P---DIMIVVGGVIPPGDFDELYAAGATAIFPPGTVIADAAIDLLHRLAERLG 746
1REQ_A       675 GR---P---DILITVGGVIPEQDFDELRKDGAVEIYTPGTVIPESAISLVKKLRASLD 726
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