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Conserved domains on  [gi|530382073|ref|XP_005249200.1|]
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PREDICTED: methylmalonyl-CoA mutase, mitochondrial isoform X1 [Homo sapiens]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MM_CoA_mutase_alpha_like cd03679
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like ...
40-574 0e+00

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like subfamily; contains proteins similar to the alpha subunit of Propionbacterium shermanni MCM, as well as human and E. coli MCM. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. Sinorhizobium meliloti strain SU47 MCM plays a role in the polyhydroxyalkanoate degradation pathway. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism.


:

Pssm-ID: 239651  Cd Length: 536  Bit Score: 1182.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  40 HPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRD--TMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVE 117
Cdd:cd03679    1 LPEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADDldDMEHLDTLPGIPPFVRGPYATMYTFRPWTIRQYAGFSTAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 118 ESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLA 197
Cdd:cd03679   81 ESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPILA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 198 NFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILEL 277
Cdd:cd03679  161 FYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSKNMPKFNSISISGYHMQEAGATADLEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 278 AYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKmFQPKNSKSLLLRAHCQTSGWS 357
Cdd:cd03679  241 AYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFMEIAKLRAARLLWAKLVKQ-FGPKNPKSLALRTHSQTSGWS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 358 LTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTND 437
Cdd:cd03679  320 LTEQDPYNNVVRTCIEAMAAVFGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 438 VYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEK 517
Cdd:cd03679  400 LAEKAWALIQEIEELGGMAKAIESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIAR 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073 518 LKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFG 574
Cdd:cd03679  480 LKKLRAERDPEAVQAALDALTEAAETGEGNLLALAVDAARARATVGEISDALEKVFG 536
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
613-744 3.10e-78

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.


:

Pssm-ID: 129726  Cd Length: 132  Bit Score: 249.25  E-value: 3.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  613 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSL 692
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382073  693 GRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD 132
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
41-744 0e+00

methylmalonyl-CoA mutase; Reviewed


:

Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1397.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  41 PEWAALA---KKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEE--LPGVKPFTRGPYPTMYTFRPWTIRQYAGFST 115
Cdd:PRK09426   5 PDFADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLEGLEHLdtLPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 116 VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV 195
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 196 LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL 275
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 276 ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIeKMFQPKNSKSLLLRAHCQTSG 355
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIV-KQFGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 356 WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT 435
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 436 NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQI 515
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 516 EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK 595
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARSGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 596 EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLA 675
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382073 676 AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLG 712
 
Name Accession Description Interval E-value
MM_CoA_mutase_alpha_like cd03679
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like ...
40-574 0e+00

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like subfamily; contains proteins similar to the alpha subunit of Propionbacterium shermanni MCM, as well as human and E. coli MCM. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. Sinorhizobium meliloti strain SU47 MCM plays a role in the polyhydroxyalkanoate degradation pathway. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism.


Pssm-ID: 239651  Cd Length: 536  Bit Score: 1182.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  40 HPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRD--TMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVE 117
Cdd:cd03679    1 LPEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADDldDMEHLDTLPGIPPFVRGPYATMYTFRPWTIRQYAGFSTAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 118 ESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLA 197
Cdd:cd03679   81 ESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPILA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 198 NFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILEL 277
Cdd:cd03679  161 FYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSKNMPKFNSISISGYHMQEAGATADLEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 278 AYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKmFQPKNSKSLLLRAHCQTSGWS 357
Cdd:cd03679  241 AYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFMEIAKLRAARLLWAKLVKQ-FGPKNPKSLALRTHSQTSGWS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 358 LTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTND 437
Cdd:cd03679  320 LTEQDPYNNVVRTCIEAMAAVFGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 438 VYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEK 517
Cdd:cd03679  400 LAEKAWALIQEIEELGGMAKAIESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIAR 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073 518 LKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFG 574
Cdd:cd03679  480 LKKLRAERDPEAVQAALDALTEAAETGEGNLLALAVDAARARATVGEISDALEKVFG 536
acid_CoA_mut_N TIGR00641
methylmalonyl-CoA mutase N-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
61-582 0e+00

methylmalonyl-CoA mutase N-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 abd 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 N-terminal domain subfamily. In a neighbor-joining tree, AF2215 branches with a bacterial isobutyryl-CoA mutase, which is also the same length. Scoring between the noise and trusted cutoffs are the non-catalytic, partially homologous beta chains from certain heterodimeric examples of 5.4.99.2.


Pssm-ID: 273190  Cd Length: 526  Bit Score: 1013.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   61 WHTPEGISIKPLYS----KRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSV 136
Cdd:TIGR00641   1 WHTAEGIPVKPLYTpalaDWDYMEKLGTFPGEPPFTRGPYATMYRFRPWTIRQYAGFSTAEESNKFYRRNLAAGQKGLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  137 AFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGT 216
Cdd:TIGR00641  81 AFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIEDMRILFDGIPLDKVSVSMTMNGAVLPILALYVVVAEEQGVPPEKLTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  217 IQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGL 296
Cdd:TIGR00641 161 IQNDILKEFMVRNTYIFPPEPSMRIIADIIAYTAKNMPKWNSISISGYHMQEAGATAVQELAFTLADGIEYIRAGLSAGL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  297 TIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMA 376
Cdd:TIGR00641 241 DVDSFAPRLSFFFGIGMNFFMEIAKLRAARRLWAKLVKEWFGAKNPKSMSLRTHCQTSGWSLTAQDPYNNIVRTAIEALA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  377 AVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMA 456
Cdd:TIGR00641 321 AVLGGTQSLHTNSFDEALGLPTDFSARIARNTQQIIQEESGVTRVIDPLGGSYYVEWLTDDIYERAWKYIQEIEEMGGMA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  457 KAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAA 536
Cdd:TIGR00641 401 KAIERGIPKLRIEEAAARTQARIDSGRQVIVGVNKYQLEEEDEVEVLKVDNSSVREEQIAKLKKLRAERDQEKVEAALDA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 530382073  537 LTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRM 582
Cdd:TIGR00641 481 LTKAAEKEDENLLALAIDAARARATLGEITDALEKVFGEYRAPIRT 526
MM_CoA_mutase pfam01642
Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of ...
63-573 0e+00

Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of enzymes that uses coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the formation of an adenosyl radical from the cofactor. This radical then initiates a free-radical rearrangement of its substrate, succinyl-CoA, to methylmalonyl-CoA.


Pssm-ID: 279913  Cd Length: 511  Bit Score: 925.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   63 TPEGISIKPLYSKRDTM--DLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDL 140
Cdd:pfam01642   1 TYEGIPVKPLYTPEDIAeeDLGDSLPGEFPFTRGVYPTMYRGRPWTIRQYAGFGTAEETNARYRYLLAAGQTGLSVAFDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  141 ATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQND 220
Cdd:pfam01642  81 PTQRGYDSDHPRAEGEVGKAGVAIDSLEDMETLFDGIPLDKVSVSMTINAPALPLLAMYIAAAEEQGVDLEKLRGTIQND 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  221 ILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDE 300
Cdd:pfam01642 161 ILKEYIARGTYIYPPEPSMRIIADIIEYAAKNMPKFNTISISGYHIREAGATAVQELAFTLADGIEYLRALLEAGLDVDE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  301 FAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFG 380
Cdd:pfam01642 241 FAPRLSFFFAIGMNFFEEIAKFRAARRLWARIVKERFGAKNPRSLKLRFHAQTSGWSLTAQDPYNNILRTTTEAMAAVLG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  381 GTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVA 460
Cdd:pfam01642 321 GTQSLHTNPFDEALALPTEFSARIARNTQLILQEESGVTKVVDPLGGSYYVESLTDEIAEKAWALFQEIEELGGMLAAIE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  461 EGIPKLRIEECAARRQARIDSGSEVIVGVNKYQL-EKEDAVEVLAIDNTsVRNRQIEKLKKIKSSRDQALAERCLAALTE 539
Cdd:pfam01642 401 SGYPQREIAESAARRQKAIASGKEVIVGVNKYRPnETEKPLEILRVDPA-VRERQAARLEALRAERDGARVKAALAALGN 479
                         490       500       510
                  ....*....|....*....|....*....|....
gi 530382073  540 CAASgdGNILALAVDASRARCTVGEITDALKKVF 573
Cdd:pfam01642 480 AARG--GNLLARAIFAARAGATLGEISDALREVF 511
Sbm COG1884
Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];
42-579 0e+00

Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];


Pssm-ID: 224796  Cd Length: 548  Bit Score: 828.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  42 EWAALAKKQLKGKNPED--LIWHTPEGISIKPLYSKRDTMDLPEE----LPGVKPFTRGPYPTMYTFRPWTIRQYAGFST 115
Cdd:COG1884    4 EWEEKTLKPWLEKPGERkkLFKTTSEGIDVKPLYTPEDVARWDYLeklgVPGEYPFTRGVYPTMYRGRLWTMRQYAGFGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 116 VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV 195
Cdd:COG1884   84 AEETNRRYRYLLAAGQTGLSVAFDLPTLRGYDSDHPRAEGEVGKAGVAIDTLKDMEILFDGIPLDKVSTSMTINGPAPPL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 196 LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL 275
Cdd:COG1884  164 LAMYLAVAEEQGVDREKLRGTIQNDILKEYIARNTYIYPPEPSMRIIVDIIEYCAKEVPKFNSISISGYHIREAGATAVQ 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 276 ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSG 355
Cdd:COG1884  244 ELAFTLADGVEYVRALLERGLDVDEFAPRLSFFFAAGNDFFEEVAKLRAARRLWARIMKEEFGAKNPRSMMLRFHTQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 356 WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT 435
Cdd:COG1884  324 WSLTAQDPENNILRTTIQALAAVLGGTQSLHTNSFDEALALPTEFSARIARNTQLILAEESGVADVVDPLGGSYYVEWLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 436 NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKY-QLEKEDAVEVLAIDNTSVRNRQ 514
Cdd:COG1884  404 DELEEAAWAYIEEIEAMGGMLKAIEDGYPQREIAESAARRQARIEEGERVIVGVNEYpEEGPEEPVEILKVDPEAVRERQ 483
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382073 515 IEKLKKIKSSRDQALAERCLAALTEcAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKAN 579
Cdd:COG1884  484 IARLKKVRAERDEEAVEAALAALRK-AAEEDENLMPYAIEAVRAYATLGEISDALREVFGEYRAP 547
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
613-744 3.10e-78

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.


Pssm-ID: 129726  Cd Length: 132  Bit Score: 249.25  E-value: 3.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  613 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSL 692
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382073  693 GRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD 132
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
616-737 1.70e-63

methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.


Pssm-ID: 239022  Cd Length: 122  Bit Score: 208.99  E-value: 1.70e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 616 RLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRP 695
Cdd:cd02071    1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530382073 696 DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLD 737
Cdd:cd02071   81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
608-741 1.75e-53

Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];


Pssm-ID: 225096  Cd Length: 143  Bit Score: 181.72  E-value: 1.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 608 MEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIK 687
Cdd:COG2185    6 LRDRGARPRVLVAKLGLDGHDRGAKVIARALADAGFEVINLGLFQTPEEAVRAAVEEDVDVIGVSSLDGGHLTLVPGLVE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530382073 688 ELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEK 741
Cdd:COG2185   86 ALREAGVEDILVVVGGVIPPGDYQELKEMGVDRIFGPGTPIEEALSDLLTRLGA 139
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
615-726 4.50e-21

B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.


Pssm-ID: 280471  Cd Length: 118  Bit Score: 90.04  E-value: 4.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  615 PRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLgR 694
Cdd:pfam02310   1 GKVVLATVGGDLHPLGLNYVAAALREAGFEVILLGANVPPEDIVEAIRDEKPDVVGLSALMTTTLPGAKELIELLKGI-R 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 530382073  695 PDILVMCGGVIPPQDYEFLFEVGVSNVFGPGT 726
Cdd:pfam02310  80 PRVKVVVGGPHPTFDPELAAELGDDVVRGEGE 111
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
41-744 0e+00

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1397.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  41 PEWAALA---KKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEE--LPGVKPFTRGPYPTMYTFRPWTIRQYAGFST 115
Cdd:PRK09426   5 PDFADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLEGLEHLdtLPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 116 VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV 195
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 196 LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL 275
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 276 ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIeKMFQPKNSKSLLLRAHCQTSG 355
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIV-KQFGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 356 WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT 435
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 436 NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQI 515
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 516 EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK 595
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARSGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 596 EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLA 675
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382073 676 AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLG 712
mmCoA_mut_beta TIGR00642
methylmalonyl-CoA mutase, heterodimeric type, beta chain; The adenosylcobalamin-binding, ...
49-501 2.54e-71

methylmalonyl-CoA mutase, heterodimeric type, beta chain; The adenosylcobalamin-binding, catalytic chain of methylmalonyl-CoA mutase may form homodimers, as in mitochondrion and E. coli, or heterodimers with a shorter, homologous chain that does not bind adenosylcobalamin. This model describes this non-catalytic beta chain, as found in the enzyme from Propionibacterium freudenreichii, for which the 3-dimensional structure has been solved. [Central intermediary metabolism, Other]


Pssm-ID: 273191 [Multi-domain]  Cd Length: 619  Bit Score: 246.39  E-value: 2.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   49 KQLKGKNPED-LIWHTPEGISIKPLYSKRDTMDLPEeLPGVKPFTRGPYPTMYTFRPWTIRQyagfSTVEESNKfyKDNI 127
Cdd:TIGR00642  31 KQLTGAECEKrLTVHTVDGFDIVPMYRPKDAPKKLG-LPGVAPFVRGTTVRNGDHDAWDVRA----LHVEDPDE--AFTN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  128 KAGQQGLSvafdlathRGYDSDNPRVRGDvgmaGVAIDTVEDtkiLFDGIPLEKMSVSMTMNGAVIP-VLANFIVTGEEQ 206
Cdd:TIGR00642 104 KAILEGLE--------RGVTSLLLRVDPD----AIAPDHLDA---LLSDVLLEMTKVEVFSRYDQGAaAEALVSVYERSD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  207 GVPKEKLTGTIQNDILKEFMVRNtyifPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLE 286
Cdd:TIGR00642 169 GKPAKDLALNLGLDPIKFALLQG----VTEPDLTVLGDWVRRAAKFSPDSRAVTVDANIYHNAGAGDVAELAWALATGAE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  287 YSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKM-FQPKNSKSlllRAHCQTSGWSLTEQDPYN 365
Cdd:TIGR00642 245 YLRALTEQGFTATEAFDTINFRVTATHDQFMTIAKLRALRELWARIGEVFgDDEDKRGA---RQHAITSWRNKTREDPYV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  366 NIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVK-SARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALK 444
Cdd:TIGR00642 322 NILRGSIATFSASVGGADSITVLPFDVALGLPEDDfPLRIARNTQLLLAEEVHIGRVNDPAGGSYYVESLTRSLADAAWK 401
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073  445 LINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVE 501
Cdd:TIGR00642 402 EFQEVEKLGGFSKAVMTEHVTKVLDACNAERAKRLANRRQPITGVNEFPNIGARSIE 458
 
Name Accession Description Interval E-value
MM_CoA_mutase_alpha_like cd03679
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like ...
40-574 0e+00

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like subfamily; contains proteins similar to the alpha subunit of Propionbacterium shermanni MCM, as well as human and E. coli MCM. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. Sinorhizobium meliloti strain SU47 MCM plays a role in the polyhydroxyalkanoate degradation pathway. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism.


Pssm-ID: 239651  Cd Length: 536  Bit Score: 1182.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  40 HPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRD--TMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVE 117
Cdd:cd03679    1 LPEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADDldDMEHLDTLPGIPPFVRGPYATMYTFRPWTIRQYAGFSTAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 118 ESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLA 197
Cdd:cd03679   81 ESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPILA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 198 NFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILEL 277
Cdd:cd03679  161 FYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSKNMPKFNSISISGYHMQEAGATADLEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 278 AYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKmFQPKNSKSLLLRAHCQTSGWS 357
Cdd:cd03679  241 AYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFMEIAKLRAARLLWAKLVKQ-FGPKNPKSLALRTHSQTSGWS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 358 LTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTND 437
Cdd:cd03679  320 LTEQDPYNNVVRTCIEAMAAVFGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDD 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 438 VYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEK 517
Cdd:cd03679  400 LAEKAWALIQEIEELGGMAKAIESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIAR 479
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073 518 LKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFG 574
Cdd:cd03679  480 LKKLRAERDPEAVQAALDALTEAAETGEGNLLALAVDAARARATVGEISDALEKVFG 536
acid_CoA_mut_N TIGR00641
methylmalonyl-CoA mutase N-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
61-582 0e+00

methylmalonyl-CoA mutase N-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 abd 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 N-terminal domain subfamily. In a neighbor-joining tree, AF2215 branches with a bacterial isobutyryl-CoA mutase, which is also the same length. Scoring between the noise and trusted cutoffs are the non-catalytic, partially homologous beta chains from certain heterodimeric examples of 5.4.99.2.


Pssm-ID: 273190  Cd Length: 526  Bit Score: 1013.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   61 WHTPEGISIKPLYS----KRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSV 136
Cdd:TIGR00641   1 WHTAEGIPVKPLYTpalaDWDYMEKLGTFPGEPPFTRGPYATMYRFRPWTIRQYAGFSTAEESNKFYRRNLAAGQKGLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  137 AFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGT 216
Cdd:TIGR00641  81 AFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIEDMRILFDGIPLDKVSVSMTMNGAVLPILALYVVVAEEQGVPPEKLTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  217 IQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGL 296
Cdd:TIGR00641 161 IQNDILKEFMVRNTYIFPPEPSMRIIADIIAYTAKNMPKWNSISISGYHMQEAGATAVQELAFTLADGIEYIRAGLSAGL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  297 TIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMA 376
Cdd:TIGR00641 241 DVDSFAPRLSFFFGIGMNFFMEIAKLRAARRLWAKLVKEWFGAKNPKSMSLRTHCQTSGWSLTAQDPYNNIVRTAIEALA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  377 AVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMA 456
Cdd:TIGR00641 321 AVLGGTQSLHTNSFDEALGLPTDFSARIARNTQQIIQEESGVTRVIDPLGGSYYVEWLTDDIYERAWKYIQEIEEMGGMA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  457 KAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAA 536
Cdd:TIGR00641 401 KAIERGIPKLRIEEAAARTQARIDSGRQVIVGVNKYQLEEEDEVEVLKVDNSSVREEQIAKLKKLRAERDQEKVEAALDA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 530382073  537 LTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRM 582
Cdd:TIGR00641 481 LTKAAEKEDENLLALAIDAARARATLGEITDALEKVFGEYRAPIRT 526
MM_CoA_mutase pfam01642
Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of ...
63-573 0e+00

Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of enzymes that uses coenzyme B12 (adenosylcobalamin) as a cofactor. The enzyme induces the formation of an adenosyl radical from the cofactor. This radical then initiates a free-radical rearrangement of its substrate, succinyl-CoA, to methylmalonyl-CoA.


Pssm-ID: 279913  Cd Length: 511  Bit Score: 925.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   63 TPEGISIKPLYSKRDTM--DLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDL 140
Cdd:pfam01642   1 TYEGIPVKPLYTPEDIAeeDLGDSLPGEFPFTRGVYPTMYRGRPWTIRQYAGFGTAEETNARYRYLLAAGQTGLSVAFDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  141 ATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQND 220
Cdd:pfam01642  81 PTQRGYDSDHPRAEGEVGKAGVAIDSLEDMETLFDGIPLDKVSVSMTINAPALPLLAMYIAAAEEQGVDLEKLRGTIQND 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  221 ILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDE 300
Cdd:pfam01642 161 ILKEYIARGTYIYPPEPSMRIIADIIEYAAKNMPKFNTISISGYHIREAGATAVQELAFTLADGIEYLRALLEAGLDVDE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  301 FAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFG 380
Cdd:pfam01642 241 FAPRLSFFFAIGMNFFEEIAKFRAARRLWARIVKERFGAKNPRSLKLRFHAQTSGWSLTAQDPYNNILRTTTEAMAAVLG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  381 GTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVA 460
Cdd:pfam01642 321 GTQSLHTNPFDEALALPTEFSARIARNTQLILQEESGVTKVVDPLGGSYYVESLTDEIAEKAWALFQEIEELGGMLAAIE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  461 EGIPKLRIEECAARRQARIDSGSEVIVGVNKYQL-EKEDAVEVLAIDNTsVRNRQIEKLKKIKSSRDQALAERCLAALTE 539
Cdd:pfam01642 401 SGYPQREIAESAARRQKAIASGKEVIVGVNKYRPnETEKPLEILRVDPA-VRERQAARLEALRAERDGARVKAALAALGN 479
                         490       500       510
                  ....*....|....*....|....*....|....
gi 530382073  540 CAASgdGNILALAVDASRARCTVGEITDALKKVF 573
Cdd:pfam01642 480 AARG--GNLLARAIFAARAGATLGEISDALREVF 511
Sbm COG1884
Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];
42-579 0e+00

Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];


Pssm-ID: 224796  Cd Length: 548  Bit Score: 828.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  42 EWAALAKKQLKGKNPED--LIWHTPEGISIKPLYSKRDTMDLPEE----LPGVKPFTRGPYPTMYTFRPWTIRQYAGFST 115
Cdd:COG1884    4 EWEEKTLKPWLEKPGERkkLFKTTSEGIDVKPLYTPEDVARWDYLeklgVPGEYPFTRGVYPTMYRGRLWTMRQYAGFGT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 116 VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV 195
Cdd:COG1884   84 AEETNRRYRYLLAAGQTGLSVAFDLPTLRGYDSDHPRAEGEVGKAGVAIDTLKDMEILFDGIPLDKVSTSMTINGPAPPL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 196 LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL 275
Cdd:COG1884  164 LAMYLAVAEEQGVDREKLRGTIQNDILKEYIARNTYIYPPEPSMRIIVDIIEYCAKEVPKFNSISISGYHIREAGATAVQ 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 276 ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSG 355
Cdd:COG1884  244 ELAFTLADGVEYVRALLERGLDVDEFAPRLSFFFAAGNDFFEEVAKLRAARRLWARIMKEEFGAKNPRSMMLRFHTQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 356 WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT 435
Cdd:COG1884  324 WSLTAQDPENNILRTTIQALAAVLGGTQSLHTNSFDEALALPTEFSARIARNTQLILAEESGVADVVDPLGGSYYVEWLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 436 NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKY-QLEKEDAVEVLAIDNTSVRNRQ 514
Cdd:COG1884  404 DELEEAAWAYIEEIEAMGGMLKAIEDGYPQREIAESAARRQARIEEGERVIVGVNEYpEEGPEEPVEILKVDPEAVRERQ 483
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530382073 515 IEKLKKIKSSRDQALAERCLAALTEcAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKAN 579
Cdd:COG1884  484 IARLKKVRAERDEEAVEAALAALRK-AAEEDENLMPYAIEAVRAYATLGEISDALREVFGEYRAP 547
MM_CoA_mutase_ICM_like cd03680
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA ...
42-574 0e+00

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA mutase (ICM)-like subfamily; contains archaeal and bacterial proteins similar to the large subunit of Streptomyces cinnamonensis coenzyme B12-dependent ICM. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA, intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis.


Pssm-ID: 239652  Cd Length: 538  Bit Score: 736.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  42 EWAALAKKQLKGKNPE-DLIWHTPEGISIKPLYSKRDTMDLPEE----LPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTV 116
Cdd:cd03680    3 EWEEETLAPWLKKFPErKEKFTTLSGIPVKRVYTPADLPEDDYLedigYPGEYPFTRGVYPTMYRGRLWTMRQFAGFGTA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 117 EESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVL 196
Cdd:cd03680   83 EETNKRFKYLLEQGQTGLSVAFDLPTLMGYDSDHPMAEGEVGKVGVAIDTLADMEILFDGIPLDKVSTSMTINPPAAILL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 197 ANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILE 276
Cdd:cd03680  163 AMYIAVAEKQGVPLEKLRGTIQNDILKEYIAQKEWIFPPEPSVRLVTDIIEYCAKNVPKWNPISISGYHIREAGATAVQE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 277 LAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGW 356
Cdd:cd03680  243 LAFTLADGIAYVEAVLERGLDVDEFAPRLSFFFNSHNDFFEEIAKFRAARRIWAKIMKERFGAKNPRSMMLRFHTQTAGA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 357 SLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTN 436
Cdd:cd03680  323 SLTAQQPENNIVRTALQALAAVLGGTQSLHTNSFDEALALPTEEAVRIALRTQQIIAYESGVADVVDPLGGSYYVEALTD 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 437 DVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTsVRNRQIE 516
Cdd:cd03680  403 EIEEEAWKYIDKIDAMGGMIKAIEDGYFQREIADAAYKYQKEIESGERIVVGVNKFVVEEEPPIILLKVDDE-VEERQIE 481
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530382073 517 KLKKIKSSRDQALAERCLAALTEcAASGDGNILALAVDASRARCTVGEITDALKKVFG 574
Cdd:cd03680  482 RLKEVRAERDNAKVQEALDALRK-AAEDEENLMPYIIEAVKAYATLGEICDVLREVFG 538
MM_CoA_mutase cd00512
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM)-like family; contains ...
104-503 0e+00

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM)-like family; contains proteins similar to MCM, and the large subunit of Streptomyces coenzyme B12-dependent isobutyryl-CoA mutase (ICM). MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In higher animals, MCM is involved in the breakdown of odd-chain fatty acids, several amino acids, and cholesterol. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include Propionbacterium shermanni MCM during propionic acid fermentation, E.coli MCM in a pathway for the conversion of succinate to propionate and Streptomyces MCM in polyketide biosynthesis. P. shermanni and Streptomyces cinnamonensis MCMs are alpha/beta heterodimers, with both subunits being homologous members of this family. It has been shown for P. shermanni MCM that only the alpha subunit binds coenzyme B12 and substrates. Human MCM is a homodimer with two active sites. Mouse and E.coli MCMs are also homodimers. ICM from S. cinnamonensis is comprised of a large and a small subunit. The holoenzyme appears to be an alpha2beta2 heterotetramer with up to 2 molecules of coenzyme B12 bound. The small subunit binds coenzyme B12. ICM catalyzes the reversible rearrangement of n-butyryl-CoA to isobutyryl-CoA (intermediates in fatty acid and valine catabolism, which in S. cinnamonensis can be converted to methylmalonyl-CoA and used in polyketide synthesis). In humans, impaired activity of MCM results in methylmalonic aciduria, a disorder of propionic acid metabolism.


Pssm-ID: 238283  Cd Length: 399  Bit Score: 582.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 104 PWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMS 183
Cdd:cd00512    1 PWTQRQLAGFGTAEETNKRYRRNLAAGQTGLSVAFDLPTLRGYDSDNPRDAGEVGMCGVAIDTLEDMDELFQGIPLEQTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 184 VSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISG 263
Cdd:cd00512   81 VSMTINGPALPALALYVVVAERQGVDASDLAGTLQNDIIKEYIAQGTYIFPPEPSLRVLGDIIEYCSANIPKWNPVSISG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 264 YHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKmFQPKNSK 343
Cdd:cd00512  161 YHMQEAGATPVQELAYTLATGIEYVRACLERGLDVDEFAPRLSFFFGIGMNFFEEIAKLRAARRIWARITRD-FGGAEPK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 344 SLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVAD 423
Cdd:cd00512  240 SRRLRYHVQTSGRSLTAQQPYNNVARTSIQAMAATLGGAQSLHTNAYDEAIGLPTEFSARIALRTQQVLAEESGLARVID 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 424 PWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVL 503
Cdd:cd00512  320 PLGGSYYVEELTDSLEDAAWKEFQEIEKRGGMLKAVETGYVKGVIDESAAERQARIESGKQPIVGVNKYRMEEAPPIEPK 399
MM_CoA_mutase_MeaA cd03681
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, MeaA-like subfamily; ...
104-493 7.88e-107

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, MeaA-like subfamily; contains various methylmalonyl coenzyme A (CoA) mutase (MCM)-like proteins similar to the Streptomyces cinnamonensis MeaA, Methylobacterium extorquens MeaA and Streptomyces collinus B12-dependent mutase. Members of this subfamily contain an N-terminal MCM domain and a C-terminal coenzyme B12 binding domain. S. cinnamonensis MeaA is a putative B12-dependent mutase which provides methylmalonyl-CoA precursors for the biosynthesis of the monensin polyketide via an unknown pathway. S. collinus B12-dependent mutase may be involved in a pathway for acetate assimilation.


Pssm-ID: 239653  Cd Length: 407  Bit Score: 334.93  E-value: 7.88e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 104 PWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMS 183
Cdd:cd03681    1 PWIIRTYAGHSTAEESNELYRKNLAKGQTGLSVAFDLPTQTGYDSDHILAKGEVGKVGVPINHLGDMRILFNQIPLEQMN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 184 VSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISG 263
Cdd:cd03681   81 TSMTINATAMWLLSLYVAVAEEQGADVTALQGTTQNDIIKEYLSRGTYIFPPAPSLRLIVDMIEYCLKNIPKWNPMNICS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 264 YHMQEAGADAILELAYTLADGLEYSRTGLQAG-LTIDEF---APRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQP 339
Cdd:cd03681  161 YHLQEAGATPVQELAFALATAIAVLDAVRDRNcFPEDEFedvVSRISFFVNAGIRFVEEMCKMRAFTELWDEITRDRYGI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 340 KNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGG---TQSLHTNSFDEALGLPTVKSARIARNTQIIIQEES 416
Cdd:cd03681  241 KDAKYRRFRYGVQVNSLGLTEQQPENNVWRILIEMLAVTLSKdarARAVQLPAWNEALGLPRPWDQQWSLRMQQVLAYET 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073 417 GIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQ 493
Cdd:cd03681  321 DLLEYDDLFDGSKVVEAKVEALKEEARAELQRILDMGGAVQAIENGYMKSQLVKSNAERLARIENNEMVIVGVNKWQ 397
MM_CoA_mutase_beta cd03677
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Beta subunit-like ...
42-503 1.32e-104

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Beta subunit-like subfamily; contains bacterial proteins similar to the beta subunit of MCMs from Propionbacterium shermanni and Streptomyces cinnamonensis, which are alpha/beta heterodimers. For P. shermanni MCM, it is known that only the alpha subunit binds coenzyme B12 and substrates. The role of the beta subunit is unclear. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. Methylobacterium extorquens MCM participates in the glyoxylate regeneration pathway. In M. extorquens, MCM forms a complex with MeaB; MeaB may protect MCM from irreversible inactivation. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Examples include P. shermanni MCM during propionic acid fermentation and Streptomyces MCM in polyketide biosynthesis.


Pssm-ID: 239649  Cd Length: 424  Bit Score: 329.57  E-value: 1.32e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  42 EWAALAKKQLKGKNPED-LIWHTPEGISIKPLYSKRDTMDLPeelpgvkpftrgPYPTMYTFRPWTIRQYAGFSTVEESN 120
Cdd:cd03677    8 AWKAKVEKDLKGAPFEErLVWKTYDGITIKPLYTREDAAPLP------------PVPEGAAPGGWDVCQRIDVPDAAEAN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 121 KFYKDNIKAGQQGLSVAFDLATHrgydsdnprvrgdvgmagvaidTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFI 200
Cdd:cd03677   76 EAALADLERGATALWLVLDNAGC----------------------SPEDLARLLEGVDLDLAPVYLDAGFLSLAAAAALL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 201 VTGEEQgvpkEKLTGTIQNDILKEFMVrnTYIFPPEPSMKIIADIFeytAKHMPKFNSISISGYHMQEAGADAILELAYT 280
Cdd:cd03677  134 ALVEDR----KALAGSLGLDPLGALAR--TGSLFLEPDLARLAELA---ARSAPGLRAITVDAVPYHNAGATAAQELAYA 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 281 LADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKsllLRAHCQTSGWSLTE 360
Cdd:cd03677  205 LAAAVEYLRALTEAGLDVEEAARQIEFRLAVGSDQFLEIAKLRALRLLWARIAEAYGVPEARA---ARIHARTSRRNKTR 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 361 QDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYD 440
Cdd:cd03677  282 YDPYVNMLRTTTEAFSAGLGGADSITVLPFDAALGLPDDFARRIARNTQLILKEESHLGRVADPAGGSYYIESLTDQLAE 361
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530382073 441 AALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVL 503
Cdd:cd03677  362 KAWELFQEIEAAGGFVAALESGLIQKKIAESAAKRQKALATRKKPLTGVNEYPNLEEKPLERL 424
MM_CoA_mutase_1 cd03678
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, unknown subfamily 1; ...
81-502 2.05e-87

Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, unknown subfamily 1; composed of uncharacterized bacterial proteins containing a C-terminal MCM domain. MCM catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA. The reaction proceeds via radical intermediates beginning with a substrate-induced homolytic cleavage of the Co-C bond of coenzyme B12 to produce cob(II)alamin and the deoxyadenosyl radical. MCM plays an important role in the conversion of propionyl-CoA to succinyl-CoA during the degradation of propionate for the Krebs cycle. In some bacteria, MCM is involved in the reverse metabolic reaction, the rearrangement of succinyl-CoA to methylmalonyl-CoA. Members of this subfamily also contain an N-terminal coenzyme B12 binding domain followed by a domain similar to the E. coli ArgK membrane ATPase.


Pssm-ID: 239650  Cd Length: 495  Bit Score: 286.34  E-value: 2.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  81 LPEELPGVKPFTRGPYPTMYTFRPWTiRQYAGFSTVEESNKFYKdNIKAGQ--QGLSVAFDLATHRGYDSD-NPRVRGDV 157
Cdd:cd03678   59 LRENVPGEFPFTAGVFPFKRTGEDPT-RMFAGEGTPERTNRRFH-YLSEGMpaKRLSTAFDSVTLYGEDPDpRPDIYGKI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 158 GMAGVAIDTVEDTKILFDGIPL--EKMSVSMTMNGAVIPVLANFIVTGEEQGVPK------------EKLTGTIQNDILK 223
Cdd:cd03678  137 GNSGVSVATLDDMKKLYSGFDLcaPNTSVSMTINGPAPMLLAFFLNTAIDQQVEKfrrengiraetlRSVRGTVQADILK 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 224 EFMVRNTYIFPPEPSMKIIADIFEYTAKHMPK-FNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFA 302
Cdd:cd03678  217 EDQAQNTCIFSTEFALRMMGDIQEYFIAHQVRnFYSVSISGYHIAEAGANPITQLAFTLANGFTYVEYYLSRGMHIDDFA 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 303 PRLSFFWGIGMN-FYMEIAkmRAGRRLWAHLIEKMFQpKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGG 381
Cdd:cd03678  297 PNLSFFFSNGLDpEYAVIG--RVARRIWARAMREKYG-ANERSQMLKYHIQTSGRSLHAQEIDFNDIRTTLQALYAIYDN 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 382 TQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAE 461
Cdd:cd03678  374 CNSLHTNAYDEAITTPTEESVRRALAIQLIINRELGLAKNENPLQGSFIIEELTDLVEEAVLAEFERISERGGVLGAMET 453
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 530382073 462 GIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEV 502
Cdd:cd03678  454 GYQRNKIQEESLYYESLKHDGELPIIGVNTFRSPNGDPTIL 494
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
613-744 3.10e-78

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.


Pssm-ID: 129726  Cd Length: 132  Bit Score: 249.25  E-value: 3.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  613 RRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSL 692
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530382073  693 GRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD 132
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
616-737 1.70e-63

methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), which initiates the conversion of succinyl CoA and methylmalonyl CoA by forming an adenosyl radical, which then undergoes a rearrangement exchanging a hydrogen atom with a group attached to a neighboring carbon atom. This family is present in both mammals and bacteria. Bacterial members are heterodimers and involved in the fermentation of pyruvate to propionate. Mammalian members are homodimers and responsible for the conversion of odd-chain fatty acids and branched-chain amino acids via propionyl CoA to succinyl CoA for further degradation.


Pssm-ID: 239022  Cd Length: 122  Bit Score: 208.99  E-value: 1.70e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 616 RLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRP 695
Cdd:cd02071    1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530382073 696 DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLD 737
Cdd:cd02071   81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
608-741 1.75e-53

Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and metabolism];


Pssm-ID: 225096  Cd Length: 143  Bit Score: 181.72  E-value: 1.75e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 608 MEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIK 687
Cdd:COG2185    6 LRDRGARPRVLVAKLGLDGHDRGAKVIARALADAGFEVINLGLFQTPEEAVRAAVEEDVDVIGVSSLDGGHLTLVPGLVE 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530382073 688 ELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEK 741
Cdd:COG2185   86 ALREAGVEDILVVVGGVIPPGDYQELKEMGVDRIFGPGTPIEEALSDLLTRLGA 139
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
616-738 7.86e-42

B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide, it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins.


Pssm-ID: 239018  Cd Length: 119  Bit Score: 148.42  E-value: 7.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 616 RLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRP 695
Cdd:cd02067    1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530382073 696 DILVMCGGVIPPQDYEFLFEVGVSNVFGPGTripkAAVQVLDD 738
Cdd:cd02067   81 DIPVLVGGAIVTRDFKFLKEIGVDAYFGPAT----EAVEVLKK 119
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
616-737 4.48e-28

B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide. This domain is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins. Not all members of this family contain the conserved binding motif.


Pssm-ID: 239016  Cd Length: 125  Bit Score: 110.17  E-value: 4.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 616 RLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRp 695
Cdd:cd02065    1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530382073 696 DILVMCGGVIPPQDYE----FLFEVGVSNVFGPGTRIPKAAVQVLD 737
Cdd:cd02065   80 DIPVVVGGAHPTADPEepkvDAVVIGEGEYAGPALLEVEGIAYRKN 125
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
615-726 4.50e-21

B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.


Pssm-ID: 280471  Cd Length: 118  Bit Score: 90.04  E-value: 4.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  615 PRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLgR 694
Cdd:pfam02310   1 GKVVLATVGGDLHPLGLNYVAAALREAGFEVILLGANVPPEDIVEAIRDEKPDVVGLSALMTTTLPGAKELIELLKGI-R 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 530382073  695 PDILVMCGGVIPPQDYEFLFEVGVSNVFGPGT 726
Cdd:pfam02310  80 PRVKVVVGGPHPTFDPELAAELGDDVVRGEGE 111
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
617-734 2.85e-04

B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S)-glutamate with (2S,3S)-3-methylaspartate. The rearrangement reaction is initiated by the extraction of a hydrogen from the protein-bound substrate by a 5'-desoxyadenosyl radical, which is generated by the homolytic cleavage of the organometallic bond of the cofactor B12. Glm is a heterotetrameric molecule consisting of two alpha and two epsilon polypeptide chains.


Pssm-ID: 239023  Cd Length: 128  Bit Score: 40.14  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 617 LLVAKMGQDGHDRGAKVIATGFADLGFDV-DIGplFQTPR-EVAQQAVDADVHAVGISTLaAGHKTLVPELIKE-LNSLG 693
Cdd:cd02072    2 IVLGVIGSDCHAVGNKILDHAFTEAGFNVvNLG--VLSPQeEFIDAAIETDADAILVSSL-YGHGEIDCKGLREkCDEAG 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530382073 694 RPDILVMCGG--VIPPQDYEFL---F-EVGVSNVFGPGTRIPKAAVQ 734
Cdd:cd02072   79 LKDILLYVGGnlVVGKQDFEDVekrFkEMGFDRVFAPGTPPEEAIAD 125
MthylAspMutase TIGR01501
methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of ...
614-736 7.68e-04

methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of methylaspartate mutase (glutamate mutase), a cobalamin-dependent enzyme that catalyzes the first step in a pathway of glutamate fermentation. [Energy metabolism, Amino acids and amines, Energy metabolism, Fermentation]


Pssm-ID: 130565  Cd Length: 134  Bit Score: 39.09  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  614 RPRLLVAKMGQDGHDRGAKVIATGFADLGFDV-DIGplFQTPREV-AQQAVDADVHAVGISTLAAGHKTLVPELIKELNS 691
Cdd:TIGR01501   1 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVvNLG--VLSPQEEfIKAAIETKADAILVSSLYGHGEIDCKGLRQKCDE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530382073  692 LGRPDILVMCGG--VIPPQDYEFL----FEVGVSNVFGPGTRiPKAAVQVL 736
Cdd:TIGR01501  79 AGLEGILLYVGGnlVVGKQDFPDVekrfKEMGFDRVFAPGTP-PEVVIADL 128
dhbA_paeA TIGR04316
2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2, ...
629-722 3.39e-03

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Members of this family are 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EC 1.3.1.28), the third enzyme in the biosynthesis of 2,3-dihydroxybenzoic acid (DHB) from chorismate. The first two enzymes are isochorismate synthase (EC 5.4.4.2) and isochorismatase (EC 3.3.2.1). Synthesis is often followed by adenylation by the enzyme DHBA-AMP ligase (EC 2.7.7.58) to activate (DHB) for a non-ribosomal peptide synthetase.


Pssm-ID: 275120  Cd Length: 250  Bit Score: 38.42  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  629 RGAKVIAtgfadlgFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAghktlVPELIKEL-NSLGRPDILVMCGGV--- 704
Cdd:TIGR04316  21 AGARVAA-------VDRNFEQLLELVADLRRYGYPFATYKLDVADSAA-----VDEVVQRLeREYGPIDVLVNVAGIlrl 88
                          90       100
                  ....*....|....*....|...
gi 530382073  705 -----IPPQDYEFLFEVGVSNVF 722
Cdd:TIGR04316  89 gaidsLSDEDWQATFAVNTFGVF 111
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
41-744 0e+00

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1397.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  41 PEWAALA---KKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEE--LPGVKPFTRGPYPTMYTFRPWTIRQYAGFST 115
Cdd:PRK09426   5 PDFADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLEGLEHLdtLPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 116 VEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPV 195
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 196 LANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAIL 275
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 276 ELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIeKMFQPKNSKSLLLRAHCQTSG 355
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIV-KQFGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 356 WSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLT 435
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 436 NDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQI 515
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 516 EKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESK 595
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARSGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073 596 EITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLA 675
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530382073 676 AGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLE 744
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLG 712
mmCoA_mut_beta TIGR00642
methylmalonyl-CoA mutase, heterodimeric type, beta chain; The adenosylcobalamin-binding, ...
49-501 2.54e-71

methylmalonyl-CoA mutase, heterodimeric type, beta chain; The adenosylcobalamin-binding, catalytic chain of methylmalonyl-CoA mutase may form homodimers, as in mitochondrion and E. coli, or heterodimers with a shorter, homologous chain that does not bind adenosylcobalamin. This model describes this non-catalytic beta chain, as found in the enzyme from Propionibacterium freudenreichii, for which the 3-dimensional structure has been solved. [Central intermediary metabolism, Other]


Pssm-ID: 273191 [Multi-domain]  Cd Length: 619  Bit Score: 246.39  E-value: 2.54e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073   49 KQLKGKNPED-LIWHTPEGISIKPLYSKRDTMDLPEeLPGVKPFTRGPYPTMYTFRPWTIRQyagfSTVEESNKfyKDNI 127
Cdd:TIGR00642  31 KQLTGAECEKrLTVHTVDGFDIVPMYRPKDAPKKLG-LPGVAPFVRGTTVRNGDHDAWDVRA----LHVEDPDE--AFTN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  128 KAGQQGLSvafdlathRGYDSDNPRVRGDvgmaGVAIDTVEDtkiLFDGIPLEKMSVSMTMNGAVIP-VLANFIVTGEEQ 206
Cdd:TIGR00642 104 KAILEGLE--------RGVTSLLLRVDPD----AIAPDHLDA---LLSDVLLEMTKVEVFSRYDQGAaAEALVSVYERSD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  207 GVPKEKLTGTIQNDILKEFMVRNtyifPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLE 286
Cdd:TIGR00642 169 GKPAKDLALNLGLDPIKFALLQG----VTEPDLTVLGDWVRRAAKFSPDSRAVTVDANIYHNAGAGDVAELAWALATGAE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  287 YSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKM-FQPKNSKSlllRAHCQTSGWSLTEQDPYN 365
Cdd:TIGR00642 245 YLRALTEQGFTATEAFDTINFRVTATHDQFMTIAKLRALRELWARIGEVFgDDEDKRGA---RQHAITSWRNKTREDPYV 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530382073  366 NIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVK-SARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALK 444
Cdd:TIGR00642 322 NILRGSIATFSASVGGADSITVLPFDVALGLPEDDfPLRIARNTQLLLAEEVHIGRVNDPAGGSYYVESLTRSLADAAWK 401
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530382073  445 LINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVE 501
Cdd:TIGR00642 402 EFQEVEKLGGFSKAVMTEHVTKVLDACNAERAKRLANRRQPITGVNEFPNIGARSIE 458
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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