NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|25144500|ref|NP_497786|]
View 

putative methylmalonyl-CoA mutase, mitochondrial [Caenorhabditis elegans]

Protein Classification

methylmalonyl-CoA mutase( domain architecture ID 11484152)

methylmalonyl-CoA mutase catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
32-737 0e+00

methylmalonyl-CoA mutase; Reviewed


:

Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1384.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   32 WAAMA---KKAMKGREADTLTWNTPEGIPIKPLYLRSDR-DCDAQRSveLPGQFPFTRGPYPTMYTQRPWTIRQYAGFST 107
Cdd:PRK09426   7 FADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLeGLEHLDT--LPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  108 VEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPV 187
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  188 LAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVL 267
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  268 EMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMMLRTHSQTSG 347
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIVKQ-FGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  348 WSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLT 427
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  428 DEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQC 507
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  508 AKLNHIRATRDAEKAQKALDAITEGAR-GNGNLMELAIEAARARCTVGEISDAMEKVFNRHAAVNRLVSGAYKSEFGETS 586
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARsGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  587 EMSQVLERVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLA 666
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25144500  667 AGHLTLIPQLIGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANLPEA 737
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLGYA 714
 
Name Accession Description Interval E-value
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
32-737 0e+00

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1384.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   32 WAAMA---KKAMKGREADTLTWNTPEGIPIKPLYLRSDR-DCDAQRSveLPGQFPFTRGPYPTMYTQRPWTIRQYAGFST 107
Cdd:PRK09426   7 FADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLeGLEHLDT--LPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  108 VEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPV 187
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  188 LAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVL 267
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  268 EMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMMLRTHSQTSG 347
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIVKQ-FGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  348 WSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLT 427
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  428 DEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQC 507
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  508 AKLNHIRATRDAEKAQKALDAITEGAR-GNGNLMELAIEAARARCTVGEISDAMEKVFNRHAAVNRLVSGAYKSEFGETS 586
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARsGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  587 EMSQVLERVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLA 666
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25144500  667 AGHLTLIPQLIGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANLPEA 737
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLGYA 714
MM_CoA_mutase_alpha_like cd03679
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like ...
30-565 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 [Multi-domain]  Cd Length: 536  Bit Score: 1133.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  30 QKWAAMAKKAMKGREADTLTWNTPEGIPIKPLYLRSDrDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVE 109
Cdd:cd03679   2 PEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADD-LDDMEHLDTLPGIPPFVRGPYATMYTFRPWTIRQYAGFSTAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 110 ESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLA 189
Cdd:cd03679  81 ESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPILA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 190 MYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEM 269
Cdd:cd03679 161 FYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSKNMPKFNSISISGYHMQEAGATADLEL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 270 AFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMMLRTHSQTSGWS 349
Cdd:cd03679 241 AYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFMEIAKLRAARLLWAKLVKQ-FGPKNPKSLALRTHSQTSGWS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 350 LTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDE 429
Cdd:cd03679 320 LTEQDPYNNVVRTCIEAMAAVFGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDD 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 430 IYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAK 509
Cdd:cd03679 400 LAEKAWALIQEIEELGGMAKAIESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIAR 479
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25144500 510 LNHIRATRDAEKAQKALDAITEGAR-GNGNLMELAIEAARARCTVGEISDAMEKVFN 565
Cdd:cd03679 480 LKKLRAERDPEAVQAALDALTEAAEtGEGNLLALAVDAARARATVGEISDALEKVFG 536
Sbm COG1884
Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];
39-569 0e+00

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


Pssm-ID: 441488  Cd Length: 533  Bit Score: 1026.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  39 AMKGREADTLTWNTPEGIPIKPLYLRSDR-DCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKE 117
Cdd:COG1884   1 KLRKKPERKLEFTTLSGIPVKPVYTPADLaDLDYLEDLGFPGEFPYTRGVYPTMYRGRPWTMRQYAGFGTAEETNARYRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 118 NIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEE 197
Cdd:COG1884  81 LLAAGQTGLSVAFDLPTLRGYDSDHPRAYGEVGKAGVAIDSLEDMEILFDGIPLDKVSVSMTINGPAPPLLAMYIAAAEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 198 AGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGI 277
Cdd:COG1884 161 QGVDPEKLRGTIQNDILKEYIARNTYIFPPEPSMRLIGDIFEYCAKHVPKFNSISISGYHIREAGATAVQELAFTLADGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 278 QYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYN 357
Cdd:COG1884 241 EYVEAALARGLDVDDFAPRLSFFFNIGMDFFEEVAKFRAARRIWARIMKERFGAKNPRSMMLRFHTQTSGWSLTAQQPLN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 358 NIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAV 437
Cdd:COG1884 321 NIVRTTLQALAAVLGGTQSLHTNAYDEALALPTEESARIALRTQQIIAEETGVTDTVDPLGGSYYVESLTDELEERAWAY 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 438 IKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAkVREEQCAKLNHIRATR 517
Cdd:COG1884 401 IEEIEELGGMLKAIETGYPQREIQEAAYRYQARIDSGERVIVGVNKFRLEEEPPIELLRVDPE-VRERQIERLKELRAER 479
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|..
gi 25144500 518 DAEKAQKALDAITEGARGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAA 569
Cdd:COG1884 480 DNAAVEAALAALREAARSGGNLMPLIIDAVRAYATLGEISDALREVFGEYRE 531
acid_CoA_mut_N TIGR00641
methylmalonyl-CoA mutase N-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
50-569 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 [Multi-domain]  Cd Length: 526  Bit Score: 921.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500    50 WNTPEGIPIKPLYLRSDRDCDAQRSV-ELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSV 128
Cdd:TIGR00641   1 WHTAEGIPVKPLYTPALADWDYMEKLgTFPGEPPFTRGPYATMYRFRPWTIRQYAGFSTAEESNKFYRRNLAAGQKGLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   129 AFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGT 208
Cdd:TIGR00641  81 AFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIEDMRILFDGIPLDKVSVSMTMNGAVLPILALYVVVAEEQGVPPEKLTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   209 IQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGL 288
Cdd:TIGR00641 161 IQNDILKEFMVRNTYIFPPEPSMRIIADIIAYTAKNMPKWNSISISGYHMQEAGATAVQELAFTLADGIEYIRAGLSAGL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   289 TIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMA 368
Cdd:TIGR00641 241 DVDSFAPRLSFFFGIGMNFFMEIAKLRAARRLWAKLVKEWFGAKNPKSMSLRTHCQTSGWSLTAQDPYNNIVRTAIEALA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   369 SVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMA 448
Cdd:TIGR00641 321 AVLGGTQSLHTNSFDEALGLPTDFSARIARNTQQIIQEESGVTRVIDPLGGSYYVEWLTDDIYERAWKYIQEIEEMGGMA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   449 KAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAKLNHIRATRDAEKAQKALDA 528
Cdd:TIGR00641 401 KAIERGIPKLRIEEAAARTQARIDSGRQVIVGVNKYQLEEEDEVEVLKVDNSSVREEQIAKLKKLRAERDQEKVEAALDA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 25144500   529 ITEGA-RGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAA 569
Cdd:TIGR00641 481 LTKAAeKEDENLLALAIDAARARATLGEITDALEKVFGEYRA 522
MM_CoA_mutase pfam01642
Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of ...
52-556 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: 460279 [Multi-domain]  Cd Length: 503  Bit Score: 917.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500    52 TPEGIPIKPLYLRsdRDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFD 131
Cdd:pfam01642   2 TNEGIPVKPLYTP--EDLYEELGDSLPGEFPFTRGVYPTMYRGRPWTIRQYAGFGTAEETNERYRYLLAAGQTGLSVAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   132 LATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQN 211
Cdd:pfam01642  80 LPTQRGYDSDHPRAEGEVGKAGVAIDSLEDMETLFDGIPLDKVSVSMTINAPALPLLAMYIAAAEEQGVDPEKLRGTIQN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   212 DILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTID 291
Cdd:pfam01642 160 DILKEYIARGTYIYPPEPSMRLIADIIEYCAKNMPKWNTISISGYHIREAGATAVQELAFTLADGIEYVRALLEAGLDVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   292 AFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVF 371
Cdd:pfam01642 240 EFAPRLSFFFAIGMNFFEEIAKFRAARRLWARIMKERFGAKNPKSLKLRFHAQTSGWSLTAQDPYNNILRTTTEAMAAVL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   372 GGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAV 451
Cdd:pfam01642 320 GGTQSLHTNPFDEALALPTEFSARIARNTQQILAEESGVTRVVDPLGGSYYVESLTDEIAEKAWALFQEIEELGGMLAAI 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   452 ASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAkVREEQCAKLNHIRATRDAEKAQKALDAITE 531
Cdd:pfam01642 400 ESGYPQREIAESAYRRQKAIASGKEVIVGVNKYPNEEEKPLEILRVDPE-VRERQAARLEALRAARDGARVKAALAALGN 478
                         490       500
                  ....*....|....*....|....*
gi 25144500   532 GARGNGNLMELAIEAARARCTVGEI 556
Cdd:pfam01642 479 AARGGENLMARAVFAANAYATLGEI 503
 
Name Accession Description Interval E-value
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
32-737 0e+00

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 1384.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   32 WAAMA---KKAMKGREADTLTWNTPEGIPIKPLYLRSDR-DCDAQRSveLPGQFPFTRGPYPTMYTQRPWTIRQYAGFST 107
Cdd:PRK09426   7 FADLAlkaAASAPGKTPDSLVWQTPEGIDVKPLYTAADLeGLEHLDT--LPGFAPFLRGPYATMYAGRPWTIRQYAGFST 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  108 VEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPV 187
Cdd:PRK09426  85 AEESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  188 LAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVL 267
Cdd:PRK09426 165 LAFYIVAAEEQGVPPEKLSGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSQNMPKFNSISISGYHMQEAGATADL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  268 EMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMMLRTHSQTSG 347
Cdd:PRK09426 245 ELAYTLADGREYVRAGLAAGLDIDDFAPRLSFFWAIGMNFFMEIAKLRAARLLWAKIVKQ-FGPKNPKSLALRTHCQTSG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  348 WSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLT 427
Cdd:PRK09426 324 WSLTEQDPYNNVVRTTIEAMAATLGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITRVVDPWAGSYYVESLT 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  428 DEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQC 507
Cdd:PRK09426 404 HELAEKAWAHIEEVEALGGMAKAIEAGIPKLRIEEAAARTQARIDSGKQVIVGVNKYRLDKEDPIDVLEVDNTAVRAEQI 483
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  508 AKLNHIRATRDAEKAQKALDAITEGAR-GNGNLMELAIEAARARCTVGEISDAMEKVFNRHAAVNRLVSGAYKSEFGETS 586
Cdd:PRK09426 484 ARLERLRAERDEAAVEAALAALTRAARsGEGNLLALAVDAARARATVGEISDALEKVFGRHRAEIRTISGVYGSEYGDDP 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  587 EMSQVLERVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLA 666
Cdd:PRK09426 564 EFAAARALVEAFAEAEGRRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLA 643
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25144500  667 AGHLTLIPQLIGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANLPEA 737
Cdd:PRK09426 644 AGHKTLVPALIEALKKLGREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLELLSARLGYA 714
MM_CoA_mutase_alpha_like cd03679
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Alpha subunit-like ...
30-565 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 [Multi-domain]  Cd Length: 536  Bit Score: 1133.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  30 QKWAAMAKKAMKGREADTLTWNTPEGIPIKPLYLRSDrDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVE 109
Cdd:cd03679   2 PEWAELAAKALKGREPEGLNWHTPEGIPVKPLYTADD-LDDMEHLDTLPGIPPFVRGPYATMYTFRPWTIRQYAGFSTAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 110 ESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLA 189
Cdd:cd03679  81 ESNAFYRRNLAAGQKGLSVAFDLATHRGYDSDHPRVVGDVGKAGVAIDSVEDMKILFDGIPLDKMSVSMTMNGAVLPILA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 190 MYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEM 269
Cdd:cd03679 161 FYIVAAEEQGVPPEKLTGTIQNDILKEFMVRNTYIYPPEPSMRIIADIFAYTSKNMPKFNSISISGYHMQEAGATADLEL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 270 AFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMMLRTHSQTSGWS 349
Cdd:cd03679 241 AYTLADGLEYIRTGLKAGLDIDEFAPRLSFFWGIGMNFFMEIAKLRAARLLWAKLVKQ-FGPKNPKSLALRTHSQTSGWS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 350 LTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDE 429
Cdd:cd03679 320 LTEQDPYNNVVRTCIEAMAAVFGGTQSLHTNALDEAIALPTDFSARIARNTQLILQEETGITKVVDPWGGSYYMESLTDD 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 430 IYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAK 509
Cdd:cd03679 400 LAEKAWALIQEIEELGGMAKAIESGIPKLRIEEAAARRQARIDSGREVIVGVNKYRLDHEEPLDVLKIDNTAVRAEQIAR 479
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 25144500 510 LNHIRATRDAEKAQKALDAITEGAR-GNGNLMELAIEAARARCTVGEISDAMEKVFN 565
Cdd:cd03679 480 LKKLRAERDPEAVQAALDALTEAAEtGEGNLLALAVDAARARATVGEISDALEKVFG 536
Sbm COG1884
Methylmalonyl-CoA mutase, N-terminal domain/subunit [Lipid transport and metabolism];
39-569 0e+00

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


Pssm-ID: 441488  Cd Length: 533  Bit Score: 1026.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  39 AMKGREADTLTWNTPEGIPIKPLYLRSDR-DCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKE 117
Cdd:COG1884   1 KLRKKPERKLEFTTLSGIPVKPVYTPADLaDLDYLEDLGFPGEFPYTRGVYPTMYRGRPWTMRQYAGFGTAEETNARYRY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 118 NIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEE 197
Cdd:COG1884  81 LLAAGQTGLSVAFDLPTLRGYDSDHPRAYGEVGKAGVAIDSLEDMEILFDGIPLDKVSVSMTINGPAPPLLAMYIAAAEE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 198 AGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGI 277
Cdd:COG1884 161 QGVDPEKLRGTIQNDILKEYIARNTYIFPPEPSMRLIGDIFEYCAKHVPKFNSISISGYHIREAGATAVQELAFTLADGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 278 QYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYN 357
Cdd:COG1884 241 EYVEAALARGLDVDDFAPRLSFFFNIGMDFFEEVAKFRAARRIWARIMKERFGAKNPRSMMLRFHTQTSGWSLTAQQPLN 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 358 NIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAV 437
Cdd:COG1884 321 NIVRTTLQALAAVLGGTQSLHTNAYDEALALPTEESARIALRTQQIIAEETGVTDTVDPLGGSYYVESLTDELEERAWAY 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 438 IKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAkVREEQCAKLNHIRATR 517
Cdd:COG1884 401 IEEIEELGGMLKAIETGYPQREIQEAAYRYQARIDSGERVIVGVNKFRLEEEPPIELLRVDPE-VRERQIERLKELRAER 479
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|..
gi 25144500 518 DAEKAQKALDAITEGARGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAA 569
Cdd:COG1884 480 DNAAVEAALAALREAARSGGNLMPLIIDAVRAYATLGEISDALREVFGEYRE 531
acid_CoA_mut_N TIGR00641
methylmalonyl-CoA mutase N-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
50-569 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 [Multi-domain]  Cd Length: 526  Bit Score: 921.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500    50 WNTPEGIPIKPLYLRSDRDCDAQRSV-ELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSV 128
Cdd:TIGR00641   1 WHTAEGIPVKPLYTPALADWDYMEKLgTFPGEPPFTRGPYATMYRFRPWTIRQYAGFSTAEESNKFYRRNLAAGQKGLSV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   129 AFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGT 208
Cdd:TIGR00641  81 AFDLPTHRGYDSDNPRVAGDVGMAGVAIDSIEDMRILFDGIPLDKVSVSMTMNGAVLPILALYVVVAEEQGVPPEKLTGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   209 IQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGL 288
Cdd:TIGR00641 161 IQNDILKEFMVRNTYIFPPEPSMRIIADIIAYTAKNMPKWNSISISGYHMQEAGATAVQELAFTLADGIEYIRAGLSAGL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   289 TIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMA 368
Cdd:TIGR00641 241 DVDSFAPRLSFFFGIGMNFFMEIAKLRAARRLWAKLVKEWFGAKNPKSMSLRTHCQTSGWSLTAQDPYNNIVRTAIEALA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   369 SVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMA 448
Cdd:TIGR00641 321 AVLGGTQSLHTNSFDEALGLPTDFSARIARNTQQIIQEESGVTRVIDPLGGSYYVEWLTDDIYERAWKYIQEIEEMGGMA 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   449 KAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAKLNHIRATRDAEKAQKALDA 528
Cdd:TIGR00641 401 KAIERGIPKLRIEEAAARTQARIDSGRQVIVGVNKYQLEEEDEVEVLKVDNSSVREEQIAKLKKLRAERDQEKVEAALDA 480
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 25144500   529 ITEGA-RGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAA 569
Cdd:TIGR00641 481 LTKAAeKEDENLLALAIDAARARATLGEITDALEKVFGEYRA 522
MM_CoA_mutase pfam01642
Methylmalonyl-CoA mutase; The enzyme methylmalonyl-CoA mutase is a member of a class of ...
52-556 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: 460279 [Multi-domain]  Cd Length: 503  Bit Score: 917.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500    52 TPEGIPIKPLYLRsdRDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFD 131
Cdd:pfam01642   2 TNEGIPVKPLYTP--EDLYEELGDSLPGEFPFTRGVYPTMYRGRPWTIRQYAGFGTAEETNERYRYLLAAGQTGLSVAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   132 LATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQN 211
Cdd:pfam01642  80 LPTQRGYDSDHPRAEGEVGKAGVAIDSLEDMETLFDGIPLDKVSVSMTINAPALPLLAMYIAAAEEQGVDPEKLRGTIQN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   212 DILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTID 291
Cdd:pfam01642 160 DILKEYIARGTYIYPPEPSMRLIADIIEYCAKNMPKWNTISISGYHIREAGATAVQELAFTLADGIEYVRALLEAGLDVD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   292 AFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVF 371
Cdd:pfam01642 240 EFAPRLSFFFAIGMNFFEEIAKFRAARRLWARIMKERFGAKNPKSLKLRFHAQTSGWSLTAQDPYNNILRTTTEAMAAVL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   372 GGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAV 451
Cdd:pfam01642 320 GGTQSLHTNPFDEALALPTEFSARIARNTQQILAEESGVTRVVDPLGGSYYVESLTDEIAEKAWALFQEIEELGGMLAAI 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   452 ASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAkVREEQCAKLNHIRATRDAEKAQKALDAITE 531
Cdd:pfam01642 400 ESGYPQREIAESAYRRQKAIASGKEVIVGVNKYPNEEEKPLEILRVDPE-VRERQAARLEALRAARDGARVKAALAALGN 478
                         490       500
                  ....*....|....*....|....*
gi 25144500   532 GARGNGNLMELAIEAARARCTVGEI 556
Cdd:pfam01642 479 AARGGENLMARAVFAANAYATLGEI 503
MM_CoA_mutase_ICM_like cd03680
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, isobutyryl-CoA ...
36-564 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 [Multi-domain]  Cd Length: 538  Bit Score: 752.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  36 AKKAMKGREADtltWNTPEGIPIKPLYLRSDR-DCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKF 114
Cdd:cd03680  12 WLKKFPERKEK---FTTLSGIPVKRVYTPADLpEDDYLEDIGYPGEYPFTRGVYPTMYRGRLWTMRQFAGFGTAEETNKR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 115 YKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVA 194
Cdd:cd03680  89 FKYLLEQGQTGLSVAFDLPTLMGYDSDHPMAEGEVGKVGVAIDTLADMEILFDGIPLDKVSTSMTINPPAAILLAMYIAV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 195 AEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIA 274
Cdd:cd03680 169 AEKQGVPLEKLRGTIQNDILKEYIAQKEWIFPPEPSVRLVTDIIEYCAKNVPKWNPISISGYHIREAGATAVQELAFTLA 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 275 DGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQD 354
Cdd:cd03680 249 DGIAYVEAVLERGLDVDEFAPRLSFFFNSHNDFFEEIAKFRAARRIWAKIMKERFGAKNPRSMMLRFHTQTAGASLTAQQ 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 355 PYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKA 434
Cdd:cd03680 329 PENNIVRTALQALAAVLGGTQSLHTNSFDEALALPTEEAVRIALRTQQIIAYESGVADVVDPLGGSYYVEALTDEIEEEA 408
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 435 LAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAkVREEQCAKLNHIR 514
Cdd:cd03680 409 WKYIDKIDAMGGMIKAIEDGYFQREIADAAYKYQKEIESGERIVVGVNKFVVEEEPPIILLKVDDE-VEERQIERLKEVR 487
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 25144500 515 ATRDAEKAQKALDAITEGARGNGNLMELAIEAARARCTVGEISDAMEKVF 564
Cdd:cd03680 488 AERDNAKVQEALDALRKAAEDEENLMPYIIEAVKAYATLGEICDVLREVF 537
MM_CoA_mutase cd00512
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM)-like family; contains ...
96-495 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 [Multi-domain]  Cd Length: 399  Bit Score: 577.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  96 PWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMS 175
Cdd:cd00512   1 PWTQRQLAGFGTAEETNKRYRRNLAAGQTGLSVAFDLPTLRGYDSDNPRDAGEVGMCGVAIDTLEDMDELFQGIPLEQTS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 176 VSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISG 255
Cdd:cd00512  81 VSMTINGPALPALALYVVVAERQGVDASDLAGTLQNDIIKEYIAQGTYIFPPEPSLRVLGDIIEYCSANIPKWNPVSISG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 256 YHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFsPKSDK 335
Cdd:cd00512 161 YHMQEAGATPVQELAYTLATGIEYVRACLERGLDVDEFAPRLSFFFGIGMNFFEEIAKLRAARRIWARITRDFG-GAEPK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 336 SMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVAD 415
Cdd:cd00512 240 SRRLRYHVQTSGRSLTAQQPYNNVARTSIQAMAATLGGAQSLHTNAYDEAIGLPTEFSARIALRTQQVLAEESGLARVID 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 416 PWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVL 495
Cdd:cd00512 320 PLGGSYYVEELTDSLEDAAWKEFQEIEKRGGMLKAVETGYVKGVIDESAAERQARIESGKQPIVGVNKYRMEEAPPIEPK 399
MM_CoA_mutase_MeaA cd03681
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, MeaA-like subfamily; ...
96-484 3.67e-105

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: 327.61  E-value: 3.67e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  96 PWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMS 175
Cdd:cd03681   1 PWIIRTYAGHSTAEESNELYRKNLAKGQTGLSVAFDLPTQTGYDSDHILAKGEVGKVGVPINHLGDMRILFNQIPLEQMN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 176 VSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISG 255
Cdd:cd03681  81 TSMTINATAMWLLSLYVAVAEEQGADVTALQGTTQNDIIKEYLSRGTYIFPPAPSLRLIVDMIEYCLKNIPKWNPMNICS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 256 YHMQEAGADAVLEMAFTIADGIQYCETGLNAG-LTIDAF---APRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSP 331
Cdd:cd03681 161 YHLQEAGATPVQELAFALATAIAVLDAVRDRNcFPEDEFedvVSRISFFVNAGIRFVEEMCKMRAFTELWDEITRDRYGI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 332 KSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMA---SVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEES 408
Cdd:cd03681 241 KDAKYRRFRYGVQVNSLGLTEQQPENNVWRILIEMLAvtlSKDARARAVQLPAWNEALGLPRPWDQQWSLRMQQVLAYET 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25144500 409 GICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKY 484
Cdd:cd03681 321 DLLEYDDLFDGSKVVEAKVEALKEEARAELQRILDMGGAVQAIENGYMKSQLVKSNAERLARIENNEMVIVGVNKW 396
MM_CoA_mutase_beta cd03677
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, Beta subunit-like ...
26-495 3.35e-102

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 [Multi-domain]  Cd Length: 424  Bit Score: 320.33  E-value: 3.35e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  26 SPIDQK-WAAMAKKAMKGREA-DTLTWNTPEGIPIKPLYLRSDrdcdaqrSVELPGQfpftrgpyPTMYTQRPWTIRQYA 103
Cdd:cd03677   2 PPVSREaWKAKVEKDLKGAPFeERLVWKTYDGITIKPLYTRED-------AAPLPPV--------PEGAAPGGWDVCQRI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 104 GFSTVEESNKFYKENIKAGQQGLSVAFDLAThrgydsdnprvfgdvgmagvavDSVEDMRQLFDGINLEKMSVSMTMNGA 183
Cdd:cd03677  67 DVPDAAEANEAALADLERGATALWLVLDNAG----------------------CSPEDLARLLEGVDLDLAPVYLDAGFL 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 184 VVPVLAMYVVAAEeagvSRKLLAGTIQNDILKEFMVrnTYIYPPEPSMRIIGDIFAytsREMPKFNSISISGYHMQEAGA 263
Cdd:cd03677 125 SLAAAAALLALVE----DRKALAGSLGLDPLGALAR--TGSLFLEPDLARLAELAA---RSAPGLRAITVDAVPYHNAGA 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 264 DAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKErFSPKSDKSMmlRTHS 343
Cdd:cd03677 196 TAAQELAYALAAAVEYLRALTEAGLDVEEAARQIEFRLAVGSDQFLEIAKLRALRLLWARIAEA-YGVPEARAA--RIHA 272
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 344 QTSGWSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMM 423
Cdd:cd03677 273 RTSRRNKTRYDPYVNMLRTTTEAFSAGLGGADSITVLPFDAALGLPDDFARRIARNTQLILKEESHLGRVADPAGGSYYI 352
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25144500 424 ESLTDEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVL 495
Cdd:cd03677 353 ESLTDQLAEKAWELFQEIEAAGGFVAALESGLIQKKIAESAAKRQKALATRKKPLTGVNEYPNLEEKPLERL 424
MM_CoA_mutase_1 cd03678
Coenzyme B12-dependent-methylmalonyl coenzyme A (CoA) mutase (MCM) family, unknown subfamily 1; ...
77-485 3.51e-93

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: 299.44  E-value: 3.51e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500  77 LPGQFPFTRGPYPTMYTQRPWTiRQYAGFSTVEESNKFYKEnIKAGQ--QGLSVAFDLATHRGYDSD-NPRVFGDVGMAG 153
Cdd:cd03678  63 VPGEFPFTAGVFPFKRTGEDPT-RMFAGEGTPERTNRRFHY-LSEGMpaKRLSTAFDSVTLYGEDPDpRPDIYGKIGNSG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 154 VAVDSVEDMRQLFDGINL--EKMSVSMTMNGAVVPVLAMYVVAA---------EEAGVSRKLLA---GTIQNDILKEFMV 219
Cdd:cd03678 141 VSVATLDDMKKLYSGFDLcaPNTSVSMTINGPAPMLLAFFLNTAidqqvekfrRENGIRAETLRsvrGTVQADILKEDQA 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 220 RNTYIYPPEPSMRIIGDIFAY-TSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLS 298
Cdd:cd03678 221 QNTCIFSTEFALRMMGDIQEYfIAHQVRNFYSVSISGYHIAEAGANPITQLAFTLANGFTYVEYYLSRGMHIDDFAPNLS 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 299 FFWGISMN-FYMEIAkmRAARRLWANLIKERFSpKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVFGGTQSL 377
Cdd:cd03678 301 FFFSNGLDpEYAVIG--RVARRIWARAMREKYG-ANERSQMLKYHIQTSGRSLHAQEIDFNDIRTTLQALYAIYDNCNSL 377
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 378 HTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAVASGMTK 457
Cdd:cd03678 378 HTNAYDEAITTPTEESVRRALAIQLIINRELGLAKNENPLQGSFIIEELTDLVEEAVLAEFERISERGGVLGAMETGYQR 457
                       410       420
                ....*....|....*....|....*...
gi 25144500 458 LKIEEAAAKKQARIDAGKDVIVGVNKYR 485
Cdd:cd03678 458 NKIQEESLYYESLKHDGELPIIGVNTFR 485
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
604-734 1.03e-69

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 [Multi-domain]  Cd Length: 132  Bit Score: 224.21  E-value: 1.03e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   604 RQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKL 683
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 25144500   684 GRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANL 734
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLL 131
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
607-728 7.26e-64

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 [Multi-domain]  Cd Length: 122  Bit Score: 208.22  E-value: 7.26e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 607 RIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLGRP 686
Cdd:cd02071   1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 25144500 687 DILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILE 728
Cdd:cd02071  81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
597-729 8.92e-61

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 200.37  E-value: 8.92e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 597 SFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQL 676
Cdd:COG2185   2 AFAEKTGRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPEL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 25144500 677 IGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEK 729
Cdd:COG2185  82 IELLKEAGAGDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLLEL 134
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
607-718 1.21e-39

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 [Multi-domain]  Cd Length: 119  Bit Score: 141.87  E-value: 1.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 607 RIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLGRP 686
Cdd:cd02067   1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 25144500 687 DILVVAGGVIPPQDYKELYDAGVALVFGPGTR 718
Cdd:cd02067  81 DIPVLVGGAIVTRDFKFLKEIGVDAYFGPATE 112
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
607-717 1.99e-25

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 [Multi-domain]  Cd Length: 125  Bit Score: 101.70  E-value: 1.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500 607 RIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLGRp 686
Cdd:cd02065   1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79
                        90       100       110
                ....*....|....*....|....*....|....*
gi 25144500 687 DILVVAGGVIPPQDYKE----LYDAGVALVFGPGT 717
Cdd:cd02065  80 DIPVVVGGAHPTADPEEpkvdAVVIGEGEYAGPAL 114
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
606-717 3.52e-17

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: 426713 [Multi-domain]  Cd Length: 121  Bit Score: 78.14  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144500   606 PRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLgR 685
Cdd:pfam02310   1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGI-R 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 25144500   686 PDILVVAGGVIPPQDYKELYDAGVAL---VFGPGT 717
Cdd:pfam02310  80 PRVKVVVGGPHPTFDPEELLEARPGVddvVFGEGE 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH