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Conserved domains on  [gi|7245512|pdb|1CCW|A]
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Chain A, PROTEIN (GLUTAMATE MUTASE)

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
1-137 9.04e-89

methylaspartate mutase subunit S; Provisional


:

Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 254.10  E-value: 9.04e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A         1 MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
1CCW_A        81 AGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
 
Name Accession Description Interval E-value
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
1-137 9.04e-89

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 254.10  E-value: 9.04e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A         1 MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
1CCW_A        81 AGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
5-132 4.25e-85

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 [Multi-domain]  Cd Length: 128  Bit Score: 244.30  E-value: 4.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLE 84
Cdd:cd02072   1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGLREKCDEAGLK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1CCW_A       85 GILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKK 132
Cdd:cd02072  81 DILLYVGGNLVVGKQDFEDVEKRFKEMGFDRVFAPGTPPEEAIADLKK 128
MthylAspMutase TIGR01501
methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of ...
3-136 6.11e-82

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: 236.70  E-value: 6.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A          3 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAG 82
Cdd:TIGR01501   1 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNLGVLSPQEEFIKAAIETKADAILVSSLYGHGEIDCKGLRQKCDEAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
1CCW_A         83 LEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNI 136
Cdd:TIGR01501  81 LEGILLYVGGNLVVGKQDFPDVEKRFKEMGFDRVFAPGTPPEVVIADLKKDLNI 134
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
1-135 1.34e-43

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


Pssm-ID: 225096 [Multi-domain]  Cd Length: 143  Bit Score: 139.73  E-value: 1.34e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        1 MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDE 80
Cdd:COG2185  10 GARPRVLVAKLGLDGHDRGAKVIARALADAGFEVINLGLFQTPEEAVRAAVEEDVDVIGVSSLDGGHLTLVPGLVEALRE 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1CCW_A       81 AGLEGILLYVGGNIVVGKqhwpdvEKRFKDMGYDRVYAPGTPPEVGIADLKKDLN 135
Cdd:COG2185  90 AGVEDILVVVGGVIPPGD------YQELKEMGVDRIFGPGTPIEEALSDLLTRLG 138
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
5-128 1.57e-11

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: 57.33  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A          5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKcDEAGLE 84
Cdd:pfam02310   2 KVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRL-LKGIRP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
1CCW_A         85 GILLYVGGNIVVGKQHWPDVEKRFKDmgyDRVYAPGTPPEVGIA 128
Cdd:pfam02310  81 RVKVVVGGPHPTFDPEELLEARPGVD---DVVFGEGEDALEALL 121
 
Name Accession Description Interval E-value
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
1-137 9.04e-89

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 254.10  E-value: 9.04e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A         1 MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
1CCW_A        81 AGLEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNIE 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
5-132 4.25e-85

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 [Multi-domain]  Cd Length: 128  Bit Score: 244.30  E-value: 4.25e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLE 84
Cdd:cd02072   1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGLREKCDEAGLK 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1CCW_A       85 GILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKK 132
Cdd:cd02072  81 DILLYVGGNLVVGKQDFEDVEKRFKEMGFDRVFAPGTPPEEAIADLKK 128
MthylAspMutase TIGR01501
methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of ...
3-136 6.11e-82

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: 236.70  E-value: 6.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A          3 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAG 82
Cdd:TIGR01501   1 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNLGVLSPQEEFIKAAIETKADAILVSSLYGHGEIDCKGLRQKCDEAG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
1CCW_A         83 LEGILLYVGGNIVVGKQHWPDVEKRFKDMGYDRVYAPGTPPEVGIADLKKDLNI 136
Cdd:TIGR01501  81 LEGILLYVGGNLVVGKQDFPDVEKRFKEMGFDRVFAPGTPPEVVIADLKKDLNI 134
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
1-135 1.34e-43

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


Pssm-ID: 225096 [Multi-domain]  Cd Length: 143  Bit Score: 139.73  E-value: 1.34e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        1 MEKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDE 80
Cdd:COG2185  10 GARPRVLVAKLGLDGHDRGAKVIARALADAGFEVINLGLFQTPEEAVRAAVEEDVDVIGVSSLDGGHLTLVPGLVEALRE 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1CCW_A       81 AGLEGILLYVGGNIVVGKqhwpdvEKRFKDMGYDRVYAPGTPPEVGIADLKKDLN 135
Cdd:COG2185  90 AGVEDILVVVGGVIPPGD------YQELKEMGVDRIFGPGTPIEEALSDLLTRLG 138
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
5-132 1.70e-37

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: 123.38  E-value: 1.70e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLE 84
Cdd:cd02067   1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1CCW_A       85 GILLYVGGNIVVGKqhwpdvEKRFKDMGYDRVYAPGTppeVGIADLKK 132
Cdd:cd02067  81 DIPVLVGGAIVTRD------FKFLKEIGVDAYFGPAT---EAVEVLKK 119
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
5-132 3.44e-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 [Multi-domain]  Cd Length: 125  Bit Score: 100.15  E-value: 3.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLe 84
Cdd:cd02065   1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1CCW_A       85 GILLYVGGNIVVGKQHWPDVEkrFKDMGYDRVYAPGTPPEVGIADLKK 132
Cdd:cd02065  80 DIPVVVGGAHPTADPEEPKVD--AVVIGEGEYAGPALLEVEGIAYRKN 125
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
6-132 3.72e-14

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: 64.15  E-value: 3.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        6 IVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEG 85
Cdd:cd02071   2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAGD 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1CCW_A       86 ILLYVGGNIVvgkqhwPDVEKRFKDMGYDRVYAPGTPPEVGIADLKK 132
Cdd:cd02071  82 ILVVGGGIIP------PEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
6-134 6.38e-12

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: 58.58  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A          6 IVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEG 85
Cdd:TIGR00640   5 ILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKLGRPD 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
1CCW_A         86 ILLYVGGniVVGKQhwpDVEKRFKdMGYDRVYAPGTPPEVGIADLKKDL 134
Cdd:TIGR00640  85 ILVVVGG--VIPPQ---DYEELKE-MGVAEVFGPGTPIPEIAIFVLKDI 127
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
5-128 1.57e-11

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: 57.33  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A          5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKcDEAGLE 84
Cdd:pfam02310   2 KVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRL-LKGIRP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
1CCW_A         85 GILLYVGGNIVVGKQHWPDVEKRFKDmgyDRVYAPGTPPEVGIA 128
Cdd:pfam02310  81 RVKVVVGGPHPTFDPEELLEARPGVD---DVVFGEGEDALEALL 121
MtbC1 COG5012
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
5-92 3.23e-09

Methanogenic corrinoid protein MtbC1 [Energy production and conversion];


Pssm-ID: 227345 [Multi-domain]  Cd Length: 227  Bit Score: 52.72  E-value: 3.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        5 TIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLE 84
Cdd:COG5012 106 KVVIGTVEGDVHDIGKNIVATMLEAAGFEVIDLGRDVPVEEFVEKAKELKPDLVSMSALMTTTMIGMKDVIELLKEEGIR 185

                ....*....
1CCW_A       85 G-ILLYVGG 92
Cdd:COG5012 186 DkVIVMVGG 194
methionine_synthase_B12_BD cd02069
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ...
2-63 8.61e-08

B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as an intermediate methyl carrier from methyltetrahydrofolate (CH3H4folate) to homocysteine (Hcy).


Pssm-ID: 239020 [Multi-domain]  Cd Length: 213  Bit Score: 48.80  E-value: 8.61e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1CCW_A        2 EKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSL 63
Cdd:cd02069  87 SKGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGL 148
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
11-134 2.60e-07

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 47.94  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1CCW_A        11 IGSDCHAVGNKILDHAFTNAGFNVVnIGVL--SPQELfIKAAIETKADAILVSSLYGQGEIDCKGLRQKCDEAGLEGILL 88
Cdd:PRK09426 590 MGQDGHDRGAKVIATAFADLGFDVD-IGPLfqTPEEA-ARQAVENDVHVVGVSSLAAGHKTLVPALIEALKKLGREDIMV 667
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
1CCW_A        89 YVGGNIvvgkqhwPDVEKRF-KDMGYDRVYAPGTPpevgIADLKKDL 134
Cdd:PRK09426 668 VVGGVI-------PPQDYDFlYEAGVAAIFGPGTV----IADAAIDL 703
corrinoid_protein_B12-BD cd02070
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ...
2-63 1.07e-06

B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins that bind methyl-Co(III) 5-hydroxybenzimidazolylcobamide as a cofactor. They play a role on the methanogenesis from trimethylamine, dimethylamine or monomethylamine, which is initiated by a series of corrinoid-dependent methyltransferases.


Pssm-ID: 239021 [Multi-domain]  Cd Length: 201  Bit Score: 45.69  E-value: 1.07e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1CCW_A        2 EKKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSL 63
Cdd:cd02070  81 KKGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSAL 142
MetH2 COG1410
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism];
3-63 2.96e-06

Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism];


Pssm-ID: 224328 [Multi-domain]  Cd Length: 842  Bit Score: 45.03  E-value: 2.96e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1CCW_A        3 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNIGVLSPQELFIKAAIETKADAILVSSL 63
Cdd:COG1410 407 KGKIVIATVKGDVHDIGKNIVDVVLSCNGYEVVDLGVMVPAEKILEAAEEEKADIIGLSGL 467
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
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