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Conserved domains on  [gi|740853680|ref|WP_038638933|]
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MULTISPECIES: methylaspartate mutase subunit S [Citrobacter]

Protein Classification

methylaspartate mutase subunit S( domain architecture ID 10011783)

methylaspartate mutase subunit S is part of the enzyme complex that catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate)

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 1.08e-80

methylaspartate mutase subunit S; Provisional


:

Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 234.07  E-value: 1.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   1 MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680  81 RGLGDILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHDLEDVCALIANDIHQH 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
 
Name Accession Description Interval E-value
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
 1-137 1.08e-80

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 234.07  E-value: 1.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   1 MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680  81 RGLGDILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHDLEDVCALIANDIHQH 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
MthylAspMutase TIGR01501
methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of ...
 3-136 2.75e-72

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: 212.81  E-value: 2.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680    3 KSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERG 82
Cdd:TIGR01501   1 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNLGVLSPQEEFIKAAIETKADAILVSSLYGHGEIDCKGLRQKCDEAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 740853680   83 LGDILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHDLEDVCALIANDIHQ 136
Cdd:TIGR01501  81 LEGILLYVGGNLVVGKQDFPDVEKRFKEMGFDRVFAPGTPPEVVIADLKKDLNI 134
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
 5-131 2.68e-71

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: 210.01  E-value: 2.68e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERGLG 84
Cdd:cd02072    1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGLREKCDEAGLK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 740853680  85 DILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHD-LEDVCALIA 131
Cdd:cd02072   81 DILLYVGGNLVVGKQDFEDVEKRFKEMGFDRVFAPGTPpEEAIADLKK 128
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 1-137 2.50e-36

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 121.79  E-value: 2.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   1 MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIE 80
Cdd:COG2185    8 GRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIELLKE 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680  81 RGLGDILLYVGGNLVvgkhdfADVEVKFKEMGFNRVFAPSHDLEDvcalIANDIHQH 137
Cdd:COG2185   88 AGAGDILVVVGGVIP------PEDIEALKAAGVDAVFGPGTDLEE----IIEDLLEL 134
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 5-95 1.21e-10

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: 55.41  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680    5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERcIERGLG 84
Cdd:pfam02310   2 KVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRL-LKGIRP 80

                          90
                  ....*....|.
gi 740853680   85 DILLYVGGNLV 95
Cdd:pfam02310  81 RVKVVVGGPHP 91
 
Name Accession Description Interval E-value
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
 1-137 1.08e-80

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 234.07  E-value: 1.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   1 MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIE 80
Cdd:PRK02261   1 MKKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYGHGEIDCRGLREKCIE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680  81 RGLGDILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHDLEDVCALIANDIHQH 137
Cdd:PRK02261  81 AGLGDILLYVGGNLVVGKHDFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKKDLNQR 137
MthylAspMutase TIGR01501
methylaspartate mutase, S subunit; This model represents the S (sigma) subunit of ...
 3-136 2.75e-72

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: 212.81  E-value: 2.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680    3 KSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERG 82
Cdd:TIGR01501   1 KKTIVLGVIGSDCHAVGNKILDHAFTNAGFNVVNLGVLSPQEEFIKAAIETKADAILVSSLYGHGEIDCKGLRQKCDEAG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 740853680   83 LGDILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHDLEDVCALIANDIHQ 136
Cdd:TIGR01501  81 LEGILLYVGGNLVVGKQDFPDVEKRFKEMGFDRVFAPGTPPEVVIADLKKDLNI 134
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
 5-131 2.68e-71

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: 210.01  E-value: 2.68e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERGLG 84
Cdd:cd02072    1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYGHGEIDCKGLREKCDEAGLK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 740853680  85 DILLYVGGNLVVGKHDFADVEVKFKEMGFNRVFAPSHD-LEDVCALIA 131
Cdd:cd02072   81 DILLYVGGNLVVGKQDFEDVEKRFKEMGFDRVFAPGTPpEEAIADLKK 128
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 1-137 2.50e-36

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 121.79  E-value: 2.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   1 MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIE 80
Cdd:COG2185    8 GRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIELLKE 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680  81 RGLGDILLYVGGNLVvgkhdfADVEVKFKEMGFNRVFAPSHDLEDvcalIANDIHQH 137
Cdd:COG2185   88 AGAGDILVVVGGVIP------PEDIEALKAAGVDAVFGPGTDLEE----IIEDLLEL 134
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
 5-122 8.87e-33

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: 112.21  E-value: 8.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERGLG 84
Cdd:cd02067    1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 740853680  85 DILLYVGGNLVVGKHDFAdvevkfKEMGFNRVFAPSHD 122
Cdd:cd02067   81 DIPVLVGGAIVTRDFKFL------KEIGVDAYFGPATE 112
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
 5-119 1.11e-20

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: 81.28  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERGLg 84
Cdd:cd02065    1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 740853680  85 DILLYVGGNLVVGKHDfaDVEVKFKEMGFNRVFAP 119
Cdd:cd02065   80 DIPVVVGGAHPTADPE--EPKVDAVVIGEGEYAGP 112
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 5-95 1.21e-10

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: 55.41  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680    5 TLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERcIERGLG 84
Cdd:pfam02310   2 KVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRL-LKGIRP 80

                          90
                  ....*....|.
gi 740853680   85 DILLYVGGNLV 95
Cdd:pfam02310  81 RVKVVVGGPHP 91
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 6-132 7.15e-10

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: 53.37  E-value: 7.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   6 LVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIERGLGD 85
Cdd:cd02071    2 ILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAGD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 740853680  86 ILLYVGGnlVVGKHDFADVevkfKEMGFNRVFAPSHDLEDVCALIAN 132
Cdd:cd02071   82 ILVVGGG--IIPPEDYELL----KEMGVAEIFGPGTSIEEIIDKIRD 122
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
 2-137 9.70e-09

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: 50.49  E-value: 9.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680    2 KKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIER 81
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 740853680   82 GLGDILLYVGGnlVVGKHDFAdvevKFKEMGFNRVFAPSHDLEDVCALIANDIHQH 137
Cdd:TIGR00640  81 GRPDILVVVGG--VIPPQDYE----ELKEMGVAEVFGPGTPIPEIAIFVLKDIEKL 130
MtbC1 COG5012
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
2-103 2.02e-08

Methanogenic corrinoid protein MtbC1 [Energy production and conversion];


Pssm-ID: 444036 [Multi-domain]  Cd Length: 219  Bit Score: 51.05  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   2 KKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVSSIYGHGDIDCLGLRERCIER 81
Cdd:COG5012   93 RKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKELIEALREA 172

                         90       100
                 ....*....|....*....|...
gi 740853680  82 GLGD-ILLYVGGNLVvgKHDFAD 103
Cdd:COG5012  173 GLRDkVKVIVGGAPV--TEELAE 193
methionine_synthase_B12_BD cd02069
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ...
 3-61 2.52e-07

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: 48.03  E-value: 2.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 740853680   3 KSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVS 61
Cdd:cd02069   88 KGKIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLS 146
corrinoid_protein_B12-BD cd02070
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ...
 2-61 2.87e-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: 44.92  E-value: 2.87e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 740853680   2 KKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAIVVS 61
Cdd:cd02070   81 KKGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLS 140
MetH2 COG1410
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ...
 2-58 5.69e-06

Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; Methionine synthase I, cobalamin-binding domain is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 441020 [Multi-domain]  Cd Length: 1141  Bit Score: 44.94  E-value: 5.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 740853680    2 KKSTLVIGVIGADCHAVGNKVLDRVFTAHDFHVINLGVMVSQDEYIDAAIETGADAI 58
Cdd:COG1410   713 SKGKIVLATVKGDVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADII 769
metH PRK09490
B12-dependent methionine synthase; Provisional
 32-61 2.38e-04

B12-dependent methionine synthase; Provisional


Pssm-ID: 236539 [Multi-domain]  Cd Length: 1229  Bit Score: 40.16  E-value: 2.38e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 740853680   32 FHVINLGVMVSQDEYIDAAIETGADAIVVS 61
Cdd:PRK09490  780 YEVIDLGVMVPAEKILETAKEENADIIGLS 809
 
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.
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