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Conserved domains on  [gi|663534881|gb|AIF24760|]
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cobalamin B12-binding domain-containing protein (mcmA2) [uncultured marine thaumarchaeote SAT1000_39_F02]

Protein Classification

cobalamin B12-binding domain-containing protein( domain architecture ID 10114614)

cobalamin B12-binding domain-containing protein similar to the C-terminal domain of Escherichia coli methylmalonyl-CoA mutase, and to the small subunits of Aquincola tertiaricarbonis 2-hydroxyisobutyryl-CoA mutase and Streptomyces cinnamonensis isobutyryl-CoA mutase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 11-132 1.89e-57

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: 174.32  E-value: 1.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGIK 90
Cdd:cd02071    1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663534881  91 DVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIRN 132
Cdd:cd02071   81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
 
Name Accession Description Interval E-value
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 11-132 1.89e-57

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: 174.32  E-value: 1.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGIK 90
Cdd:cd02071    1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663534881  91 DVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIRN 132
Cdd:cd02071   81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 4-131 2.34e-56

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 171.86  E-value: 2.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   4 KTTSRQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKE 83
Cdd:COG2185    5 EKTGRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIEL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 663534881  84 LRKKGIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIR 131
Cdd:COG2185   85 LKEAGAGDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLL 132
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
 8-139 3.21e-49

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: 154.11  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881    8 RQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKK 87
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 663534881   88 GIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIRNGVSKLRK 139
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD 132
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
 8-125 1.84e-38

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 137.31  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   8 RQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKK 87
Cdd:PRK09426 581 RRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLAAGHKTLVPALIEALKKL 660

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663534881  88 GIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVD 125
Cdd:PRK09426 661 GREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIAD 698
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 10-102 6.68e-23

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: 86.61  E-value: 6.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   10 IKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGi 89
Cdd:pfam02310   1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIR- 79

                          90
                  ....*....|...
gi 663534881   90 KDVLVVGGGTIPE 102
Cdd:pfam02310  80 PRVKVVVGGPHPT 92
 
Name Accession Description Interval E-value
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 11-132 1.89e-57

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: 174.32  E-value: 1.89e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGIK 90
Cdd:cd02071    1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 663534881  91 DVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIRN 132
Cdd:cd02071   81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 4-131 2.34e-56

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 171.86  E-value: 2.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   4 KTTSRQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKE 83
Cdd:COG2185    5 EKTGRRPRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIEL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 663534881  84 LRKKGIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIR 131
Cdd:COG2185   85 LKEAGAGDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLL 132
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
 8-139 3.21e-49

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: 154.11  E-value: 3.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881    8 RQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKK 87
Cdd:TIGR00640   1 RRPRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 663534881   88 GIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISHIRNGVSKLRK 139
Cdd:TIGR00640  81 GRPDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEKLLD 132
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
 11-129 1.62e-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: 128.78  E-value: 1.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGIK 90
Cdd:cd02067    1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663534881  91 DVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVDVISH 129
Cdd:cd02067   81 DIPVLVGGAIVTRDFKFLKEIGVDAYFGPATEAVEVLKK 119
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
 8-125 1.84e-38

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 137.31  E-value: 1.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   8 RQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKK 87
Cdd:PRK09426 581 RRPRILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLAAGHKTLVPALIEALKKL 660

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663534881  88 GIKDVLVVGGGTIPEEDKKSLEKSGVTGNFGPGTSLVD 125
Cdd:PRK09426 661 GREDIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIAD 698
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
 11-132 4.75e-27

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: 97.46  E-value: 4.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGIk 90
Cdd:cd02065    1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663534881  91 DVLVVGGGTIP----EEDKKSLEKSGVTGNFGPGTSLVDVISHIRN 132
Cdd:cd02065   80 DIPVVVGGAHPtadpEEPKVDAVVIGEGEYAGPALLEVEGIAYRKN 125
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 10-102 6.68e-23

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: 86.61  E-value: 6.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   10 IKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELRKKGi 89
Cdd:pfam02310   1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIR- 79

                          90
                  ....*....|...
gi 663534881   90 KDVLVVGGGTIPE 102
Cdd:pfam02310  80 PRVKVVVGGPHPT 92
MtbC1 COG5012
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
3-133 1.06e-08

Methanogenic corrinoid protein MtbC1 [Energy production and conversion];


Pssm-ID: 444036 [Multi-domain]  Cd Length: 219  Bit Score: 51.43  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   3 QKTTSRQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVK 82
Cdd:COG5012   88 AEEGGRKGKVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKELIE 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663534881  83 ELRKKGIKD--VLVVGGGTIPEEDKKSLeksGVTGNFGPGTSLVDVISHIRNG 133
Cdd:COG5012  168 ALREAGLRDkvKVIVGGAPVTEELAEEI---GADAYAEDAADAVELAKELLAE 217
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
 8-131 1.02e-07

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 47.64  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   8 RQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGaHGTLFPRVVKE-LRK 86
Cdd:PRK02261   2 KKKTVVLGVIGADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYG-HGEIDCRGLREkCIE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663534881  87 KGIKDVLVVGGGTI------PEEDKKSLEKSGVTGNFGPGTSLVDVISHIR 131
Cdd:PRK02261  81 AGLGDILLYVGGNLvvgkhdFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLK 131
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
 11-121 4.99e-06

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: 43.22  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGaHGTLFPRVVKE-LRKKGI 89
Cdd:cd02072    1 TIVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYG-HGEIDCKGLREkCDEAGL 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663534881  90 KDVLVVGGGTIP------EEDKKSLEKSGVTGNFGPGT 121
Cdd:cd02072   80 KDILLYVGGNLVvgkqdfEDVEKRFKEMGFDRVFAPGT 117
corrinoid_protein_B12-BD cd02070
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ...
 1-103 5.32e-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: 43.76  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881   1 MKQKTTSRQIKILVAKLGLDGHDRGALVLCRGFRDAGMEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRV 80
Cdd:cd02070   74 LGKSKSAKKGKVVIGTVEGDIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSALMTTTMGGMKEV 153

                         90       100
                 ....*....|....*....|....*
gi 663534881  81 VKELRKKGIKD--VLVVGGGTIPEE 103
Cdd:cd02070  154 IEALKEAGLRDkvKVMVGGAPVNQE 178
methionine_synthase_B12_BD cd02069
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ...
 11-100 3.58e-04

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: 38.78  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663534881  11 KILVAKLGLDGHDRG----ALVL-CRGFrdagmEVIYSGLFATPDRVAQIAEDEDVDAVALSLLNGAHGTLFPRVVKELR 85
Cdd:cd02069   90 KIVLATVKGDVHDIGknlvGVILsNNGY-----EVIDLGVMVPIEKILEAAKEHKADIIGLSGLLVPSLDEMVEVAEEMN 164

                         90
                 ....*....|....*
gi 663534881  86 KKGIKDVLVVGGGTI 100
Cdd:cd02069  165 RRGIKIPLLIGGAAT 179
 
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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