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Conserved domains on  [gi|1063532586|ref|WP_069395838|]
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cobalamin B12-binding domain-containing protein [Mycobacterium shimoidei]

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), ...
 4-125 5.00e-50

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: 155.44  E-value: 5.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:cd02071     1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRR 125
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), ...
 4-125 5.00e-50

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: 155.44  E-value: 5.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:cd02071     1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRR 125
Cdd:cd02071    81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 3-126 7.19e-50

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 155.30  E-value: 7.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:COG2185    11 PRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIELLKEAGA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063532586  83 GDIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRL 126
Cdd:COG2185    91 GDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLLEL 134
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
 3-129 4.22e-44

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: 140.63  E-value: 4.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:TIGR00640   3 PRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKLGR 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063532586  83 GDIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRLTGE 129
Cdd:TIGR00640  83 PDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEK 129
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
 4-126 1.25e-34

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 126.14  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:PRK09426  584 RILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLAAGHKTLVPALIEALKKLGRE 663

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRL 126
Cdd:PRK09426  664 DIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLEL 706
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 3-110 1.13e-20

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: 80.83  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:pfam02310   1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80

                          90       100
                  ....*....|....*....|....*...
gi 1063532586  83 gDIAVVVGGTIPEADVPKLLEAGAAAVF 110
Cdd:pfam02310  81 -RVKVVVGGPHPTFDPEELLEARPGVDD 107
 
Name Accession Description Interval E-value
MM_CoA_mut_B12_BD cd02071
methylmalonyl CoA mutase B12 binding domain. This domain binds to B12 (adenosylcobamide), ...
 4-125 5.00e-50

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: 155.44  E-value: 5.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:cd02071     1 RILVAKPGLDGHDRGAKVIARALRDAGFEVIYTGLRQTPEEIVEAAIQEDVDVIGLSSLSGGHMTLFPEVIELLRELGAG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRR 125
Cdd:cd02071    81 DILVVGGGIIPPEDYELLKEMGVAEIFGPGTSIEEIIDKIRD 122
Sbm COG2185
Methylmalonyl-CoA mutase, C-terminal domain/subunit (cobalamin-binding) [Lipid transport and ...
 3-126 7.19e-50

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


Pssm-ID: 441788 [Multi-domain]  Cd Length: 134  Bit Score: 155.30  E-value: 7.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:COG2185    11 PRVLLAKPGLDGHDRGAKVIARALRDAGFEVIYLGLFQTPEEIVRAAIEEDADVIGVSSLDGGHLELVPELIELLKEAGA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063532586  83 GDIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRL 126
Cdd:COG2185    91 GDILVVVGGVIPPEDIEALKAAGVDAVFGPGTDLEEIIEDLLEL 134
acid_CoA_mut_C TIGR00640
methylmalonyl-CoA mutase C-terminal domain; Methylmalonyl-CoA mutase (EC 5.4.99.2) catalyzes a ...
 3-129 4.22e-44

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: 140.63  E-value: 4.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:TIGR00640   3 PRILVAKMGQDGHDRGAKVIATALADLGFDVDYGPLFQTPEEIARQAVEADVHVVGVSSLAGGHLTLVPELIKELNKLGR 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063532586  83 GDIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRLTGE 129
Cdd:TIGR00640  83 PDILVVVGGVIPPQDYEELKEMGVAEVFGPGTPIPEIAIFVLKDIEK 129
PRK09426 PRK09426
methylmalonyl-CoA mutase; Reviewed
 4-126 1.25e-34

methylmalonyl-CoA mutase; Reviewed


Pssm-ID: 236508 [Multi-domain]  Cd Length: 714  Bit Score: 126.14  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:PRK09426  584 RILVAKMGQDGHDRGAKVIATAFADLGFDVDIGPLFQTPEEAARQAVENDVHVVGVSSLAAGHKTLVPALIEALKKLGRE 663

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGTSLEVLVRDIRRL 126
Cdd:PRK09426  664 DIMVVVGGVIPPQDYDFLYEAGVAAIFGPGTVIADAAIDLLEL 706
B12-binding cd02067
B12 binding domain (B12-BD). This domain binds different cobalamid derivates, like B12 ...
 4-114 1.79e-34

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: 115.68  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:cd02067     1 KVVIATVGGDGHDIGKNIVARALRDAGFEVIDLGVDVPPEEIVEAAKEEDADAIGLSGLLTTHMTLMKEVIEELKEAGLD 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063532586  84 DIAVVVGGTIPEADVPKLLEAGAAAVFPTGT 114
Cdd:cd02067    81 DIPVLVGGAIVTRDFKFLKEIGVDAYFGPAT 111
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
 4-125 3.78e-21

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: 82.05  E-value: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAg 83
Cdd:cd02065     1 KVLGATVGGDVHDIGKNIVAIALRDNGFEVIDLGVDVPPEEIVEAAKEEDADVVGLSALSTTHMEAMKLVIEALKELGI- 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063532586  84 DIAVVVGGTIP----EADVPKLLEAGAAAVFPTGTSLEVLVRDIRR 125
Cdd:cd02065    80 DIPVVVGGAHPtadpEEPKVDAVVIGEGEYAGPALLEVEGIAYRKN 125
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
 3-110 1.13e-20

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: 80.83  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   3 VRILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADA 82
Cdd:pfam02310   1 GKVVVATVGGDLHPLGLNYVAAALRAAGFEVIILGANVPPEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRP 80

                          90       100
                  ....*....|....*....|....*...
gi 1063532586  83 gDIAVVVGGTIPEADVPKLLEAGAAAVF 110
Cdd:pfam02310  81 -RVKVVVGGPHPTFDPEELLEARPGVDD 107
MtbC1 COG5012
Methanogenic corrinoid protein MtbC1 [Energy production and conversion];
4-125 1.64e-11

Methanogenic corrinoid protein MtbC1 [Energy production and conversion];


Pssm-ID: 444036 [Multi-domain]  Cd Length: 219  Bit Score: 59.14  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGAHLALTTRTVEALRAADAG 83
Cdd:COG5012    96 KVVIGTVEGDLHDIGKNIVADMLRAAGFEVIDLGADVPPEEFVEAAKEEKPDIVGLSALLTTTMPAMKELIEALREAGLR 175

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063532586  84 D-IAVVVGGTIPEADVPKllEAGAAAVFPTGTSLEVLVRDIRR 125
Cdd:COG5012   176 DkVKVIVGGAPVTEELAE--EIGADAYAEDAADAVELAKELLA 216
PRK02261 PRK02261
methylaspartate mutase subunit S; Provisional
 11-125 1.65e-08

methylaspartate mutase subunit S; Provisional


Pssm-ID: 179400 [Multi-domain]  Cd Length: 137  Bit Score: 49.56  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586  11 GLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGaHLALTTRTV-EALRAADAGDIAVVV 89
Cdd:PRK02261   12 GADCHAVGNKILDRALTEAGFEVINLGVMTSQEEFIDAAIETDADAILVSSLYG-HGEIDCRGLrEKCIEAGLGDILLYV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063532586  90 GGTI------PEADVPKLLEAGAAAVFPTGTSLEVLVRDIRR 125
Cdd:PRK02261   91 GGNLvvgkhdFEEVEKKFKEMGFDRVFPPGTDPEEAIDDLKK 132
Glm_B12_BD cd02072
B12 binding domain of glutamate mutase (Glm). Glutamate mutase catalysis the conversion of (S) ...
 5-125 5.24e-05

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: 40.14  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   5 ILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILSGaHLALTTRTV-EALRAADAG 83
Cdd:cd02072     2 IVLGVIGSDCHAVGNKILDHAFTEAGFNVVNLGVLSPQEEFIDAAIETDADAILVSSLYG-HGEIDCKGLrEKCDEAGLK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063532586  84 DIAVVVGGTIPE-----ADVPKLLEA-GAAAVFPTGTSLEVLVRDIRR 125
Cdd:cd02072    81 DILLYVGGNLVVgkqdfEDVEKRFKEmGFDRVFAPGTPPEEAIADLKK 128
methionine_synthase_B12_BD cd02069
B12 binding domain of methionine synthase. This domain binds methylcobalamin, which it uses as ...
 4-62 2.58e-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: 39.17  E-value: 2.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063532586   4 RILIAKPGLDGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSIL 62
Cdd:cd02069    90 KIVLATVKGDVHDIGKNLVGVILSNNGYEVIDLGVMVPIEKILEAAKEHKADIIGLSGL 148
MetH2 COG1410
Methionine synthase I, cobalamin-binding domain [Amino acid transport and metabolism]; ...
 13-91 4.06e-04

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: 38.78  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586   13 DGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILsgahlaLTT------RTVEALRAADAgDIA 86
Cdd:COG1410    725 DVHDIGKNIVGVVLENNGYEVIDLGVMVPAEKILEAAKEHKADIIGLSGL------MTTsldemkEVAEEMRRRGL-DIP 797


                   ....*
gi 1063532586   87 VVVGG 91
Cdd:COG1410    798 VLIGG 802
corrinoid_protein_B12-BD cd02070
B12 binding domain of corrinoid proteins. A family of small methanogenic corrinoid proteins ...
 13-91 1.16e-03

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: 37.22  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063532586  13 DGHDRGAKIVARTLRDAGFEVIYTGIRQRIEDIASVAVQEDVALVGLSILsgahlaLTT------RTVEALRAAD-AGDI 85
Cdd:cd02070    93 DIHDIGKNLVATMLEANGFEVIDLGRDVPPEEFVEAVKEHKPDILGLSAL------MTTtmggmkEVIEALKEAGlRDKV 166


                  ....*.
gi 1063532586  86 AVVVGG 91
Cdd:cd02070   167 KVMVGG 172
 
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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