aminomethyltransferase family protein similar to human mitochondrial aminomethyltransferase (glycine cleavage system T protein), which is part of the glycine cleavage system that catalyzes the degradation of glycine
sarcosine oxidase, alpha subunit family, heterotetrameric form; This model describes the alpha ...
7-995
0e+00
sarcosine oxidase, alpha subunit family, heterotetrameric form; This model describes the alpha subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason.Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
Pssm-ID: 273584 [Multi-domain] Cd Length: 985 Bit Score: 1278.90 E-value: 0e+00
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and ...
607-998
9.27e-133
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and metabolism]; Glycine cleavage system protein T (aminomethyltransferase) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440173 [Multi-domain] Cd Length: 372 Bit Score: 404.85 E-value: 9.27e-133
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
615-877
2.60e-81
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.
Pssm-ID: 460255 Cd Length: 254 Bit Score: 264.07 E-value: 2.60e-81
sarcosine oxidase, alpha subunit family, heterotetrameric form; This model describes the alpha ...
7-995
0e+00
sarcosine oxidase, alpha subunit family, heterotetrameric form; This model describes the alpha subunit of a family of known and putative heterotetrameric sarcosine oxidases. Five operons of such oxidases are found in Mesorhizobium loti and three in Agrobacterium tumefaciens, a high enough copy number to suggest that not all members are share the same function. The model is designated as subfamily rather than equivalog for this reason.Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]
Pssm-ID: 273584 [Multi-domain] Cd Length: 985 Bit Score: 1278.90 E-value: 0e+00
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and ...
607-998
9.27e-133
Glycine cleavage system protein T (aminomethyltransferase) [Amino acid transport and metabolism]; Glycine cleavage system protein T (aminomethyltransferase) is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440173 [Multi-domain] Cd Length: 372 Bit Score: 404.85 E-value: 9.27e-133
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, ...
615-877
2.60e-81
Aminomethyltransferase folate-binding domain; This is a family of glycine cleavage T-proteins, part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes. GCV catalyzes the catabolism of glycine in eukaryotes. The T-protein is an aminomethyl transferase.
Pssm-ID: 460255 Cd Length: 254 Bit Score: 264.07 E-value: 2.60e-81
Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase ...
517-597
2.69e-36
Sarcosine oxidase A3 domain; This short domain is found in Heterotetrameric Sarcosine Oxidase's alpha A3 domain. This domain binds to FMN in sarcosine oxidase. This domain is related to pfam04324 but lacks its iron binding cysteine residues.
Pssm-ID: 375343 [Multi-domain] Cd Length: 87 Bit Score: 131.73 E-value: 2.69e-36
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
16-101
4.38e-25
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 99.54 E-value: 4.38e-25
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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