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Links from Protein

Items: 12

1.

4Fe-4S dicluster domain-containing protein

Date:
2024-08-14

Family Accession:
NF024585.5
Method:
HMM

2.

radical SAM protein

Radical SAM proteins catalyse diverse reactions, including unusual methylations, isomerisation, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. [1]. 11222759. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE;. Nucleic Acids Res 2001;29:1097-1106. [2]. 17335281. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification. Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O;. J Am Chem Soc. 2007;129:3462-3463. [3]. 16766528. A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. Berteau O, Guillot A, Benjdia A, Rabot S;. J Biol Chem. 2006;281:22464-22470. (from Pfam)

GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Molecular Function:
4 iron, 4 sulfur cluster binding (GO:0051539)
Date:
2024-10-16

Family Accession:
NF015983.5
Method:
HMM

3.

4Fe-4S binding protein

Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. (from Pfam)

Date:
2024-08-14

Family Accession:
NF012267.5
Method:
HMM

4.
new record, indexing in progress
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5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.

glycyl-radical enzyme activating protein

This subset of the radical-SAM family (PF04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA, [1]), benzylsuccinate synthase (BssD, [2]), gycerol dehydratase (DhaB2, [3]) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.

GO Terms:
Biological Process:
post-translational protein modification (GO:0043687)
Molecular Function:
4 iron, 4 sulfur cluster binding (GO:0051539)
Molecular Function:
S-adenosyl-L-methionine binding (GO:1904047)
Date:
2024-02-28

Family Accession:
TIGR02494.1
Method:
HMM

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