Protein Family Models

Carboxymuconolactone decarboxylase (CMD) EC:4.1.1.44 is involved in protocatechuate catabolism. In some bacteria a gene fusion event leads to expression of CMD with a hydrolase involved in the same pathway [1]. In these bifunctional proteins (e.g. Swiss:O67982) CMD represents the C-terminal domain, Pfam:PF00561 represents the N-terminal domain. [1]. 9495744. Characterization of a protocatechuate catabolic gene cluster. from Rhodococcus opacus 1CP: evidence for a merged enzyme with. 4-carboxymuconolactone-decarboxylating and 3-oxoadipate. enol-lactone-hydrolyzing activity.. Eulberg D, Lakner S, Golovleva LA, Schlomann M;. J Bacteriol 1998;180:1072-1081.. [2]. 16597838. Crystal structure of the conserved protein TTHA0727 from Thermus. thermophilus HB8 at 1.9 A resolution: A CMD family member. distinct from carboxymuconolactone decarboxylase (CMD) and AhpD.. Ito K, Arai R, Fusatomi E, Kamo-Uchikubo T, Kawaguchi S, Akasaka. R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S;. Protein Sci. 2006;15:1187-1192. (from Pfam)

Date:

2024-08-14

CMD and perox_Avi_7169 domain-containing protein

Date:

2017-03-02

Members of this family represent a narrow clade that falls within a family of alkylhydroperoxidase-related proteins, fused to or adjacent to a sequence described by TIGR04029. These two partners occur almost always in the context of a putative FMN-dependent luciferase-like monooxygenase (LLM) (TIGR04027), and an ABC transporter in which TIGR04028 models the substrate-binding protein.

Date:

2021-09-10

Homology through a core region (see TIGR00778) shared with alkylhydroperoxidase AhpD, with the motif CxxCxxxHxxxxxxxG, suggests a peroxidase function. A number of homologs to this family are known to act as peroxidases or to correlate with resistance to oxidative stress. At least one member, from Myxococcus xanthus, is a selenoprotein, with an otherwise conserved Cys replaced by Sec.

Date:

2022-03-28

This HMM represents a 51-residue core region of homology among a family of mostly uncharacterized proteins of 110 to 227 amino acids. Most members of this family contain the motif EXXXXXX[SA]XXXXXC[VIL]XCXXXH. Members of the family include the alkylhydroperoxidase AhpD of Mycobacterium tuberculosis, a macrophage infectivity potentiator peptide of Legionella pneumophila, and an uncharacterized peptide in the tetrachloroethene reductive dehalogenase operon of Dehalospirillum multivorans. We suggest that many peptides containing this domain may have alkylhydroperoxidase or related antioxidant activity.

Date:

2024-05-30