Protein Family Models for Protein (Select 446841975) - Protein Family Models

Select item 4227601.

This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif. (from Pfam)

Date:: 2024-08-14

Family Accession:: NF024891.5
Method:: HMM

Select item 4132412.

CobQ/CobB/MinD/ParA nucleotide binding domain

This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA Swiss:P29946 and CbiP Swiss:Q05597 from S.typhimurium [4], and CobQ Swiss:Q52686 from R. capsulatus [3]. These amidases catalyse amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria [4]. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family [6]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166. [2]. 9742226. Cobalamin (vitamin B12) biosynthesis: functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide. Raux E, Lanois A, Rambach A, Warren MJ, Thermes C;. Biochem J 1998;335:167-173. [3]. 7635831. Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. Pollich M, Klug G;. J Bacteriol 1995;177:4481-4487. [4]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM;. J Bacteriol 1993;175:3303-3316. [5]. 10966576. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of AT. TRUNCATED at 1650 bytes (from Pfam)

Date:: 2024-10-16

Family Accession:: NF013793.5
Method:: HMM

Select item 3999523.

new record, indexing in progress

Family Accession:

Select item 3902934.

new record, indexing in progress

Family Accession:

Select item 3638195.

new record, indexing in progress

Family Accession:

Select item 3480496.

new record, indexing in progress

Family Accession:

Select item 217707.

ATP-dependent dethiobiotin synthetase BioD

ATP-dependent dethiobiotin synthetase BioD catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring

Date:: 2024-08-20

Family Accession:: 10000625
Method:: Sparcle

Select item 184348.

dethiobiotin synthase

Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor.

Gene:: bioD

GO Terms:

Molecular Function:: magnesium ion binding (GO:0000287)

Molecular Function:: dethiobiotin synthase activity (GO:0004141)

Molecular Function:: ATP binding (GO:0005524)

Biological Process:: biotin biosynthetic process (GO:0009102)

Date:: 2024-05-30

Family Accession:: TIGR00347.1
Method:: HMM

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