Summary: MaoC like domain
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MaoC like domain Provide feedback
The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase . The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity . This domain is also present in the NodN nodulation protein N.
Sugino H, Sasaki M, Azakami H, Yamashita M, Murooka Y , J Bacteriol 1992;174:2485-2492.: A monoamine-regulated Klebsiella aerogenes operon containing the monoamine oxidase structural gene (maoA) and the maoC gene. PUBMED:8647101 EPMC:8647101
Fukui T, Shiomi N, Doi Y; , J Bacteriol. 1998;180:667-673.: Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. PUBMED:9457873 EPMC:9457873
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002539The C terminus of the MaoC protein is found to share similarity with a wide variety of enzymes. All these enzymes contain multiple domains. This domain is found in parts of two enzymes that have been assigned dehydratase activities. A deletion mutant of the C-terminal 271 amino acids in SWISSPROT abolished its 2-enoyl-CoA hydratase activity, suggesting that this region may be a hydratase enzyme [PUBMED:9891075]. The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [PUBMED:1556068].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||metabolic process (GO:0008152)|
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The HotDog fold was first observed in the structure of Escherichia coli beta-hydroxydecanoyl thiol ester dehydratase (FabA), where Leesong et al. noticed that each subunit of this dimeric enzyme contained a mixed alpha + beta 'hot dog' fold. They described the seven-stranded antiparallel beta-sheet as the 'bun', which wraps around a five-turn alpha-helical 'sausage', This superfamily contains a diverse range of enzymes. Membership includes numerous prokaryotic, archaeal and eukaryotic proteins involved in several related, but distinct, catalytic activities, from metabolic roles such as thioester hydrolysis in fatty acid metabolism, to degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. The superfamily also includes FapR, a non-catalytic bacterial homologue that is involved in transcriptional regulation of fatty acid biosynthesis .
The clan contains the following 13 members:4HBT 4HBT_2 4HBT_3 Acyl-ACP_TE Acyl_CoA_thio AfsA DUF4442 FabA FcoT MaoC_dehydrat_N MaoC_dehydratas PS-DH YiiD_Cterm
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Curation and family details
|Seed source:||Pfam-B_297 (release 4.0)|
|Author:||Bashton M, Bateman A|
|Number in seed:||32|
|Number in full:||6997|
|Average length of the domain:||119.40 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||29.77 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MaoC_dehydratas domain has been found. There are 72 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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