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146  structures 2304  species 1  interaction 8000  sequences 92  architectures

Family: GMC_oxred_C (PF05199)

Summary: GMC oxidoreductase

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This is the Wikipedia entry entitled "Glucose-methanol-choline oxidoreductase family". More...

Glucose-methanol-choline oxidoreductase family Edit Wikipedia article

GMC oxidoreductase
PDB 3cox EBI.jpg
crystal structure of cholesterol oxidase complexed with a steroid substrate. implications for fad dependent alcohol oxidases
Identifiers
Symbol GMC_oxred_N
Pfam PF00732
Pfam clan CL0063
InterPro IPR000172
PROSITE PDOC00543
SCOP 1gal
SUPERFAMILY 1gal
OPM superfamily 140
OPM protein 1b4v
GMC oxidoreductase
PDB 1coy EBI.jpg
crystal structure of cholesterol oxidase complexed with a steroid substrate. implications for fad dependent alcohol oxidases
Identifiers
Symbol GMC_oxred_C
Pfam PF05199
InterPro IPR007867
PROSITE PDOC00543
SCOP 1gal
SUPERFAMILY 1gal

In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.

The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases.[1][2] These enzymes include a variety of proteins; choline dehydrogenase (CHD) EC 1.1.99.1, methanol oxidase (MOX) EC 1.1.3.13 and cellobiose dehydrogenase EC 1.1.99.18[3] which share a number of regions of sequence similarities. They contain two conserved protein domains. The N-terminal domain corresponds to the FAD ADP-binding domain, the C-terminal domain is a steroid-biding domain.[4][5]


References[edit]

  1. ^ Cavener DR (February 1992). "GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities". J. Mol. Biol. 223 (3): 811–4. doi:10.1016/0022-2836(92)90992-S. PMID 1542121. 
  2. ^ Li J, Vrielink A, Brick P, Blow DM (November 1993). "Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases". Biochemistry 32 (43): 11507–15. doi:10.1021/bi00094a006. PMID 8218217. 
  3. ^ Henriksson G, Johansson G, Pettersson G (March 2000). "A critical review of cellobiose dehydrogenases". J. Biotechnol. 78 (2): 93–113. doi:10.1016/S0168-1656(00)00206-6. PMID 10725534. 
  4. ^ Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE (2004). "Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp.". Biochemistry 43 (37): 11683–90. doi:10.1021/bi048609q. PMID 15362852. 
  5. ^ Vrielink A, Lloyd LF, Blow DM (1991). "Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution.". J Mol Biol 219 (3): 533–54. doi:10.1016/0022-2836(91)90192-9. PMID 2051487. 

This article incorporates text from the public domain Pfam and InterPro IPR000172

This article incorporates text from the public domain Pfam and InterPro IPR007867

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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This domain found associated with PF00732.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007867

The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases [PUBMED:1542121, PUBMED:8218217]. These enzymes include a variety of proteins; choline dehydrogenase (CHD), methanol oxidase (MOX) and cellobiose dehydrogenase (EC) [PUBMED:10725534] which share a number of regions of sequence similarities. The function of this C-terminal conserved domain is not yet known.

Gene Ontology

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Domain organisation

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Alignments

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(4016)
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RP35
(2161)
RP55
(3210)
RP75
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  Seed
(85)
Full
(8000)
Representative proteomes NCBI
(7618)
Meta
(4016)
RP15
(1059)
RP35
(2161)
RP55
(3210)
RP75
(3849)
Alignment:
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  Seed
(85)
Full
(8000)
Representative proteomes NCBI
(7618)
Meta
(4016)
RP15
(1059)
RP35
(2161)
RP55
(3210)
RP75
(3849)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_891 (release 2.1)
Previous IDs: none
Type: Domain
Author: Studholme DJ, Bateman, A
Number in seed: 85
Number in full: 8000
Average length of the domain: 132.70 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 23.46 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.4 24.4
Trusted cut-off 24.4 24.4
Noise cut-off 24.3 24.3
Model length: 144
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

GMC_oxred_N

Structures

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 GMC_oxred_C domain has been found. There are 146 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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