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50  structures 2279  species 2  interactions 7804  sequences 78  architectures

Family: GMC_oxred_N (PF00732)

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.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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This family of proteins bind FAD as a cofactor.

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000172

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. One of these regions, located in the N-terminal section, corresponds to the FAD ADP- binding domain. The function of the other conserved domains is not yet known.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan NADP_Rossmann (CL0063), which contains the following 180 members:

2-Hacid_dh_C 3Beta_HSD 3HCDH_N adh_short adh_short_C2 ADH_zinc_N ADH_zinc_N_2 AdoHcyase_NAD AdoMet_MTase AlaDh_PNT_C Amino_oxidase ApbA AviRa Bac_GDH Bin3 CheR CMAS CmcI CoA_binding CoA_binding_2 CoA_binding_3 Cons_hypoth95 DAO DapB_N DFP DNA_circ_N DNA_methylase DOT1 DREV dTMP_synthase DUF1442 DUF1776 DUF2431 DUF268 DUF3321 DUF43 DUF633 DUF938 DXP_redisom_C DXP_reductoisom Eco57I ELFV_dehydrog Eno-Rase_FAD_bd Eno-Rase_NADH_b Enoyl_reductase Epimerase F420_oxidored FAD_binding_2 FAD_binding_3 FAD_oxidored Fibrillarin FMO-like FmrO FtsJ G-7-MTase G6PD_N GCD14 GDI GFO_IDH_MocA GIDA GidB GLF Glyco_hydro_4 GMC_oxred_N Gp_dh_N GRAS GRDA HI0933_like HIM1 IlvN K_oxygenase KR LCM Ldh_1_N Lycopene_cycl Malic_M Mannitol_dh Met_10 Methyltrans_Mon Methyltrans_SAM Methyltransf_10 Methyltransf_11 Methyltransf_12 Methyltransf_15 Methyltransf_16 Methyltransf_17 Methyltransf_18 Methyltransf_19 Methyltransf_2 Methyltransf_20 Methyltransf_21 Methyltransf_22 Methyltransf_23 Methyltransf_24 Methyltransf_25 Methyltransf_26 Methyltransf_27 Methyltransf_28 Methyltransf_29 Methyltransf_3 Methyltransf_30 Methyltransf_31 Methyltransf_32 Methyltransf_4 Methyltransf_5 Methyltransf_7 Methyltransf_8 Methyltransf_9 Methyltransf_PK MethyltransfD12 MetW Mg-por_mtran_C Mqo MT-A70 MTS Mur_ligase N2227 N6-adenineMlase N6_Mtase N6_N4_Mtase NAD_binding_10 NAD_binding_11 NAD_binding_2 NAD_binding_3 NAD_binding_4 NAD_binding_5 NAD_binding_7 NAD_binding_8 NAD_binding_9 NAD_Gly3P_dh_N NAS NmrA NNMT_PNMT_TEMT NodS Nol1_Nop2_Fmu Nol1_Nop2_Fmu_2 NSP13 OCD_Mu_crystall PARP_regulatory PCMT PDH Polysacc_synt_2 Pox_MCEL Prenylcys_lyase PrmA PRMT5 Pyr_redox Pyr_redox_2 Pyr_redox_3 RmlD_sub_bind Rossmann-like rRNA_methylase RrnaAD Rsm22 RsmJ Saccharop_dh SAM_MT SE Semialdhyde_dh Shikimate_DH Spermine_synth Strep_67kDa_ant TehB THF_DHG_CYH_C Thi4 ThiF TPMT TrkA_N TRM TRM13 tRNA_U5-meth_tr Trp_halogenase TylF Ubie_methyltran UDPG_MGDP_dh_N UPF0020 UPF0146 V_cholerae_RfbT XdhC_C YjeF_N

Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(20)
Full
(7804)
Representative proteomes NCBI
(7620)
Meta
(5057)
RP15
(1106)
RP35
(2163)
RP55
(3210)
RP75
(3835)
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Format an alignment

  Seed
(20)
Full
(7804)
Representative proteomes NCBI
(7620)
Meta
(5057)
RP15
(1106)
RP35
(2163)
RP55
(3210)
RP75
(3835)
Alignment:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(20)
Full
(7804)
Representative proteomes NCBI
(7620)
Meta
(5057)
RP15
(1106)
RP35
(2163)
RP55
(3210)
RP75
(3835)
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.

Pfam alignments:

HMM logo

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Trees

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: GMC_oxred;
Type: Domain
Author: Bateman A, Studholme, DJ
Number in seed: 20
Number in full: 7804
Average length of the domain: 264.90 aa
Average identity of full alignment: 27 %
Average coverage of the sequence by the domain: 47.78 %

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 20.5 20.5
Trusted cut-off 20.5 20.5
Noise cut-off 20.4 20.4
Model length: 296
Family (HMM) version: 14
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

GMC_oxred_C 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_N domain has been found. There are 50 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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