General information | DisProt: | DP00379 | Name: | Methane monooxygenase component C | Synonym(s): | MMOC_METCA
EC=1.14.13.25
Methane monooxygenase reductase
MMOR
Methane hydroxylase
| First appeared in release: | Release 3.0 (02/17/2006) | UniProt: | P22868 | UniGene: | | SwissProt: | MMOC_METCA | TrEMBL: | | NCBI (GI): | 18266834 | Source organism: | Methylococcus capsulatus | Sequence length: | 348 | Percent disordered: | 10% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MQRVHTITAV TEDGESLRFE CRSDEDVITA ALRQNIFLMS SCREGGCATC KALCSEGDYD - 60 LKGCSVQALP PEEEEEGLVL LCRTYPKTDL EIELPYTHCR ISFGEVGSFE AEVVGLNWVS - 120 SNTVQFLLQK RPDECGNRGV KFEPGQFMDL TIPGTDVSRS YSPANLPNPE GRLEFLIRVL - 180 PEGRFSDYLR NDARVGQVLS VKGPLGVFGL KERGMAPRYF VAGGTGLAPV VSMVRQMQEW - 240 TAPNETRIYF GVNTEPELFY IDELKSLERS MRNLTVKACV WHPSGDWEGE QGSPIDALRE - 300 DLESSDANPD IYLCGPPGMI DAACELVRSR GIPGEQVFFE KFLPSGAA
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Functional narrative |
Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. The component C is the iron-sulfur flavoprotein of sMMO.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 99 - 107 | Length: | 9 | Region sequence: |
CRISFGEVG | Modification type: | Fragment
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Entropic chain
| Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)
| References:
- Chatwood LL, Müller J, Gross JD, Wagner G, Lippard SJ. "NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)." Biochemistry. 2004; 43(38): 11983-91. PubMed: 15379538
| Comments:
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Region 2 | Type: | Disordered | Name: | | Location: | 131 - 146 | Length: | 16 | Region sequence: |
RPDECGNRGVKFEPGQ | Modification type: | Fragment
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)
| References:
- Chatwood LL, Müller J, Gross JD, Wagner G, Lippard SJ. "NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)." Biochemistry. 2004; 43(38): 11983-91. PubMed: 15379538
| Comments:
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Region 3 | Type: | Disordered | Name: | | Location: | 163 - 172 | Length: | 10 | Region sequence: |
PANLPNPEGR | Modification type: | Fragment
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)
| References:
- Chatwood LL, Müller J, Gross JD, Wagner G, Lippard SJ. "NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)." Biochemistry. 2004; 43(38): 11983-91. PubMed: 15379538
| Comments:
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Comments |
The fragment used to determine the disordered regions was the 250 residue FAD/NADH binding domain of MMOR. (NCBI: 56554015)
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