Annotation for this protein is in progress - please check future releases for more complete information



DP00379: Methane monooxygenase component CFASTA viewXML view

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



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.

Region 1: 99-107 Region 2: 131-146 Region 3: 163-172

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.


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:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)

References:
  1. 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:
 



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:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)

References:
  1. 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:
 



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:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 6.7; DTT 1 mM; NaN3 (0.1%); Pefabloc 2 mM; Sodium phosphate buffer 50 mM)

References:
  1. 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:
 



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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