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UniProtKB/Swiss-Prot entry P27353

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MEMA_METTR
Primary accession number P27353
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Methane monooxygenase component A alpha chain
Synonyms EC 1.14.13.25
Methane hydroxylase
Gene name
Name: mmoX
From
Methylosinus trichosporium [TaxID: 426] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Methylocystaceae; Methylosinus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=OB3b;
PubMed=1904125 [NCBI, ExPASy, EBI, Israel, Japan]
Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.;
"Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b.";
Mol. Microbiol. 5:335-342(1991).
[2]
 SEQUENCE REVISION.
McDonald I.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
 PROTEIN SEQUENCE OF 2-16.
PubMed=1845980 [NCBI, ExPASy, EBI, Israel, Japan]
Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.;
"Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction.";
J. Biol. Chem. 266:540-550(1991).
Comments
  • FUNCTION: 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.
  • CATALYTIC ACTIVITY: Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.
  • COFACTOR: Binds 2 iron ions.
  • SUBUNIT: M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X55394; CAA39068.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15207; S15207.
3D structure databases
PDB
1MHY; X-ray; 2.00 A; D=17-526.[ExPASy / RCSB / EBI]
1MHZ; X-ray; 2.70 A; D=17-526.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1MHY; -.
1MHZ; -.
ModBase P27353.
Ontologies
GO
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0015049; Molecular function: methane monooxygenase activity (inferred from electronic annotation from EC).
GO:0006725; Biological process: cellular aromatic compound metabolic process (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR003430; Phenol_Hydrox.
IPR012348; Ribncl_red_rel.
Graphical view of domain structure.
Gene3D G3DSA:1.10.620.20; Ribncl_red_rel; 1.
Pfam PF02332; Phenol_Hydrox; 1.
Pfam graphical view of domain structure.
BLOCKS P27353.
ProtoNet P27353.
Other
LinkHub P27353; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Iron; Metal-binding; Monooxygenase; NADP; One-carbon metabolism; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   526  525     Methane monooxygenase component A alpha chain. PRO_0000096406
ACT_SITE   151   151        Potential. 
METAL   114   114        Iron 1 (By similarity). 
METAL   144   144        Iron 1 (By similarity). 
METAL   147   147        Iron 1 (By similarity). 
METAL   209   209        Iron 2 (By similarity). 
METAL   243   243        Iron 2 (By similarity). 
METAL   246   246        Iron 2 (By similarity). 
HELIX   25    29  5      
HELIX   30    35  6      
HELIX   64    83  20      
HELIX   85    88  4      
HELIX   91    93  3      
HELIX   97   127  31      
HELIX   131   161  31      
TURN   166   170  5      
HELIX   171   174  4      
HELIX   175   177  3      
HELIX   179   188  10      
HELIX   190   193  4      
HELIX   197   204  8      
TURN   205   207  3      
HELIX   208   211  4      
HELIX   213   226  14      
HELIX   231   257  27      
HELIX   261   292  32      
HELIX   301   308  8      
HELIX   309   315  7      
HELIX   316   320  5      
HELIX   321   324  4      
HELIX   332   338  7      
TURN   339   341  3      
HELIX   342   352  11      
HELIX   354   356  3      
STRAND   357   360  4      
HELIX   366   375  10      
TURN   377   382  6      
HELIX   383   393  11      
TURN   394   396  3      
HELIX   398   400  3      
HELIX   404   410  7      
TURN   419   421  3      
TURN   427   429  3      
STRAND   437   441  5      
STRAND   444   448  5      
HELIX   451   459  9      
HELIX   461   463  3      
HELIX   469   473  5      
HELIX   478   484  7      
STRAND   492   496  5      
STRAND   498   500  3      
HELIX   509   514  6      
HELIX   522   525  4      
Sequence information
Length: 526 AA [This is the length of the unprocessed precursor] Molecular weight: 59954 Da [This is the MW of the unprocessed precursor] CRC64: A56F4AAD0A55726B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAISLATKAA TDALKVNRAP VGVEPQEVHK WLQSFNWDFK ENRTKYPTKY HMANETKEQF 

        70         80         90        100        110        120 
KVIAKEYARM EAAKDERQFG TLLDGLTRLG AGNKVHPRWG ETMKVISNFL EVGEYNAIAA 

       130        140        150        160        170        180 
SAMLWDSATA AEQKNGYLAQ VLDEIRHTHQ CAFINHYYSK HYHDPAGHND ARRTRAIGPL 

       190        200        210        220        230        240 
WKGMKRVFAD GFISGDAVEC SVNLQLVGEA CFTNPLIVAV TEWASANGDE ITPTVFLSVE 

       250        260        270        280        290        300 
TDELRHMANG YQTVVSIAND PASAKFLNTD LNNAFWTQQK YFTPVLGYLF EYGSKFKVEP 

       310        320        330        340        350        360 
WVKTWNRWVY EDWGGIWIGR LGKYGVESPA SLRDAKRDAY WAHHDLALAA YAMWPLGFAR 

       370        380        390        400        410        420 
LALPDEEDQA WFEANYPGWA DHYGKIFNEW KKLGYEDPKS GFIPYQWLLA NGHDVYIDRV 

       430        440        450        460        470        480 
SQVPFIPSLA KGTGSLRVHE FNGKKHSLTD DWGERQWLIE PERYECHNVF EQYEGRELSE 

       490        500        510        520 
VIAEGHGVRS DGKTLIAQPH TRGDNLWTLE DIKRAGCVFP DPLAKF
P27353 in FASTA format

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