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[1]
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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).
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[2]
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PROTEIN SEQUENCE OF 2-12.
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).
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- 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.
- 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.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 169 AA [This is the length of the unprocessed precursor] |
Molecular weight: 19326 Da [This is the MW of the unprocessed precursor] |
CRC64: 460D4D8D234C2229 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAKREPIHDN SIRTEWEAKI AKLTSVDQAT KFIQDFRLAY TSPFRKSYDI DVDYQYIERK
70 80 90 100 110 120
IEEKLSVLKT EKLPVADLIT KATTGEDRAA VEATWIAKIK AAKSKYEADG IHIEFRQLYK
130 140 150 160
PPVLPVNVFL RTDAALGTVL MEIRNTDYYG TPLEGLRKEP GVKVLHLQA
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P27355 in FASTA format |
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