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P27355

- MEMG_METTR

UniProt

P27355 - MEMG_METTR

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Protein
Methane monooxygenase component A gamma chain
Gene
mmoZ
Organism
Methylosinus trichosporium
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.

GO - Molecular functioni

  1. methane monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. methane metabolic process Source: InterPro
  2. one-carbon metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3869.

Names & Taxonomyi

Protein namesi
Recommended name:
Methane monooxygenase component A gamma chain (EC:1.14.13.25)
Alternative name(s):
Methane hydroxylase
Gene namesi
Name:mmoZ
OrganismiMethylosinus trichosporium
Taxonomic identifieri426 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 169168Methane monooxygenase component A gamma chain
PRO_0000096410Add
BLAST

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93
Helixi11 – 2111
Helixi26 – 4015
Turni49 – 535
Helixi54 – 7219
Helixi75 – 806
Helixi88 – 10013
Helixi105 – 11915
Turni120 – 1234
Helixi126 – 14419
Turni145 – 1495
Helixi153 – 1608
Beta strandi163 – 1675

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00G1-169[»]
1MHZX-ray2.70G1-169[»]
ProteinModelPortaliP27355.
SMRiP27355. Positions 2-168.

Miscellaneous databases

EvolutionaryTraceiP27355.

Family & Domainsi

Family and domain databases

Gene3Di1.20.1280.10. 1 hit.
1.20.1280.30. 1 hit.
InterProiIPR004222. Me_mOase_g.
IPR015952. Me_mOase_g_dom1.
IPR015953. Me_mOase_g_dom2.
[Graphical view]
PfamiPF02964. MeMO_Hyd_G. 1 hit.
[Graphical view]
PIRSFiPIRSF018503. Me_mOase_g. 1 hit.
ProDomiPD022203. Me_mOase_g. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF47152. SSF47152. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27355-1 [UniParc]FASTAAdd to Basket

« Hide

MAKREPIHDN SIRTEWEAKI AKLTSVDQAT KFIQDFRLAY TSPFRKSYDI    50
DVDYQYIERK IEEKLSVLKT EKLPVADLIT KATTGEDRAA VEATWIAKIK 100
AAKSKYEADG IHIEFRQLYK PPVLPVNVFL RTDAALGTVL MEIRNTDYYG 150
TPLEGLRKEP GVKVLHLQA 169
Length:169
Mass (Da):19,326
Last modified:January 23, 2007 - v3
Checksum:i460D4D8D234C2229
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55394 Genomic DNA. Translation: CAA39071.1.
PIRiS15210. C39049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55394 Genomic DNA. Translation: CAA39071.1 .
PIRi S15210. C39049.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MHY X-ray 2.00 G 1-169 [» ]
1MHZ X-ray 2.70 G 1-169 [» ]
ProteinModelPortali P27355.
SMRi P27355. Positions 2-168.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3869.

Miscellaneous databases

EvolutionaryTracei P27355.

Family and domain databases

Gene3Di 1.20.1280.10. 1 hit.
1.20.1280.30. 1 hit.
InterProi IPR004222. Me_mOase_g.
IPR015952. Me_mOase_g_dom1.
IPR015953. Me_mOase_g_dom2.
[Graphical view ]
Pfami PF02964. MeMO_Hyd_G. 1 hit.
[Graphical view ]
PIRSFi PIRSF018503. Me_mOase_g. 1 hit.
ProDomi PD022203. Me_mOase_g. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF47152. SSF47152. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b."
    Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.
    Mol. Microbiol. 5:335-342(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: OB3b.
  2. "Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction."
    Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.
    J. Biol. Chem. 266:540-550(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.

Entry informationi

Entry nameiMEMG_METTR
AccessioniPrimary (citable) accession number: P27355
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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