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P18798 (MEMB_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methane monooxygenase component A beta chain
EC=1.14.13.25
Alternative name(s):
Methane hydroxylase
Gene names
Name:mmoY
Ordered Locus Names:MCA1195
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus ›

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Subunit structure

M.capsulatus 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 389388Methane monooxygenase component A beta chain
PRO_0000096407

Experimental info

Sequence conflict3701R → A in AAB62393. Ref.1

Secondary structure

1 ..................................................... 389
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18798 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 1737FEA30EEA9875

FASTA38945,133
        10         20         30         40         50         60 
MSMLGERRRG LTDPEMAAVI LKALPEAPLD GNNKMGYFVT PRWKRLTEYE ALTVYAQPNA 

        70         80         90        100        110        120 
DWIAGGLDWG DWTQKFHGGR PSWGNETTEL RTVDWFKHRD PLRRWHAPYV KDKAEEWRYT 

       130        140        150        160        170        180 
DRFLQGYSAD GQIRAMNPTW RDEFINRYWG AFLFNEYGLF NAHSQGAREA LSDVTRVSLA 

       190        200        210        220        230        240 
FWGFDKIDIA QMIQLERGFL AKIVPGFDES TAVPKAEWTN GEVYKSARLA VEGLWQEVFD 

       250        260        270        280        290        300 
WNESAFSVHA VYDALFGQFV RREFFQRLAP RFGDNLTPFF INQAQTYFQI AKQGVQDLYY 

       310        320        330        340        350        360 
NCLGDDPEFS DYNRTVMRNW TGKWLEPTIA ALRDFMGLFA KLPAGTTDKE EITASLYRVV 

       370        380 
DDWIEDYASR IDFKADRDQI VKAVLAGLK

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of methane monooxygenase from Methylococcus capsulatus (Bath)."
Stainthorpe A.C., Murrell J.C., Salmond G.P.C., Dalton H., Lees V.
Arch. Microbiol. 152:154-159(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41.
Strain: ATCC 33009 / NCIMB 11132 / Bath.
[2]McDonald I., Murrell J.C.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 142-145 AND C-TERMINUS.
[3]"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)."
Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. expand/collapse author list , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.
PLoS Biol. 2:1616-1628(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33009 / NCIMB 11132 / Bath.
[4]"Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane."
Rosenzweig A.C., Frederick C.A., Lippard S.J., Nordlund P.
Nature 366:537-543(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M90050 Genomic DNA. Translation: AAB62393.2.
AE017282 Genomic DNA. Translation: AAU92727.1.
PIRA61412.
JL0101.
RefSeqYP_113660.1. NC_002977.6.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYZX-ray2.15C/D1-389[»]
1FZ0X-ray2.07C/D1-389[»]
1FZ1X-ray1.96C/D1-389[»]
1FZ2X-ray2.15C/D1-389[»]
1FZ3X-ray2.03C/D1-389[»]
1FZ4X-ray2.38C/D1-389[»]
1FZ5X-ray2.40C/D1-389[»]
1FZ6X-ray2.05C/D1-389[»]
1FZ7X-ray1.96C/D1-389[»]
1FZ8X-ray2.10C/D1-389[»]
1FZ9X-ray2.30C/D1-389[»]
1FZHX-ray2.60C/D1-389[»]
1FZIX-ray3.30C/D1-389[»]
1MMOX-ray2.20B/C6-389[»]
1MTYX-ray1.70B/C6-389[»]
1XMFX-ray2.32C/D2-388[»]
1XMGX-ray2.10C/D2-388[»]
1XMHX-ray2.32C/D2-388[»]
1XU3X-ray2.30C/D1-389[»]
1XU5X-ray1.96C/D1-389[»]
1XVBX-ray1.80C/D1-389[»]
1XVCX-ray2.00C/D1-389[»]
1XVDX-ray2.30C/D1-389[»]
1XVEX-ray2.40C/D1-389[»]
1XVFX-ray2.00C/D1-389[»]
1XVGX-ray1.96C/D1-389[»]
4GAMX-ray2.90B/G/L/Q1-389[»]
ProteinModelPortalP18798.
SMRP18798. Positions 2-389.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59862N.
STRING243233.MCA1195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU92727; AAU92727; MCA1195.
GeneID3103426.
KEGGmca:MCA1195.
PATRIC22606222. VBIMetCap22254_1227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG268646.
HOGENOMHOG000086315.
KOK16158.
OMARRWHAPY.
ProtClustDBCLSK2395509.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3862.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFPIRSF000040. MMOH_comp. 1 hit.
SUPFAMSSF47240. Ferritin/RR_like. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP18798.

Entry information

Entry nameMEMB_METCA
AccessionPrimary (citable) accession number: P18798
Secondary accession number(s): Q609N7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 103 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents