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P22869 (MEMA_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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 alpha chain

EC=1.14.13.25
Alternative name(s):
Methane hydroxylase
Gene names
Name:mmoX
Ordered Locus Names:MCA1194
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
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.

Cofactor

Binds 2 iron ions.

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

Chain1 – 527527Methane monooxygenase component A alpha chain
PRO_0000096405

Sites

Active site1511 Potential
Metal binding1141Iron 1
Metal binding1441Iron 1
Metal binding1471Iron 1
Metal binding2091Iron 2
Metal binding2431Iron 2
Metal binding2461Iron 2

Experimental info

Sequence conflict3061N → D in AAB62392. Ref.2
Sequence conflict4441Q → E in AAB62392. Ref.2

Secondary structure

.................................................................................. 527
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22869 [UniParc].

Last modified December 7, 2004. Version 3.
Checksum: 953438FDF5208374

FASTA52760,646
        10         20         30         40         50         60 
MALSTATKAA TDALAANRAP TSVNAQEVHR WLQSFNWDFK NNRTKYATKY KMANETKEQF 

        70         80         90        100        110        120 
KLIAKEYARM EAVKDERQFG SLQDALTRLN AGVRVHPKWN ETMKVVSNFL EVGEYNAIAA 

       130        140        150        160        170        180 
TGMLWDSAQA AEQKNGYLAQ VLDEIRHTHQ CAYVNYYFAK NGQDPAGHND ARRTRTIGPL 

       190        200        210        220        230        240 
WKGMKRVFSD GFISGDAVEC SLNLQLVGEA CFTNPLIVAV TEWAAANGDE ITPTVFLSIE 

       250        260        270        280        290        300 
TDELRHMANG YQTVVSIAND PASAKYLNTD LNNAFWTQQK YFTPVLGMLF EYGSKFKVEP 

       310        320        330        340        350        360 
WVKTWNRWVY EDWGGIWIGR LGKYGVESPR SLKDAKQDAY WAHHDLYLLA YALWPTGFFR 

       370        380        390        400        410        420 
LALPDQEEME WFEANYPGWY DHYGKIYEEW RARGCEDPSS GFIPLMWFIE NNHPIYIDRV 

       430        440        450        460        470        480 
SQVPFCPSLA KGASTLRVHE YNGQMHTFSD QWGERMWLAE PERYECQNIF EQYEGRELSE 

       490        500        510        520 
VIAELHGLRS DGKTLIAQPH VRGDKLWTLD DIKRLNCVFK NPVKAFN 

« Hide

References

« Hide 'large scale' references
[1]"The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)."
Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.
Gene 91:27-34(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6.
Strain: ATCC 33009 / NCIMB 11132 / Bath.
[2]McDonald I., Murrell J.C.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 84; 306 AND 444.
[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).
[5]"Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states."
Rosenzweig A.C., Nordlund P., Takahara P.M., Frederick C.A., Lippard S.J.
Chem. Biol. 2:409-418(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[6]"Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions."
Rosenzweig A.C., Brandstetter H., Whittington D.A., Nordlund P., Lippard S.J., Frederick C.A.
Proteins 29:141-152(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Strain: ATCC 33009 / NCIMB 11132 / Bath.
[7]"Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site."
Whittington D.A., Lippard S.J.
J. Am. Chem. Soc. 123:827-838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
Strain: ATCC 33009 / NCIMB 11132 / Bath.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90050 Genomic DNA. Translation: AAB62392.3.
AE017282 Genomic DNA. Translation: AAU92736.1.
PIRJQ0702.
RefSeqYP_113659.1. NC_002977.6.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYZX-ray2.15A/B1-527[»]
1FZ0X-ray2.07A/B1-527[»]
1FZ1X-ray1.96A/B1-527[»]
1FZ2X-ray2.15A/B1-527[»]
1FZ3X-ray2.03A/B1-527[»]
1FZ4X-ray2.38A/B1-527[»]
1FZ5X-ray2.40A/B1-527[»]
1FZ6X-ray2.05A/B1-527[»]
1FZ7X-ray1.96A/B1-527[»]
1FZ8X-ray2.10A/B1-527[»]
1FZ9X-ray2.30A/B1-527[»]
1FZHX-ray2.60A/B1-527[»]
1FZIX-ray3.30A/B1-527[»]
1MMOX-ray2.20D/E15-526[»]
1MTYX-ray1.70D/E15-526[»]
1XMFX-ray2.32A/B1-527[»]
1XMGX-ray2.10A/B1-527[»]
1XMHX-ray2.32A/B1-527[»]
1XU3X-ray2.30A/B1-527[»]
1XU5X-ray1.96A/B1-527[»]
1XVBX-ray1.80A/B1-527[»]
1XVCX-ray2.00A/B1-527[»]
1XVDX-ray2.30A/B1-527[»]
1XVEX-ray2.40A/B1-527[»]
1XVFX-ray2.00A/B1-527[»]
1XVGX-ray1.96A/B1-527[»]
4GAMX-ray2.90A/F/K/P1-527[»]
ProteinModelPortalP22869.
SMRP22869. Positions 15-526.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59861N.
STRING243233.MCA1194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU92736; AAU92736; MCA1194.
GeneID3104807.
KEGGmca:MCA1194.
PATRIC22606220. VBIMetCap22254_1226.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG29018.
HOGENOMHOG000076230.
KOK16157.
OMAAGHNDAR.
OrthoDBEOG6N67XK.
ProtClustDBCLSK819184.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3861.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP22869.

Entry information

Entry nameMEMA_METCA
AccessionPrimary (citable) accession number: P22869
Secondary accession number(s): Q609N8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 7, 2004
Last modified: December 11, 2013
This is version 106 of the entry and version 3 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