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P11987 (MEMG_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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 gamma chain

EC=1.14.13.25
Alternative name(s):
Methane hydroxylase
Gene names
Name:mmoZ
Ordered Locus Names:MCA1198
OrganismMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]
Taxonomic identifier243233 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus

Protein attributes

Sequence length170 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.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   LigandNADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmethane metabolic process

Inferred from electronic annotation. Source: InterPro

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmethane monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 170169Methane monooxygenase component A gamma chain
PRO_0000096409

Experimental info

Sequence conflict211Q → E AA sequence Ref.4
Sequence conflict261E → Q AA sequence Ref.4

Secondary structure

........................ 170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11987 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6030AF38130BA497

FASTA17019,847
        10         20         30         40         50         60 
MAKLGIHSND TRDAWVNKIA QLNTLEKAAE MLKQFRMDHT TPFRNSYELD NDYLWIEAKL 

        70         80         90        100        110        120 
EEKVAVLKAR AFNEVDFRHK TAFGEDAKSV LDGTVAKMNA AKDKWEAEKI HIGFRQAYKP 

       130        140        150        160        170 
PIMPVNYFLD GERQLGTRLM ELRNLNYYDT PLEELRKQRG VRVVHLQSPH 

« 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].
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 21-22.
[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]"Cloning of the gamma-subunit methane monooxygenase from Methylococcus capsulatus."
Mullens I.A., Dalton H.
Biotechnology (N.Y.) 5:490-493(1987)
Cited for: PROTEIN SEQUENCE OF 2-40.
[5]"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] OF 166-170.
Strain: ATCC 33009 / NCIMB 11132 / Bath.
[6]"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: AAF04157.2.
AE017282 Genomic DNA. Translation: AAU92724.1.
PIRJL0102.
RefSeqYP_113663.1. NC_002977.6.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYZX-ray2.15E/F1-170[»]
1FZ0X-ray2.07E/F1-170[»]
1FZ1X-ray1.96E/F1-170[»]
1FZ2X-ray2.15E/F1-170[»]
1FZ3X-ray2.03E/F1-170[»]
1FZ4X-ray2.38E/F1-170[»]
1FZ5X-ray2.40E/F1-170[»]
1FZ6X-ray2.05E/F1-170[»]
1FZ7X-ray1.96E/F1-170[»]
1FZ8X-ray2.10E/F1-170[»]
1FZ9X-ray2.30E/F1-170[»]
1FZHX-ray2.60E/F1-170[»]
1FZIX-ray3.30E/F1-170[»]
1MMOX-ray2.20G/H4-165[»]
1MTYX-ray1.70G/H4-165[»]
1XMFX-ray2.32E/F2-170[»]
1XMGX-ray2.10E/F2-170[»]
1XMHX-ray2.32E/F2-170[»]
1XU3X-ray2.30E/F1-170[»]
1XU5X-ray1.96E/F1-170[»]
1XVBX-ray1.80E/F1-170[»]
1XVCX-ray2.00E/F1-170[»]
1XVDX-ray2.30E/F1-170[»]
1XVEX-ray2.40E/F1-170[»]
1XVFX-ray2.00E/F1-170[»]
1XVGX-ray1.96E/F1-170[»]
4GAMX-ray2.90C/H/M/R1-170[»]
ProteinModelPortalP11987.
SMRP11987. Positions 3-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59863N.
STRING243233.MCA1198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU92724; AAU92724; MCA1198.
GeneID3102570.
KEGGmca:MCA1198.
PATRIC22606228. VBIMetCap22254_1230.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG257614.
HOGENOMHOG000086317.
KOK16159.
OMAQHEETER.
OrthoDBEOG6SV5J6.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-3863.

Family and domain databases

Gene3D1.20.1280.10. 1 hit.
1.20.1280.30. 1 hit.
InterProIPR004222. Me_mOase_g.
IPR015952. Me_mOase_g_dom1.
IPR015953. Me_mOase_g_dom2.
[Graphical view]
PfamPF02964. MeMO_Hyd_G. 1 hit.
[Graphical view]
PIRSFPIRSF018503. Me_mOase_g. 1 hit.
ProDomPD022203. Me_mOase_g. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF47152. SSF47152. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11987.

Entry information

Entry nameMEMG_METCA
AccessionPrimary (citable) accession number: P11987
Secondary accession number(s): Q609N4, Q9RLQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
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