Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methane monooxygenase component A beta chain

Gene

mmoY

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed-Annotation score: 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. cellular aromatic compound 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-3862.

Names & Taxonomyi

Protein namesi
Recommended name:
Methane monooxygenase component A beta chain (EC:1.14.13.25)
Alternative name(s):
Methane hydroxylase
Gene namesi
Name:mmoY
Ordered Locus Names:MCA1195
OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Taxonomic identifieri243233 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
ProteomesiUP000006821: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 389388Methane monooxygenase component A beta chainPRO_0000096407Add
BLAST

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

DIPiDIP-59862N.
STRINGi243233.MCA1195.

Structurei

Secondary structure

1
389
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123Combined sources
Helixi14 – 2310Combined sources
Turni35 – 384Combined sources
Beta strandi42 – 454Combined sources
Helixi48 – 536Combined sources
Helixi85 – 873Combined sources
Helixi95 – 973Combined sources
Helixi106 – 12924Combined sources
Helixi132 – 1354Combined sources
Helixi138 – 1425Combined sources
Helixi143 – 1475Combined sources
Helixi148 – 16114Combined sources
Helixi164 – 1696Combined sources
Helixi173 – 20331Combined sources
Helixi212 – 2209Combined sources
Beta strandi222 – 2243Combined sources
Helixi225 – 23612Combined sources
Helixi241 – 25010Combined sources
Helixi252 – 26211Combined sources
Helixi265 – 2684Combined sources
Helixi269 – 2724Combined sources
Helixi276 – 29924Combined sources
Helixi300 – 3045Combined sources
Turni307 – 3093Combined sources
Helixi310 – 33526Combined sources
Helixi336 – 3416Combined sources
Helixi349 – 36214Combined sources
Helixi368 – 3714Combined sources
Helixi377 – 3859Combined sources
Turni386 – 3883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/C6-362[»]
1XMFX-ray2.32C/D2-389[»]
1XMGX-ray2.10C/D2-389[»]
1XMHX-ray2.32C/D2-389[»]
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[»]
ProteinModelPortaliP18798.
SMRiP18798. Positions 2-389.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18798.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG268646.
HOGENOMiHOG000086315.
KOiK16158.
OMAiKAEEWRY.
OrthoDBiEOG679T94.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFiPIRSF000040. MMOH_comp. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P18798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLGERRRG LTDPEMAAVI LKALPEAPLD GNNKMGYFVT PRWKRLTEYE
60 70 80 90 100
ALTVYAQPNA DWIAGGLDWG DWTQKFHGGR PSWGNETTEL RTVDWFKHRD
110 120 130 140 150
PLRRWHAPYV KDKAEEWRYT DRFLQGYSAD GQIRAMNPTW RDEFINRYWG
160 170 180 190 200
AFLFNEYGLF NAHSQGAREA LSDVTRVSLA FWGFDKIDIA QMIQLERGFL
210 220 230 240 250
AKIVPGFDES TAVPKAEWTN GEVYKSARLA VEGLWQEVFD WNESAFSVHA
260 270 280 290 300
VYDALFGQFV RREFFQRLAP RFGDNLTPFF INQAQTYFQI AKQGVQDLYY
310 320 330 340 350
NCLGDDPEFS DYNRTVMRNW TGKWLEPTIA ALRDFMGLFA KLPAGTTDKE
360 370 380
EITASLYRVV DDWIEDYASR IDFKADRDQI VKAVLAGLK
Length:389
Mass (Da):45,133
Last modified:January 23, 2007 - v4
Checksum:i1737FEA30EEA9875
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti370 – 3701R → A in AAB62393 (PubMed:2505721).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62393.2.
AE017282 Genomic DNA. Translation: AAU92727.1.
PIRiA61412.
JL0101.
RefSeqiWP_010960483.1. NC_002977.6.
YP_113660.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92727; AAU92727; MCA1195.
GeneIDi3103426.
KEGGimca:MCA1195.
PATRICi22606222. VBIMetCap22254_1227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62393.2.
AE017282 Genomic DNA. Translation: AAU92727.1.
PIRiA61412.
JL0101.
RefSeqiWP_010960483.1. NC_002977.6.
YP_113660.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/C6-362[»]
1XMFX-ray2.32C/D2-389[»]
1XMGX-ray2.10C/D2-389[»]
1XMHX-ray2.32C/D2-389[»]
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[»]
ProteinModelPortaliP18798.
SMRiP18798. Positions 2-389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59862N.
STRINGi243233.MCA1195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU92727; AAU92727; MCA1195.
GeneIDi3103426.
KEGGimca:MCA1195.
PATRICi22606222. VBIMetCap22254_1227.

Phylogenomic databases

eggNOGiNOG268646.
HOGENOMiHOG000086315.
KOiK16158.
OMAiKAEEWRY.
OrthoDBiEOG679T94.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3862.

Miscellaneous databases

EvolutionaryTraceiP18798.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012078. MP_mOase_hydro.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view]
PfamiPF02332. Phenol_Hydrox. 1 hit.
[Graphical view]
PIRSFiPIRSF000040. MMOH_comp. 1 hit.
SUPFAMiSSF47240. SSF47240. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiMEMB_METCA
AccessioniPrimary (citable) accession number: P18798
Secondary accession number(s): Q609N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.