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 gamma chain

Gene

mmoZ

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3863.
BRENDAi1.14.13.25. 3305.

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
Ordered Locus Names:MCA1198
OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Taxonomic identifieri243233 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
ProteomesiUP000006821 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 170169Methane monooxygenase component A gamma chainPRO_0000096409Add
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-59863N.
STRINGi243233.MCA1198.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi10 – 2011Combined sources
Helixi25 – 3915Combined sources
Turni48 – 525Combined sources
Helixi53 – 7119Combined sources
Helixi74 – 796Combined sources
Helixi87 – 10014Combined sources
Helixi104 – 11815Combined sources
Turni119 – 1224Combined sources
Helixi125 – 14319Combined sources
Turni144 – 1485Combined sources
Helixi152 – 1598Combined sources
Beta strandi162 – 1676Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11987.
SMRiP11987. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11987.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG257614.
HOGENOMiHOG000086317.
KOiK16159.
OMAiLRNTDYY.
OrthoDBiEOG6SV5J6.

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.

P11987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKLGIHSND TRDAWVNKIA QLNTLEKAAE MLKQFRMDHT TPFRNSYELD
60 70 80 90 100
NDYLWIEAKL EEKVAVLKAR AFNEVDFRHK TAFGEDAKSV LDGTVAKMNA
110 120 130 140 150
AKDKWEAEKI HIGFRQAYKP PIMPVNYFLD GERQLGTRLM ELRNLNYYDT
160 170
PLEELRKQRG VRVVHLQSPH
Length:170
Mass (Da):19,847
Last modified:January 23, 2007 - v4
Checksum:i6030AF38130BA497
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Q → E AA sequence (Ref. 4) Curated
Sequence conflicti26 – 261E → Q AA sequence (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAF04157.2.
AE017282 Genomic DNA. Translation: AAU92724.1.
PIRiJL0102.
RefSeqiWP_010960485.1. NC_002977.6.
YP_113663.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92724; AAU92724; MCA1198.
KEGGimca:MCA1198.
PATRICi22606228. VBIMetCap22254_1230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAF04157.2.
AE017282 Genomic DNA. Translation: AAU92724.1.
PIRiJL0102.
RefSeqiWP_010960485.1. NC_002977.6.
YP_113663.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP11987.
SMRiP11987. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59863N.
STRINGi243233.MCA1198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU92724; AAU92724; MCA1198.
KEGGimca:MCA1198.
PATRICi22606228. VBIMetCap22254_1230.

Phylogenomic databases

eggNOGiNOG257614.
HOGENOMiHOG000086317.
KOiK16159.
OMAiLRNTDYY.
OrthoDBiEOG6SV5J6.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3863.
BRENDAi1.14.13.25. 3305.

Miscellaneous databases

EvolutionaryTraceiP11987.

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.
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].
    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. 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).

Entry informationi

Entry nameiMEMG_METCA
AccessioniPrimary (citable) accession number: P11987
Secondary accession number(s): Q609N4, Q9RLQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 109 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.