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P11987

- MEMG_METCA

UniProt

P11987 - MEMG_METCA

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Protein
Methane monooxygenase component A gamma chain
Gene
mmoZ, MCA1198
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - 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
Complete GO annotation...

GO - Biological processi

  1. methane 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-3863.

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: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 170169Methane monooxygenase component A gamma chain
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP11987.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG257614.
HOGENOMiHOG000086317.
KOiK16159.
OMAiQHEETER.
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

MAKLGIHSND TRDAWVNKIA QLNTLEKAAE MLKQFRMDHT TPFRNSYELD    50
NDYLWIEAKL EEKVAVLKAR AFNEVDFRHK TAFGEDAKSV LDGTVAKMNA 100
AKDKWEAEKI HIGFRQAYKP PIMPVNYFLD GERQLGTRLM ELRNLNYYDT 150
PLEELRKQRG VRVVHLQSPH 170
Length:170
Mass (Da):19,847
Last modified:January 23, 2007 - v4
Checksum:i6030AF38130BA497
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Q → E AA sequence 1 Publication
Sequence conflicti26 – 261E → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi3102570.
KEGGimca:MCA1198.
PATRICi22606228. VBIMetCap22254_1230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90050 Genomic DNA. Translation: AAF04157.2 .
AE017282 Genomic DNA. Translation: AAU92724.1 .
PIRi JL0102.
RefSeqi WP_010960485.1. NC_002977.6.
YP_113663.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FYZ X-ray 2.15 E/F 1-170 [» ]
1FZ0 X-ray 2.07 E/F 1-170 [» ]
1FZ1 X-ray 1.96 E/F 1-170 [» ]
1FZ2 X-ray 2.15 E/F 1-170 [» ]
1FZ3 X-ray 2.03 E/F 1-170 [» ]
1FZ4 X-ray 2.38 E/F 1-170 [» ]
1FZ5 X-ray 2.40 E/F 1-170 [» ]
1FZ6 X-ray 2.05 E/F 1-170 [» ]
1FZ7 X-ray 1.96 E/F 1-170 [» ]
1FZ8 X-ray 2.10 E/F 1-170 [» ]
1FZ9 X-ray 2.30 E/F 1-170 [» ]
1FZH X-ray 2.60 E/F 1-170 [» ]
1FZI X-ray 3.30 E/F 1-170 [» ]
1MMO X-ray 2.20 G/H 4-165 [» ]
1MTY X-ray 1.70 G/H 4-165 [» ]
1XMF X-ray 2.32 E/F 2-170 [» ]
1XMG X-ray 2.10 E/F 2-170 [» ]
1XMH X-ray 2.32 E/F 2-170 [» ]
1XU3 X-ray 2.30 E/F 1-170 [» ]
1XU5 X-ray 1.96 E/F 1-170 [» ]
1XVB X-ray 1.80 E/F 1-170 [» ]
1XVC X-ray 2.00 E/F 1-170 [» ]
1XVD X-ray 2.30 E/F 1-170 [» ]
1XVE X-ray 2.40 E/F 1-170 [» ]
1XVF X-ray 2.00 E/F 1-170 [» ]
1XVG X-ray 1.96 E/F 1-170 [» ]
4GAM X-ray 2.90 C/H/M/R 1-170 [» ]
ProteinModelPortali P11987.
SMRi P11987. Positions 3-170.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-59863N.
STRINGi 243233.MCA1198.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU92724 ; AAU92724 ; MCA1198 .
GeneIDi 3102570.
KEGGi mca:MCA1198.
PATRICi 22606228. VBIMetCap22254_1230.

Phylogenomic databases

eggNOGi NOG257614.
HOGENOMi HOG000086317.
KOi K16159.
OMAi QHEETER.
OrthoDBi EOG6SV5J6.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3863.

Miscellaneous databases

EvolutionaryTracei P11987.

Family and domain databases

Gene3Di 1.20.1280.10. 1 hit.
1.20.1280.30. 1 hit.
InterProi IPR004222. Me_mOase_g.
IPR015952. Me_mOase_g_dom1.
IPR015953. Me_mOase_g_dom2.
[Graphical view ]
Pfami PF02964. MeMO_Hyd_G. 1 hit.
[Graphical view ]
PIRSFi PIRSF018503. Me_mOase_g. 1 hit.
ProDomi PD022203. Me_mOase_g. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF47152. SSF47152. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 104 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

Documents

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

External Data

Dasty 3

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