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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

  • methane monooxygenase activity Source: JCVI

GO - Biological processi

  • cellular aromatic compound metabolic process Source: InterPro
  • methane metabolic process Source: JCVI
  • one-carbon metabolic process Source: UniProtKB-KW
  • oxidation-reduction process Source: JCVI
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3862.
BRENDAi1.14.13.25. 3305.

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
Proteomesi
  • UP000006821 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • methane monooxygenase complex Source: JCVI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000964072 – 389Methane monooxygenase component A beta chainAdd BLAST388

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

1389
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 12Combined sources3
Helixi14 – 23Combined sources10
Turni35 – 38Combined sources4
Beta strandi42 – 45Combined sources4
Helixi48 – 53Combined sources6
Helixi85 – 87Combined sources3
Helixi95 – 97Combined sources3
Helixi106 – 129Combined sources24
Helixi132 – 135Combined sources4
Helixi138 – 142Combined sources5
Helixi143 – 147Combined sources5
Helixi148 – 161Combined sources14
Helixi164 – 169Combined sources6
Helixi173 – 203Combined sources31
Helixi212 – 220Combined sources9
Beta strandi222 – 224Combined sources3
Helixi225 – 236Combined sources12
Helixi241 – 250Combined sources10
Helixi252 – 262Combined sources11
Helixi265 – 268Combined sources4
Helixi269 – 272Combined sources4
Helixi276 – 299Combined sources24
Helixi300 – 304Combined sources5
Turni307 – 309Combined sources3
Helixi310 – 335Combined sources26
Helixi336 – 341Combined sources6
Helixi349 – 362Combined sources14
Helixi368 – 371Combined sources4
Helixi377 – 385Combined sources9
Turni386 – 388Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18798.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105CKQ. Bacteria.
ENOG410XP26. LUCA.
HOGENOMiHOG000086315.
KOiK16158.
OMAiKAEEWRY.
OrthoDBiPOG091H11FY.

Family and domain databases

CDDicd01058. AAMH_B. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti370R → A in AAB62393 (PubMed:2505721).Curated1

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.

Genome annotation databases

EnsemblBacteriaiAAU92727; AAU92727; MCA1195.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59862N.
STRINGi243233.MCA1195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105CKQ. Bacteria.
ENOG410XP26. LUCA.
HOGENOMiHOG000086315.
KOiK16158.
OMAiKAEEWRY.
OrthoDBiPOG091H11FY.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3862.
BRENDAi1.14.13.25. 3305.

Miscellaneous databases

EvolutionaryTraceiP18798.

Family and domain databases

CDDicd01058. AAMH_B. 1 hit.
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...

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: November 2, 2016
This is version 126 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

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 one 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.