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Protein

Methane monooxygenase component A beta chain

Gene

mmoY

Organism
Methylosinus trichosporium
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-3868.

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
OrganismiMethylosinus trichosporium
Taxonomic identifieri426 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000964082 – 394Methane monooxygenase component A beta chainAdd BLAST393

Interactioni

Subunit structurei

M.trichosporium 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.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni13 – 15Combined sources3
Helixi17 – 26Combined sources10
Turni38 – 41Combined sources4
Beta strandi45 – 48Combined sources4
Helixi51 – 56Combined sources6
Helixi88 – 90Combined sources3
Helixi98 – 100Combined sources3
Helixi109 – 133Combined sources25
Helixi135 – 138Combined sources4
Helixi141 – 145Combined sources5
Helixi148 – 172Combined sources25
Helixi176 – 206Combined sources31
Helixi215 – 223Combined sources9
Helixi225 – 227Combined sources3
Helixi228 – 239Combined sources12
Helixi244 – 253Combined sources10
Helixi255 – 264Combined sources10
Turni265 – 267Combined sources3
Helixi268 – 272Combined sources5
Turni273 – 276Combined sources4
Helixi280 – 302Combined sources23
Helixi303 – 307Combined sources5
Turni310 – 312Combined sources3
Helixi313 – 338Combined sources26
Helixi339 – 344Combined sources6
Helixi364 – 368Combined sources5
Helixi373 – 375Combined sources3
Helixi381 – 389Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00B1-394[»]
1MHZX-ray2.70B1-394[»]
ProteinModelPortaliP27354.
SMRiP27354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27354.

Family & Domainsi

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.

P27354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPQSSQVT KRGLTDPERA AIIAAAVPDH ALDTQRKYHY FIQPRWKPLS
60 70 80 90 100
EYEQLSCYAQ PNPDWIAGGL DWGDWTQKFH GGRPSWGNES TELRTTDWYR
110 120 130 140 150
HRDPARRWHH PYVKDKSEEA RYTQRFLAAY SSEGSIRTID PYWRDEILNK
160 170 180 190 200
YFGALLYSEY GLFNAHSSVG RDCLSDTIRQ TAVFAALDKV DNAQMIQMER
210 220 230 240 250
LFIAKLVPGF DASTDVPKKI WTTDPIYSGA RATVQEIWQG VQDWNEILWA
260 270 280 290 300
GHAVMIATFG QFARREFFQR LATVYGDTLT PFFTAQSQTY FQTTRGAIDD
310 320 330 340 350
LFVYCLANDS EFGAHNRTFL NAWTEHYLAS SVAALKDFVG LYAKVEKSRA
360 370 380 390
DRSRRRLRGA AASSAIGRSI TPDKIGFRVD VDQKVDAVLA GYKN
Length:394
Mass (Da):45,020
Last modified:January 23, 2007 - v3
Checksum:iFA6C8F0970F28B90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55394 Genomic DNA. Translation: CAA39069.1.
PIRiS15208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55394 Genomic DNA. Translation: CAA39069.1.
PIRiS15208.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00B1-394[»]
1MHZX-ray2.70B1-394[»]
ProteinModelPortaliP27354.
SMRiP27354.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3868.

Miscellaneous databases

EvolutionaryTraceiP27354.

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_METTR
AccessioniPrimary (citable) accession number: P27354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.