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P27353

- MEMA_METTR

UniProt

P27353 - MEMA_METTR

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Protein

Methane monooxygenase component A alpha chain

Gene

mmoX

Organism
Methylosinus trichosporium
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.

Cofactori

Fe cationNote: Binds 2 iron ions.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Iron 1By similarity
Metal bindingi144 – 1441Iron 1By similarity
Metal bindingi147 – 1471Iron 1By similarity
Active sitei151 – 1511Sequence Analysis
Metal bindingi209 – 2091Iron 2By similarity
Metal bindingi243 – 2431Iron 2By similarity
Metal bindingi246 – 2461Iron 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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

Iron, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Methane monooxygenase component A alpha chain (EC:1.14.13.25)
Alternative name(s):
Methane hydroxylase
Gene namesi
Name:mmoX
OrganismiMethylosinus trichosporium
Taxonomic identifieri426 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 526525Methane monooxygenase component A alpha chainPRO_0000096406Add
BLAST

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

1
526
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 295Combined sources
Helixi30 – 356Combined sources
Helixi64 – 8320Combined sources
Helixi85 – 884Combined sources
Helixi91 – 933Combined sources
Helixi97 – 12731Combined sources
Helixi131 – 16131Combined sources
Turni166 – 1705Combined sources
Helixi171 – 1744Combined sources
Helixi175 – 1773Combined sources
Helixi179 – 18810Combined sources
Helixi190 – 1934Combined sources
Helixi197 – 2048Combined sources
Turni205 – 2073Combined sources
Helixi208 – 2114Combined sources
Helixi213 – 22614Combined sources
Helixi231 – 25727Combined sources
Helixi261 – 29232Combined sources
Helixi301 – 3088Combined sources
Helixi309 – 3157Combined sources
Helixi316 – 3205Combined sources
Helixi321 – 3244Combined sources
Helixi332 – 3387Combined sources
Turni339 – 3413Combined sources
Helixi342 – 35211Combined sources
Helixi354 – 3563Combined sources
Beta strandi357 – 3604Combined sources
Helixi366 – 37510Combined sources
Turni377 – 3826Combined sources
Helixi383 – 39311Combined sources
Turni394 – 3963Combined sources
Helixi398 – 4003Combined sources
Helixi404 – 4107Combined sources
Turni419 – 4213Combined sources
Turni427 – 4293Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi444 – 4485Combined sources
Helixi451 – 4599Combined sources
Helixi461 – 4633Combined sources
Helixi469 – 4735Combined sources
Helixi478 – 4847Combined sources
Beta strandi492 – 4965Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi502 – 5043Combined sources
Helixi509 – 5146Combined sources
Helixi522 – 5254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHYX-ray2.00D1-525[»]
1MHZX-ray2.70D1-525[»]
ProteinModelPortaliP27353.
SMRiP27353. Positions 17-526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27353.

Family & Domainsi

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P27353-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAISLATKAA TDALKVNRAP VGVEPQEVHK WLQSFNWDFK ENRTKYPTKY
60 70 80 90 100
HMANETKEQF KVIAKEYARM EAAKDERQFG TLLDGLTRLG AGNKVHPRWG
110 120 130 140 150
ETMKVISNFL EVGEYNAIAA SAMLWDSATA AEQKNGYLAQ VLDEIRHTHQ
160 170 180 190 200
CAFINHYYSK HYHDPAGHND ARRTRAIGPL WKGMKRVFAD GFISGDAVEC
210 220 230 240 250
SVNLQLVGEA CFTNPLIVAV TEWASANGDE ITPTVFLSVE TDELRHMANG
260 270 280 290 300
YQTVVSIAND PASAKFLNTD LNNAFWTQQK YFTPVLGYLF EYGSKFKVEP
310 320 330 340 350
WVKTWNRWVY EDWGGIWIGR LGKYGVESPA SLRDAKRDAY WAHHDLALAA
360 370 380 390 400
YAMWPLGFAR LALPDEEDQA WFEANYPGWA DHYGKIFNEW KKLGYEDPKS
410 420 430 440 450
GFIPYQWLLA NGHDVYIDRV SQVPFIPSLA KGTGSLRVHE FNGKKHSLTD
460 470 480 490 500
DWGERQWLIE PERYECHNVF EQYEGRELSE VIAEGHGVRS DGKTLIAQPH
510 520
TRGDNLWTLE DIKRAGCVFP DPLAKF
Length:526
Mass (Da):59,954
Last modified:January 23, 2007 - v4
Checksum:iA56F4AAD0A55726B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55394 Genomic DNA. Translation: CAA39068.2.
PIRiS15207.

Genome annotation databases

PATRICi38005870. VBIMetTri17036_0736.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55394 Genomic DNA. Translation: CAA39068.2 .
PIRi S15207.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MHY X-ray 2.00 D 1-525 [» ]
1MHZ X-ray 2.70 D 1-525 [» ]
ProteinModelPortali P27353.
SMRi P27353. Positions 17-526.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

PATRICi 38005870. VBIMetTri17036_0736.

Miscellaneous databases

EvolutionaryTracei P27353.

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR003430. Phenol_Hydrox.
IPR012348. RNR-rel.
[Graphical view ]
Pfami PF02332. Phenol_Hydrox. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular analysis of the methane monooxygenase (MMO) gene cluster of Methylosinus trichosporium OB3b."
    Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.
    Mol. Microbiol. 5:335-342(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: OB3b.
  2. McDonald I.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction."
    Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.
    J. Biol. Chem. 266:540-550(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.

Entry informationi

Entry nameiMEMA_METTR
AccessioniPrimary (citable) accession number: P27353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 84 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, Direct protein sequencing

Documents

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

External Data

Dasty 3