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Protein

Methane monooxygenase component A alpha chain

Gene

mmoX

Organism
Methylosinus trichosporium
Status
Reviewed-Annotation score: Annotation score: 4 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)DescriptionActionsGraphical viewLength
Metal bindingi114Iron 1By similarity1
Metal bindingi144Iron 1By similarity1
Metal bindingi147Iron 1By similarity1
Active sitei151Sequence analysis1
Metal bindingi209Iron 2By similarity1
Metal bindingi243Iron 2By similarity1
Metal bindingi246Iron 2By similarity1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000964062 – 526Methane monooxygenase component A alpha chainAdd BLAST525

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.

Protein-protein interaction databases

STRINGi595536.MettrDRAFT_0735.

Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 29Combined sources5
Helixi30 – 35Combined sources6
Helixi64 – 83Combined sources20
Helixi85 – 88Combined sources4
Helixi91 – 93Combined sources3
Helixi97 – 127Combined sources31
Helixi131 – 161Combined sources31
Turni166 – 170Combined sources5
Helixi171 – 174Combined sources4
Helixi175 – 177Combined sources3
Helixi179 – 188Combined sources10
Helixi190 – 193Combined sources4
Helixi197 – 204Combined sources8
Turni205 – 207Combined sources3
Helixi208 – 211Combined sources4
Helixi213 – 226Combined sources14
Helixi231 – 257Combined sources27
Helixi261 – 292Combined sources32
Helixi301 – 308Combined sources8
Helixi309 – 315Combined sources7
Helixi316 – 320Combined sources5
Helixi321 – 324Combined sources4
Helixi332 – 338Combined sources7
Turni339 – 341Combined sources3
Helixi342 – 352Combined sources11
Helixi354 – 356Combined sources3
Beta strandi357 – 360Combined sources4
Helixi366 – 375Combined sources10
Turni377 – 382Combined sources6
Helixi383 – 393Combined sources11
Turni394 – 396Combined sources3
Helixi398 – 400Combined sources3
Helixi404 – 410Combined sources7
Turni419 – 421Combined sources3
Turni427 – 429Combined sources3
Beta strandi437 – 441Combined sources5
Beta strandi444 – 448Combined sources5
Helixi451 – 459Combined sources9
Helixi461 – 463Combined sources3
Helixi469 – 473Combined sources5
Helixi478 – 484Combined sources7
Beta strandi492 – 496Combined sources5
Beta strandi498 – 500Combined sources3
Beta strandi502 – 504Combined sources3
Helixi509 – 514Combined sources6
Helixi522 – 525Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP27353.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105EUX. Bacteria.
ENOG410XRJ2. LUCA.

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.
PIRiS15207.

3D structure databases

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

Protein-protein interaction databases

STRINGi595536.MettrDRAFT_0735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi38005870. VBIMetTri17036_0736.

Phylogenomic databases

eggNOGiENOG4105EUX. Bacteria.
ENOG410XRJ2. LUCA.

Miscellaneous databases

EvolutionaryTraceiP27353.

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.
ProtoNetiSearch...

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 2, 2016
This is version 95 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

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.