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Protein

Methane monooxygenase component A alpha chain

Gene

mmoX

Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Iron 1
Metal bindingi144 – 1441Iron 1
Metal bindingi147 – 1471Iron 1
Active sitei151 – 1511Sequence Analysis
Metal bindingi209 – 2091Iron 2
Metal bindingi243 – 2431Iron 2
Metal bindingi246 – 2461Iron 2

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3861.
BRENDAi1.14.13.25. 3305.

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
Ordered Locus Names:MCA1194
OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Taxonomic identifieri243233 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
ProteomesiUP000006821 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Methane monooxygenase component A alpha chainPRO_0000096405Add
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-59861N.
STRINGi243233.MCA1194.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 295Combined sources
Helixi30 – 356Combined sources
Helixi64 – 8320Combined sources
Helixi85 – 884Combined sources
Turni89 – 935Combined sources
Helixi97 – 12731Combined sources
Helixi131 – 16131Combined sources
Turni166 – 1705Combined sources
Helixi171 – 1744Combined sources
Helixi175 – 1773Combined sources
Helixi180 – 1889Combined sources
Helixi190 – 1934Combined sources
Helixi197 – 2048Combined sources
Turni205 – 2073Combined sources
Helixi208 – 2114Combined sources
Helixi213 – 22614Combined sources
Helixi231 – 25727Combined sources
Beta strandi258 – 2603Combined sources
Helixi262 – 29231Combined sources
Helixi301 – 3099Combined sources
Helixi310 – 3156Combined sources
Helixi316 – 3194Combined sources
Helixi320 – 3245Combined sources
Helixi332 – 3398Combined sources
Helixi342 – 35211Combined sources
Helixi354 – 3563Combined sources
Beta strandi357 – 3604Combined sources
Helixi366 – 37510Combined sources
Helixi379 – 39214Combined sources
Turni393 – 3964Combined sources
Helixi398 – 4003Combined sources
Helixi405 – 4106Combined sources
Turni419 – 4213Combined sources
Turni427 – 4293Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi444 – 4507Combined sources
Helixi451 – 4599Combined sources
Helixi461 – 4633Combined sources
Helixi469 – 4724Combined sources
Turni473 – 4753Combined sources
Helixi478 – 4847Combined sources
Beta strandi492 – 4965Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi503 – 5053Combined sources
Helixi509 – 5135Combined sources
Turni514 – 5163Combined sources
Helixi522 – 5254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYZX-ray2.15A/B1-527[»]
1FZ0X-ray2.07A/B1-527[»]
1FZ1X-ray1.96A/B1-527[»]
1FZ2X-ray2.15A/B1-527[»]
1FZ3X-ray2.03A/B1-527[»]
1FZ4X-ray2.38A/B1-527[»]
1FZ5X-ray2.40A/B1-527[»]
1FZ6X-ray2.05A/B1-527[»]
1FZ7X-ray1.96A/B1-527[»]
1FZ8X-ray2.10A/B1-527[»]
1FZ9X-ray2.30A/B1-527[»]
1FZHX-ray2.60A/B1-527[»]
1FZIX-ray3.30A/B1-527[»]
1MMOX-ray2.20D/E15-526[»]
1MTYX-ray1.70D/E15-526[»]
1XMFX-ray2.32A/B1-527[»]
1XMGX-ray2.10A/B1-527[»]
1XMHX-ray2.32A/B1-527[»]
1XU3X-ray2.30A/B1-527[»]
1XU5X-ray1.96A/B1-527[»]
1XVBX-ray1.80A/B1-527[»]
1XVCX-ray2.00A/B1-527[»]
1XVDX-ray2.30A/B1-527[»]
1XVEX-ray2.40A/B1-527[»]
1XVFX-ray2.00A/B1-527[»]
1XVGX-ray1.96A/B1-527[»]
4GAMX-ray2.90A/F/K/P1-527[»]
ProteinModelPortaliP22869.
SMRiP22869. Positions 15-526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22869.

Family & Domainsi

Phylogenomic databases

eggNOGiNOG29018.
HOGENOMiHOG000076230.
KOiK16157.
OMAiHMANGYQ.
OrthoDBiEOG6N67XK.

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.

P22869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSTATKAA TDALAANRAP TSVNAQEVHR WLQSFNWDFK NNRTKYATKY
60 70 80 90 100
KMANETKEQF KLIAKEYARM EAVKDERQFG SLQDALTRLN AGVRVHPKWN
110 120 130 140 150
ETMKVVSNFL EVGEYNAIAA TGMLWDSAQA AEQKNGYLAQ VLDEIRHTHQ
160 170 180 190 200
CAYVNYYFAK NGQDPAGHND ARRTRTIGPL WKGMKRVFSD GFISGDAVEC
210 220 230 240 250
SLNLQLVGEA CFTNPLIVAV TEWAAANGDE ITPTVFLSIE TDELRHMANG
260 270 280 290 300
YQTVVSIAND PASAKYLNTD LNNAFWTQQK YFTPVLGMLF EYGSKFKVEP
310 320 330 340 350
WVKTWNRWVY EDWGGIWIGR LGKYGVESPR SLKDAKQDAY WAHHDLYLLA
360 370 380 390 400
YALWPTGFFR LALPDQEEME WFEANYPGWY DHYGKIYEEW RARGCEDPSS
410 420 430 440 450
GFIPLMWFIE NNHPIYIDRV SQVPFCPSLA KGASTLRVHE YNGQMHTFSD
460 470 480 490 500
QWGERMWLAE PERYECQNIF EQYEGRELSE VIAELHGLRS DGKTLIAQPH
510 520
VRGDKLWTLD DIKRLNCVFK NPVKAFN
Length:527
Mass (Da):60,646
Last modified:December 7, 2004 - v3
Checksum:i953438FDF5208374
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061N → D in AAB62392 (Ref. 2) Curated
Sequence conflicti444 – 4441Q → E in AAB62392 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62392.3.
AE017282 Genomic DNA. Translation: AAU92736.1.
PIRiJQ0702.
RefSeqiWP_010960482.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92736; AAU92736; MCA1194.
KEGGimca:MCA1194.
PATRICi22606220. VBIMetCap22254_1226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62392.3.
AE017282 Genomic DNA. Translation: AAU92736.1.
PIRiJQ0702.
RefSeqiWP_010960482.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYZX-ray2.15A/B1-527[»]
1FZ0X-ray2.07A/B1-527[»]
1FZ1X-ray1.96A/B1-527[»]
1FZ2X-ray2.15A/B1-527[»]
1FZ3X-ray2.03A/B1-527[»]
1FZ4X-ray2.38A/B1-527[»]
1FZ5X-ray2.40A/B1-527[»]
1FZ6X-ray2.05A/B1-527[»]
1FZ7X-ray1.96A/B1-527[»]
1FZ8X-ray2.10A/B1-527[»]
1FZ9X-ray2.30A/B1-527[»]
1FZHX-ray2.60A/B1-527[»]
1FZIX-ray3.30A/B1-527[»]
1MMOX-ray2.20D/E15-526[»]
1MTYX-ray1.70D/E15-526[»]
1XMFX-ray2.32A/B1-527[»]
1XMGX-ray2.10A/B1-527[»]
1XMHX-ray2.32A/B1-527[»]
1XU3X-ray2.30A/B1-527[»]
1XU5X-ray1.96A/B1-527[»]
1XVBX-ray1.80A/B1-527[»]
1XVCX-ray2.00A/B1-527[»]
1XVDX-ray2.30A/B1-527[»]
1XVEX-ray2.40A/B1-527[»]
1XVFX-ray2.00A/B1-527[»]
1XVGX-ray1.96A/B1-527[»]
4GAMX-ray2.90A/F/K/P1-527[»]
ProteinModelPortaliP22869.
SMRiP22869. Positions 15-526.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59861N.
STRINGi243233.MCA1194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU92736; AAU92736; MCA1194.
KEGGimca:MCA1194.
PATRICi22606220. VBIMetCap22254_1226.

Phylogenomic databases

eggNOGiNOG29018.
HOGENOMiHOG000076230.
KOiK16157.
OMAiHMANGYQ.
OrthoDBiEOG6N67XK.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3861.
BRENDAi1.14.13.25. 3305.

Miscellaneous databases

EvolutionaryTraceiP22869.

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...

Publicationsi

« Hide 'large scale' publications
  1. "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], PROTEIN SEQUENCE OF 1-6.
    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 84; 306 AND 444.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33009 / NCIMB 11132 / Bath.
  4. "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).
  5. "Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states."
    Rosenzweig A.C., Nordlund P., Takahara P.M., Frederick C.A., Lippard S.J.
    Chem. Biol. 2:409-418(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  6. "Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions."
    Rosenzweig A.C., Brandstetter H., Whittington D.A., Nordlund P., Lippard S.J., Frederick C.A.
    Proteins 29:141-152(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    Strain: ATCC 33009 / NCIMB 11132 / Bath.
  7. "Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site."
    Whittington D.A., Lippard S.J.
    J. Am. Chem. Soc. 123:827-838(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
    Strain: ATCC 33009 / NCIMB 11132 / Bath.

Entry informationi

Entry nameiMEMA_METCA
AccessioniPrimary (citable) accession number: P22869
Secondary accession number(s): Q609N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 7, 2004
Last modified: July 22, 2015
This is version 118 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.