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P22869

- MEMA_METCA

UniProt

P22869 - MEMA_METCA

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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: 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

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

  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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3861.

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiAGHNDAR.
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. 1 PublicationCurated
Sequence conflicti444 – 4441Q → E in AAB62392. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90050 Genomic DNA. Translation: AAB62392.3.
AE017282 Genomic DNA. Translation: AAU92736.1.
PIRiJQ0702.
RefSeqiYP_113659.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92736; AAU92736; MCA1194.
GeneIDi3104807.
KEGGimca:MCA1194.
PATRICi22606220. VBIMetCap22254_1226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90050 Genomic DNA. Translation: AAB62392.3 .
AE017282 Genomic DNA. Translation: AAU92736.1 .
PIRi JQ0702.
RefSeqi YP_113659.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FYZ X-ray 2.15 A/B 1-527 [» ]
1FZ0 X-ray 2.07 A/B 1-527 [» ]
1FZ1 X-ray 1.96 A/B 1-527 [» ]
1FZ2 X-ray 2.15 A/B 1-527 [» ]
1FZ3 X-ray 2.03 A/B 1-527 [» ]
1FZ4 X-ray 2.38 A/B 1-527 [» ]
1FZ5 X-ray 2.40 A/B 1-527 [» ]
1FZ6 X-ray 2.05 A/B 1-527 [» ]
1FZ7 X-ray 1.96 A/B 1-527 [» ]
1FZ8 X-ray 2.10 A/B 1-527 [» ]
1FZ9 X-ray 2.30 A/B 1-527 [» ]
1FZH X-ray 2.60 A/B 1-527 [» ]
1FZI X-ray 3.30 A/B 1-527 [» ]
1MMO X-ray 2.20 D/E 15-526 [» ]
1MTY X-ray 1.70 D/E 15-526 [» ]
1XMF X-ray 2.32 A/B 1-527 [» ]
1XMG X-ray 2.10 A/B 1-527 [» ]
1XMH X-ray 2.32 A/B 1-527 [» ]
1XU3 X-ray 2.30 A/B 1-527 [» ]
1XU5 X-ray 1.96 A/B 1-527 [» ]
1XVB X-ray 1.80 A/B 1-527 [» ]
1XVC X-ray 2.00 A/B 1-527 [» ]
1XVD X-ray 2.30 A/B 1-527 [» ]
1XVE X-ray 2.40 A/B 1-527 [» ]
1XVF X-ray 2.00 A/B 1-527 [» ]
1XVG X-ray 1.96 A/B 1-527 [» ]
4GAM X-ray 2.90 A/F/K/P 1-527 [» ]
ProteinModelPortali P22869.
SMRi P22869. Positions 15-526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59861N.
STRINGi 243233.MCA1194.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU92736 ; AAU92736 ; MCA1194 .
GeneIDi 3104807.
KEGGi mca:MCA1194.
PATRICi 22606220. VBIMetCap22254_1226.

Phylogenomic databases

eggNOGi NOG29018.
HOGENOMi HOG000076230.
KOi K16157.
OMAi AGHNDAR.
OrthoDBi EOG6N67XK.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3861.

Miscellaneous databases

EvolutionaryTracei P22869.

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

« 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: October 29, 2014
This is version 110 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