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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)DescriptionActionsGraphical viewLength
Metal bindingi114Iron 11
Metal bindingi144Iron 11
Metal bindingi147Iron 11
Active sitei151Sequence analysis1
Metal bindingi209Iron 21
Metal bindingi243Iron 21
Metal bindingi246Iron 21

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • methane monooxygenase activity Source: JCVI

GO - Biological processi

  • cellular aromatic compound metabolic process Source: InterPro
  • methane metabolic process Source: JCVI
  • one-carbon metabolic process Source: UniProtKB-KW
  • oxidation-reduction process Source: JCVI
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
Proteomesi
  • UP000006821 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  • methane monooxygenase complex Source: JCVI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000964051 – 527Methane monooxygenase component A alpha chainAdd BLAST527

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

1527
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
Turni89 – 93Combined sources5
Helixi97 – 127Combined sources31
Helixi131 – 161Combined sources31
Turni166 – 170Combined sources5
Helixi171 – 174Combined sources4
Helixi175 – 177Combined sources3
Helixi180 – 188Combined sources9
Helixi190 – 193Combined sources4
Helixi197 – 204Combined sources8
Turni205 – 207Combined sources3
Helixi208 – 211Combined sources4
Helixi213 – 226Combined sources14
Helixi231 – 257Combined sources27
Beta strandi258 – 260Combined sources3
Helixi262 – 292Combined sources31
Helixi301 – 309Combined sources9
Helixi310 – 315Combined sources6
Helixi316 – 319Combined sources4
Helixi320 – 324Combined sources5
Helixi332 – 339Combined sources8
Helixi342 – 352Combined sources11
Helixi354 – 356Combined sources3
Beta strandi357 – 360Combined sources4
Helixi366 – 375Combined sources10
Helixi379 – 392Combined sources14
Turni393 – 396Combined sources4
Helixi398 – 400Combined sources3
Helixi405 – 410Combined sources6
Turni419 – 421Combined sources3
Turni427 – 429Combined sources3
Beta strandi431 – 433Combined sources3
Beta strandi437 – 441Combined sources5
Beta strandi444 – 450Combined sources7
Helixi451 – 459Combined sources9
Helixi461 – 463Combined sources3
Helixi469 – 472Combined sources4
Turni473 – 475Combined sources3
Helixi478 – 484Combined sources7
Beta strandi492 – 496Combined sources5
Beta strandi498 – 500Combined sources3
Beta strandi503 – 505Combined sources3
Helixi509 – 513Combined sources5
Turni514 – 516Combined sources3
Helixi522 – 525Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22869.

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105EUX. Bacteria.
ENOG410XRJ2. LUCA.
HOGENOMiHOG000076230.
KOiK16157.
OMAiHMANGYQ.
OrthoDBiPOG091H08A8.

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)DescriptionActionsGraphical viewLength
Sequence conflicti306N → D in AAB62392 (Ref. 2) Curated1
Sequence conflicti444Q → E in AAB62392 (Ref. 2) Curated1

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
PDB 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.
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

eggNOGiENOG4105EUX. Bacteria.
ENOG410XRJ2. LUCA.
HOGENOMiHOG000076230.
KOiK16157.
OMAiHMANGYQ.
OrthoDBiPOG091H08A8.

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...

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: November 2, 2016
This is version 125 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

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.