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P22868

- MMOC_METCA

UniProt

P22868 - MMOC_METCA

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Protein

Methane monooxygenase component C

Gene

mmoC

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. The component C is the iron-sulfur flavoprotein of sMMO.

Catalytic activityi

Methane + NAD(P)H + O2 = methanol + NAD(P)+ + H2O.

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Iron-sulfur (2Fe-2S)
Metal bindingi47 – 471Iron-sulfur (2Fe-2S)
Metal bindingi50 – 501Iron-sulfur (2Fe-2S)
Metal bindingi82 – 821Iron-sulfur (2Fe-2S)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 23515FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. methane monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. one-carbon metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Electron transport, One-carbon metabolism, Transport

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3864.

Names & Taxonomyi

Protein namesi
Recommended name:
Methane monooxygenase component C (EC:1.14.13.25)
Alternative name(s):
Methane hydroxylase
Methane monooxygenase reductase
Short name:
MMOR
Gene namesi
Name:mmoC
Ordered Locus Names:MCA1200
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 – 348348Methane monooxygenase component CPRO_0000189408Add
BLAST

Interactioni

Subunit structurei

The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD).

Protein-protein interaction databases

STRINGi243233.MCA1200.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Turni12 – 143Combined sources
Beta strandi15 – 239Combined sources
Helixi27 – 348Combined sources
Beta strandi54 – 563Combined sources
Turni66 – 683Combined sources
Helixi71 – 777Combined sources
Turni81 – 833Combined sources
Beta strandi90 – 934Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi123 – 1286Combined sources
Beta strandi134 – 1385Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi167 – 1704Combined sources
Beta strandi173 – 1775Combined sources
Beta strandi183 – 1853Combined sources
Helixi186 – 1927Combined sources
Beta strandi193 – 20513Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi218 – 2258Combined sources
Helixi228 – 24013Combined sources
Beta strandi246 – 2516Combined sources
Beta strandi253 – 2553Combined sources
Helixi261 – 27010Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi275 – 2784Combined sources
Beta strandi288 – 2958Combined sources
Helixi296 – 3049Combined sources
Beta strandi305 – 31612Combined sources
Helixi317 – 33014Combined sources
Beta strandi335 – 3395Combined sources
Beta strandi343 – 3453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQ4NMR-A1-98[»]
1TVCNMR-A99-348[»]
DisProtiDP00379.
ProteinModelPortaliP22868.
SMRiP22868. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22868.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 98942Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini106 – 211106FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0543.
HOGENOMiHOG000263663.
KOiK16161.
OMAiILMCRTT.
OrthoDBiEOG6RNQ9P.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22868-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQRVHTITAV TEDGESLRFE CRSDEDVITA ALRQNIFLMS SCREGGCATC
60 70 80 90 100
KALCSEGDYD LKGCSVQALP PEEEEEGLVL LCRTYPKTDL EIELPYTHCR
110 120 130 140 150
ISFGEVGSFE AEVVGLNWVS SNTVQFLLQK RPDECGNRGV KFEPGQFMDL
160 170 180 190 200
TIPGTDVSRS YSPANLPNPE GRLEFLIRVL PEGRFSDYLR NDARVGQVLS
210 220 230 240 250
VKGPLGVFGL KERGMAPRYF VAGGTGLAPV VSMVRQMQEW TAPNETRIYF
260 270 280 290 300
GVNTEPELFY IDELKSLERS MRNLTVKACV WHPSGDWEGE QGSPIDALRE
310 320 330 340
DLESSDANPD IYLCGPPGMI DAACELVRSR GIPGEQVFFE KFLPSGAA
Length:348
Mass (Da):38,542
Last modified:September 26, 2001 - v2
Checksum:i7577BEB408CA1C1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62391.2.
AE017282 Genomic DNA. Translation: AAU92722.1.
PIRiJQ0701.
RefSeqiWP_010960487.1. NC_002977.6.
YP_113665.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU92722; AAU92722; MCA1200.
GeneIDi3103263.
KEGGimca:MCA1200.
PATRICi22606232. VBIMetCap22254_1232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M90050 Genomic DNA. Translation: AAB62391.2 .
AE017282 Genomic DNA. Translation: AAU92722.1 .
PIRi JQ0701.
RefSeqi WP_010960487.1. NC_002977.6.
YP_113665.1. NC_002977.6.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JQ4 NMR - A 1-98 [» ]
1TVC NMR - A 99-348 [» ]
DisProti DP00379.
ProteinModelPortali P22868.
SMRi P22868. Positions 1-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243233.MCA1200.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU92722 ; AAU92722 ; MCA1200 .
GeneIDi 3103263.
KEGGi mca:MCA1200.
PATRICi 22606232. VBIMetCap22254_1232.

Phylogenomic databases

eggNOGi COG0543.
HOGENOMi HOG000263663.
KOi K16161.
OMAi ILMCRTT.
OrthoDBi EOG6RNQ9P.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-3864.

Miscellaneous databases

EvolutionaryTracei P22868.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMi SSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view ]
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 1-16.
    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 254.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33009 / NCIMB 11132 / Bath.
  4. "NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase."
    Mueller J., Lugovskoy A.A., Wagner G., Lippard S.J.
    Biochemistry 41:42-51(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
    Strain: ATCC 33009 / NCIMB 11132 / Bath.

Entry informationi

Entry nameiMMOC_METCA
AccessioniPrimary (citable) accession number: P22868
Secondary accession number(s): Q609N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: September 26, 2001
Last modified: November 26, 2014
This is version 122 of the entry and version 2 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
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3