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Protein

Methane monooxygenase component C

Gene

mmoC

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. 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)DescriptionActionsGraphical viewLength
Metal bindingi42Iron-sulfur (2Fe-2S)1
Metal bindingi47Iron-sulfur (2Fe-2S)1
Metal bindingi50Iron-sulfur (2Fe-2S)1
Metal bindingi82Iron-sulfur (2Fe-2S)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi221 – 235FADBy similarityAdd BLAST15

GO - Molecular functioni

GO - Biological processi

  • 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

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
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_00001894081 – 348Methane monooxygenase component CAdd BLAST348

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

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Turni12 – 14Combined sources3
Beta strandi15 – 23Combined sources9
Helixi27 – 34Combined sources8
Beta strandi54 – 56Combined sources3
Turni66 – 68Combined sources3
Helixi71 – 77Combined sources7
Turni81 – 83Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi106 – 113Combined sources8
Beta strandi117 – 120Combined sources4
Beta strandi123 – 128Combined sources6
Beta strandi134 – 138Combined sources5
Beta strandi147 – 150Combined sources4
Beta strandi156 – 161Combined sources6
Beta strandi167 – 170Combined sources4
Beta strandi173 – 177Combined sources5
Beta strandi183 – 185Combined sources3
Helixi186 – 192Combined sources7
Beta strandi193 – 205Combined sources13
Beta strandi214 – 216Combined sources3
Beta strandi218 – 225Combined sources8
Helixi228 – 240Combined sources13
Beta strandi246 – 251Combined sources6
Beta strandi253 – 255Combined sources3
Helixi261 – 270Combined sources10
Beta strandi271 – 273Combined sources3
Beta strandi275 – 278Combined sources4
Beta strandi288 – 295Combined sources8
Helixi296 – 304Combined sources9
Beta strandi305 – 316Combined sources12
Helixi317 – 330Combined sources14
Beta strandi335 – 339Combined sources5
Beta strandi343 – 345Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22868.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 982Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST94
Domaini106 – 211FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST106

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107TVJ. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000263663.
KOiK16161.
OMAiGSCHASV.
OrthoDBiPOG091H05I4.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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.

Genome annotation databases

EnsemblBacteriaiAAU92722; AAU92722; MCA1200.
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.
PIRiJQ0701.
RefSeqiWP_010960487.1. NC_002977.6.

3D structure databases

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

Protein-protein interaction databases

STRINGi243233.MCA1200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4107TVJ. Bacteria.
COG0543. LUCA.
HOGENOMiHOG000263663.
KOiK16161.
OMAiGSCHASV.
OrthoDBiPOG091H05I4.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3864.

Miscellaneous databases

EvolutionaryTraceiP22868.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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]
ProtoNetiSearch...

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 2, 2016
This is version 134 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

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.