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Protein

Methane monooxygenase component C

Gene

mmoC

Organism
Methylosinus trichosporium
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 bindingi37Iron-sulfur (2Fe-2S)1
Metal bindingi41Iron-sulfur (2Fe-2S)1
Metal bindingi44Iron-sulfur (2Fe-2S)1
Metal bindingi76Iron-sulfur (2Fe-2S)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi215 – 229FADBy similarityAdd BLAST15

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMonooxygenase, Oxidoreductase
Biological processElectron transport, One-carbon metabolism, Transport
Ligand2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3870.

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
OrganismiMethylosinus trichosporium
Taxonomic identifieri426 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylocystaceaeMethylosinus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001894091 – 340Methane monooxygenase component CAdd BLAST340

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).

Structurei

3D structure databases

ProteinModelPortaliQ53563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 922Fe-2S ferredoxin-typeAdd BLAST92
Domaini101 – 205FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST105

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiView protein in InterPro
IPR001041. 2Fe-2S_ferredoxin-type.
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.
PfamiView protein in Pfam
PF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiView protein in PROSITE
PS51384. FAD_FR. 1 hit.

Sequencei

Sequence statusi: Complete.

Q53563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYQIVIETED GETCRRMRPS EDWISRAEAE RNLLASCRAG CATCKADCTD
60 70 80 90 100
GDYELIDVKV QAVPPDEEED GKVLLCRTFP RSDLHLLVPY TYDRISFEAI
110 120 130 140 150
QTNWLAEILA CDRVSSNVVR LVLQRSRPMA ARISLNFVPG QFVDIEIPGT
160 170 180 190 200
HTRRSYSMAS VAEDGQLEFI IRLLPDGAFS KFLQTEAKVG MRVDLRGPAG
210 220 230 240 250
SFFLHDHGGR SRVFVAGGTG LSPVLSMIRQ LGKASDPSPA TLLFGVTNRE
260 270 280 290 300
ELFYVDELKT LAQSMPTLGV RIAVVNDDGG NGVDKGTVID LLRAELEIDL
310 320 330 340
LLGHARRRRR RETARSCRED HRDRCPAWRS DFLEKFLASG
Length:340
Mass (Da):37,991
Last modified:November 1, 1996 - v1
Checksum:i79AE21DA8079E6D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81887 Genomic DNA. Translation: AAB21393.1.
PIRiC48360.

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.

Entry informationi

Entry nameiMMOC_METTR
AccessioniPrimary (citable) accession number: Q53563
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1996
Last modified: February 15, 2017
This is version 92 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing