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Protein

Putative methanesulfonate monooxygenase ferredoxin reductase subunit

Gene

msmD

Organism
Methylosulfonomonas methylovora
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Methanesulfonate monooxygenase (MSAMO) mediates the primary degradation of methanesulfonic acid (MSA) to produce formaldehyd and inorganic sulfite by initial hydroxylation of the carbon atom prior to spontaneous cleavage of the unstable hydroxymethanesulfonic acid. MSAMO has a restricted substrate range that includes only the short-chain aliphatic sulfonates (methane- to butanesulfonate) and excludes all larger molecules, such as arylsulfonates and aromatic sulfonates. All MSAMO components are required for enzyme activity.1 Publication

Catalytic activityi

Methanesulfonate + NADH + O2 = formaldehyde + NAD+ + sulfite + H2O.1 Publication

Cofactori

FADCurated

Enzyme regulationi

MSAMO is inhibited by metal chelators (such as bathophenanthroline, bathocuprione, neocuprione, alpha-alpha-dipyridil and sodium EDTA) and by sodium azide, sodium arsenate and potassium cyanide.1 Publication

Kineticsi

Cell-free extracts of MSA-grown strain M2 have been used. Vmax of a cytoplasmic fraction has shown to be lower as was that of a reconstituted enzyme from partially purified fractions which was increased by addition of FAD and Fe2+.1 Publication

Manual assertion based on experiment ini

  1. KM=48 µM for NADH1 Publication
  2. KM=61.5 µM for ethane sulfonic acid1 Publication
  1. Vmax=65.5 nmol/min/mg enzyme with NADH as substrate1 Publication
  2. Vmax=38.7 nmol/min/mg enzyme with ethane sulfonic acid as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi61Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi64Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi96Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14214.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative methanesulfonate monooxygenase ferredoxin reductase subunitCurated (EC:1.14.13.1111 Publication)
Alternative name(s):
Methanesulfonic acid monooxygenase ferredoxin reductase subunit
Short name:
MSA monooxygenase ferredoxin reductase subunit
Short name:
MSAMO ferredoxin reductase subunit
Gene namesi
Name:msmDImported
OrganismiMethylosulfonomonas methylovoraImported
Taxonomic identifieri50057 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylosulfonomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004308041 – 366Putative methanesulfonate monooxygenase ferredoxin reductase subunitAdd BLAST366

Interactioni

Subunit structurei

The MSA monooxygenase system consists of 4 proteins: the 2 subunits of the hydroxylase component (MsmA and MsmB), a ferredoxin (MsmC) and a ferredoxin reductase (MsmD).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9X406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 1122Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST93
Domaini122 – 221FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST100

Sequence similaritiesi

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

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.
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]
PRINTSiPR00410. 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.

Q9X406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSLARADDL AAAPLARENC AVSVETKSGV FGFDCAPGET LLYAGLRHGL
60 70 80 90 100
TLPHECATGT CGTCRARVMT GEVDVAWEEA PGAARFKRDK GDVLLCQTRA
110 120 130 140 150
VGDCVLRVPA EVAAKPARHQ IPAYRTGLME NIRRLTGDVI SFEVALSAPM
160 170 180 190 200
DFDAGQFVVV EAPGLEGARA YSMVNFTRSA DRIELVVKRK PSGGFGDWLF
210 220 230 240 250
GATAEGAKVK VFGPLGRATF HADEHKNLLM IAGGSGIAGM MSILASAAEA
260 270 280 290 300
DHFRTRKGYL FFGVRTLADG FYLQEFAQRV VEAQGNLEVT LALSHEDPAG
310 320 330 340 350
ADHPDHPGVK LASGMVHEVA GRAMAGRYDD LIAYVAGPPP MVDGALRTLI
360
TQGGLSPSAI RYDKFG
Length:366
Mass (Da):38,852
Last modified:November 1, 1999 - v1
Checksum:i96CFEA5A3B93B612
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091716 Genomic DNA. Translation: AAD26621.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091716 Genomic DNA. Translation: AAD26621.1.

3D structure databases

ProteinModelPortaliQ9X406.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14214.

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.
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]
PRINTSiPR00410. 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 nameiMSMD_METHY
AccessioniPrimary (citable) accession number: Q9X406
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.