MSMD_METHY
ID MSMD_METHY Reviewed; 366 AA.
AC Q9X406;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Putative methanesulfonate monooxygenase ferredoxin reductase subunit {ECO:0000305};
DE EC=1.14.13.111 {ECO:0000269|PubMed:16391054};
DE AltName: Full=Methanesulfonic acid monooxygenase ferredoxin reductase subunit;
DE Short=MSA monooxygenase ferredoxin reductase subunit;
DE Short=MSAMO ferredoxin reductase subunit;
GN Name=msmD {ECO:0000312|EMBL:AAD26621.1};
OS Methylosulfonomonas methylovora.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylosulfonomonas.
OX NCBI_TaxID=50057 {ECO:0000312|EMBL:AAD26621.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=M2 {ECO:0000312|EMBL:AAD26621.1};
RX PubMed=10094704; DOI=10.1128/jb.181.7.2244-2251.1999;
RA de Marco P., Moradas-Ferreira P., Higgins T.P., McDonald I., Kenna E.M.,
RA Murrell J.C.;
RT "Molecular analysis of a novel methanesulfonic acid monooxygenase from the
RT methylotroph Methylosulfonomonas methylovora.";
RL J. Bacteriol. 181:2244-2251(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=M2 {ECO:0000312|EMBL:AAD26621.1};
RX PubMed=16391054; DOI=10.1128/aem.72.1.276-283.2006;
RA Jamshad M., De Marco P., Pacheco C.C., Hanczar T., Murrell J.C.;
RT "Identification, mutagenesis, and transcriptional analysis of the
RT methanesulfonate transport operon of Methylosulfonomonas methylovora.";
RL Appl. Environ. Microbiol. 72:276-283(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8932698; DOI=10.1099/13500872-142-2-251;
RA Higgins T.P., Davey M., Trickett J., Kelly D.P., Murrell J.C.;
RT "Metabolism of methanesulfonic acid involves a multicomponent monooxygenase
RT enzyme.";
RL Microbiology 142:251-260(1996).
CC -!- FUNCTION: Methanesulfonate monooxygenase (MSAMO) mediates the primary
CC degradation of methanesulfonic acid (MSA) to produce formaldehyd and
CC inorganic sulfite by initial hydroxylation of the carbon atom prior to
CC spontaneous cleavage of the unstable hydroxymethanesulfonic acid. MSAMO
CC has a restricted substrate range that includes only the short-chain
CC aliphatic sulfonates (methane- to butanesulfonate) and excludes all
CC larger molecules, such as arylsulfonates and aromatic sulfonates. All
CC MSAMO components are required for enzyme activity.
CC {ECO:0000269|PubMed:8932698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=methanesulfonate + NADH + O2 = formaldehyde + H2O + NAD(+) +
CC sulfite; Xref=Rhea:RHEA:26077, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:17359, ChEBI:CHEBI:25224,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.111;
CC Evidence={ECO:0000269|PubMed:8932698};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: MSAMO is inhibited by metal chelators (such as
CC bathophenanthroline, bathocuprione, neocuprione, alpha-alpha-dipyridil
CC and sodium EDTA) and by sodium azide, sodium arsenate and potassium
CC cyanide. {ECO:0000269|PubMed:8932698}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for NADH {ECO:0000269|PubMed:8932698};
CC KM=61.5 uM for ethane sulfonic acid {ECO:0000269|PubMed:8932698};
CC Vmax=65.5 nmol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:8932698};
CC Vmax=38.7 nmol/min/mg enzyme with ethane sulfonic acid as substrate
CC {ECO:0000269|PubMed:8932698};
CC Note=Cell-free extracts of MSA-grown strain M2 have been used. Vmax
CC of a cytoplasmic fraction has shown to be lower as was that of a
CC reconstituted enzyme from partially purified fractions which was
CC increased by addition of FAD and Fe(2+).
CC {ECO:0000269|PubMed:8932698};
CC -!- SUBUNIT: The MSA monooxygenase system consists of 4 proteins: the 2
CC subunits of the hydroxylase component (MsmA and MsmB), a ferredoxin
CC (MsmC) and a ferredoxin reductase (MsmD).
CC {ECO:0000303|PubMed:10094704}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8932698}.
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DR EMBL; AF091716; AAD26621.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X406; -.
DR SMR; Q9X406; -.
DR BioCyc; MetaCyc:MON-14214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018648; F:methanesulfonate monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NAD;
KW Oxidoreductase.
FT CHAIN 1..366
FT /note="Putative methanesulfonate monooxygenase ferredoxin
FT reductase subunit"
FT /id="PRO_0000430804"
FT DOMAIN 20..112
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 122..221
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 61
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 64
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 366 AA; 38852 MW; 96CFEA5A3B93B612 CRC64;
MTSLARADDL AAAPLARENC AVSVETKSGV FGFDCAPGET LLYAGLRHGL TLPHECATGT
CGTCRARVMT GEVDVAWEEA PGAARFKRDK GDVLLCQTRA VGDCVLRVPA EVAAKPARHQ
IPAYRTGLME NIRRLTGDVI SFEVALSAPM DFDAGQFVVV EAPGLEGARA YSMVNFTRSA
DRIELVVKRK PSGGFGDWLF GATAEGAKVK VFGPLGRATF HADEHKNLLM IAGGSGIAGM
MSILASAAEA DHFRTRKGYL FFGVRTLADG FYLQEFAQRV VEAQGNLEVT LALSHEDPAG
ADHPDHPGVK LASGMVHEVA GRAMAGRYDD LIAYVAGPPP MVDGALRTLI TQGGLSPSAI
RYDKFG
