MSMC_METHY
ID MSMC_METHY Reviewed; 123 AA.
AC P70752;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Methanesulfonate monooxygenase ferredoxin subunit {ECO:0000305};
DE AltName: Full=Methanesulfonic acid monooxygenase electron transfer subunit {ECO:0000303|PubMed:9068643};
DE AltName: Full=Methanesulfonic acid monooxygenase ferredoxin subunit {ECO:0000303|PubMed:9068643};
DE Short=MSA monooxygenase ferredoxin subunit {ECO:0000305};
DE Short=MSAMO ferredoxin subunit {ECO:0000305};
DE EC=1.14.13.111 {ECO:0000269|PubMed:8932698};
GN Name=msmC {ECO:0000303|PubMed:10094704};
OS Methylosulfonomonas methylovora.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylosulfonomonas.
OX NCBI_TaxID=50057 {ECO:0000312|EMBL:AAC35388.1};
RN [1] {ECO:0000312|EMBL:AAC35388.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=M2 {ECO:0000312|EMBL:AAC35388.1};
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] {ECO:0000312|EMBL:AAC35388.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=M2 {ECO:0000312|EMBL:AAC35388.1};
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 PROTEIN SEQUENCE OF 2-39, COFACTOR, AND SUBUNIT.
RC STRAIN=M2 {ECO:0000312|EMBL:AAC35388.1};
RX PubMed=9068643; DOI=10.1128/jb.179.6.1974-1979.1997;
RA Higgins T.P., De Marco P., Murrell J.C.;
RT "Purification and molecular characterization of the electron transfer
RT protein of methanesulfonic acid monooxygenase.";
RL J. Bacteriol. 179:1974-1979(1997).
RN [4]
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:Q00458,
CC ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000303|PubMed:8932698};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q00458, ECO:0000255|PROSITE-ProRule:PRU00628,
CC ECO:0000303|PubMed:8932698};
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). The ferredoxin component is
CC dimeric. {ECO:0000303|PubMed:10094704, ECO:0000303|PubMed:9068643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8932698}.
CC -!- INDUCTION: The msmABCD operon is induced by methanesulfonic acid (MSA).
CC {ECO:0000269|PubMed:16391054}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; AF091716; AAC35388.1; -; Genomic_DNA.
DR AlphaFoldDB; P70752; -.
DR SMR; P70752; -.
DR BioCyc; MetaCyc:MON-14213; -.
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; IDA:UniProtKB.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Monooxygenase; NAD; Oxidoreductase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8932698"
FT CHAIN 2..123
FT /note="Methanesulfonate monooxygenase ferredoxin subunit"
FT /id="PRO_0000430803"
FT DOMAIN 4..99
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q00458"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q00458"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q00458"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:Q00458"
SQ SEQUENCE 123 AA; 13880 MW; 23C579902E584F15 CRC64;
MSWTYLCDAA DVAPNSLKLV DANDIRVVVA NYGSGFRAIP PICPHMEEPL DESGVIANCV
LTCTKHLWAW NLISLELLGE TEKPLKTYEL KEEDGKLLAF IAEELTYDFE EEDDMDDDFF
SKS
