MSMA_METHY
ID MSMA_METHY Reviewed; 414 AA.
AC Q9X404;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Methanesulfonate monooxygenase hydroxylase subunit alpha {ECO:0000305};
DE EC=1.14.13.111 {ECO:0000269|PubMed:10903510, ECO:0000269|PubMed:17169571, ECO:0000269|PubMed:8932698};
DE AltName: Full=Methanesulfonic acid monooxygenase hydroxylase large subunit {ECO:0000303|PubMed:10094704};
DE AltName: Full=Methanesulfonic acid monooxygenase hydroxylase subunit alpha {ECO:0000303|PubMed:10903510};
DE Short=MSA monooxygenase hydroxylase subunit alpha {ECO:0000303|PubMed:10903510};
DE Short=MSAMO hydroxylase subunit alpha {ECO:0000303|PubMed:10903510};
GN Name=msmA {ECO:0000303|PubMed:10094704};
OS Methylosulfonomonas methylovora.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylosulfonomonas.
OX NCBI_TaxID=50057 {ECO:0000312|EMBL:AAD26619.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=M2 {ECO:0000312|EMBL:AAD26619.1};
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:AAD26619.1};
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 1-21, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND COFACTOR.
RX PubMed=10903510; DOI=10.1046/j.1432-1327.2000.01538.x;
RA Reichenbecher W., Murrell J.C.;
RT "Purification and partial characterization of the hydroxylase component of
RT the methanesulfonic acid mono-oxygenase from methylosulfonomonas
RT methylovora strain M2.";
RL Eur. J. Biochem. 267:4763-4769(2000).
RN [4]
RP PROTEIN SEQUENCE OF 5-17; 25-38; 61-95; 108-112; 228-238; 331-365 AND
RP 397-414, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=17169571; DOI=10.1016/j.pep.2006.11.001;
RA Jamshad M., Murrell J.C., Fueloep V.;
RT "Purification and crystallization of the hydroxylase component of the
RT methanesulfonate monooxygenase from Methylosulfonomonas methylovora strain
RT M2.";
RL Protein Expr. Purif. 52:472-477(2007).
RN [5]
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:10903510, ECO:0000269|PubMed:17169571,
CC ECO:0000269|PubMed:8932698};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628,
CC ECO:0000303|PubMed:17169571};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628, ECO:0000303|PubMed:17169571};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000303|PubMed:10903510};
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 hydroxylase component
CC consists of a 3 alpha (MsmA) and 3 beta (MsmB) subunits.
CC {ECO:0000303|PubMed:10094704, ECO:0000303|PubMed:10903510}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10903510,
CC 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 alpha subunit family. {ECO:0000305}.
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DR EMBL; AF091716; AAD26619.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X404; -.
DR SMR; Q9X404; -.
DR KEGG; ag:AAD26619; -.
DR BioCyc; MetaCyc:MON-14211; -.
DR BRENDA; 1.14.13.111; 10320.
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 Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..414
FT /note="Methanesulfonate monooxygenase hydroxylase subunit
FT alpha"
FT /id="PRO_0000430801"
FT DOMAIN 44..163
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ SEQUENCE 414 AA; 48474 MW; 71B5952A4E6D4135 CRC64;
MPARNHTQWM ATPPLQKGEW VDSRVYTDQE IFDEELEKIF KKAWVPFRHE SELPKAYDFR
TTSIANEPII VTRGPDNEVR AFLNVCPHRG MLIERRPSGS LYEGQPSGNP KRMTCMFHAW
QFDMKGNCVY ISREKEGYQD RLPKESVGLR RLRCEVKFGG FVWVNLDDNP ISLEDWAGEP
FQCLRKTLEA EPMEVFHYHK AIVDTNYKLW HDTNCEFYHD FMHYHNRVTG FNDAYFARKN
ESFEHGHILV GTFEVNYDQY EGFESRAGLS FPHLPPNQWY MIDLFPGMNF NLRGSALRCD
VVTPLGPNKV MIEFRGLGLK SDTPEERQTR INHHNSIWGP FGRNLHEDLI GVQGQGTTMR
PGQESRRILH GRQENQTIHD ENGMRHYYDK WGKWMNRMPS NPELPYNAPA IAAE
