MSMB_METHY
ID MSMB_METHY Reviewed; 181 AA.
AC Q9X405;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Methanesulfonate monooxygenase hydroxylase subunit beta {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 small subunit {ECO:0000303|PubMed:10094704};
DE AltName: Full=Methanesulfonic acid monooxygenase hydroxylase subunit beta {ECO:0000303|PubMed:10903510};
DE Short=MSA monooxygenase hydroxylase subunit beta {ECO:0000303|PubMed:10903510};
DE Short=MSAMO hydroxylase subunit beta {ECO:0000303|PubMed:10903510};
GN Name=msmB {ECO:0000303|PubMed:10094704};
OS Methylosulfonomonas methylovora.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylosulfonomonas.
OX NCBI_TaxID=50057 {ECO:0000312|EMBL:AAD26620.1};
RN [1] {ECO:0000312|EMBL:AAD26620.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=M2 {ECO:0000312|EMBL:AAD26620.1};
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:AAD26620.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=M2 {ECO:0000312|EMBL:AAD26620.1};
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 1-20, SUBUNIT, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
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 67-79 AND 154-167, AND CATALYTIC ACTIVITY.
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 -!- 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 beta subunit family. {ECO:0000305}.
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DR EMBL; AF091716; AAD26620.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9X405; -.
DR SMR; Q9X405; -.
DR KEGG; ag:AAD26620; -.
DR BioCyc; MetaCyc:MON-14212; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018648; F:methanesulfonate monooxygenase activity; IEA:UniProtKB-EC.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF13577; SnoaL_4; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..181
FT /note="Methanesulfonate monooxygenase hydroxylase subunit
FT beta"
FT /id="PRO_0000430802"
SQ SEQUENCE 181 AA; 20479 MW; 9D3068F502E29FA6 CRC64;
MDIQTEMTAP PLSGGLDPAQ ARDAADAVRN AIYRATILLD SQKWDEWLAL CADNFVYDIK
AWSPEINYDM TYLHGSRKDL EALIRLLPKH NTDHSPLTRH TTIYTVDVAD EGATAKGVSA
FIVFQHLLDG TNSHIDAGES RLFLVGKYYD TFRIENGQAL FTSRETRLEN RRLDKGSHWP
I
