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Particulate methane monooxygenase beta subunit (EC 1.14.18.3) (Methane monooxygenase A subunit) (Particulate methane monooxygenase 27 kDa subunit) (Particulate methane monooxygenase hydroxylase 26 kDa subunit) (Particulate methane monooxygenase hydroxylase beta subunit) (pMMO-H beta subunit)

 PMOA_METCA              Reviewed;         247 AA.
Q607G3; G1U9W5; O05112; Q49103;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
18-JUL-2018, entry version 89.
RecName: Full=Particulate methane monooxygenase beta subunit;
EC=1.14.18.3;
AltName: Full=Methane monooxygenase A subunit;
AltName: Full=Particulate methane monooxygenase 27 kDa subunit;
AltName: Full=Particulate methane monooxygenase hydroxylase 26 kDa subunit;
AltName: Full=Particulate methane monooxygenase hydroxylase beta subunit;
Short=pMMO-H beta subunit;
Name=pmoA1; Synonyms=pmoA; OrderedLocusNames=MCA1797;
and
Name=pmoA2; OrderedLocusNames=MCA2854;
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
Methylococcaceae; Methylococcus.
NCBI_TaxID=243233;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
PubMed=7768803; DOI=10.1128/jb.177.11.3071-3079.1995;
Semrau J.D., Chistoserdov A., Lebron J., Costello A., Davagnino J.,
Kenna E., Holmes A.J., Finch R., Murrell J.C., Lidstrom M.E.;
"Particulate methane monooxygenase genes in methanotrophs.";
J. Bacteriol. 177:3071-3079(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
PubMed=10376840; DOI=10.1099/13500872-145-5-1235;
Stolyar S., Costello A.M., Peeples T.L., Lidstrom M.E.;
"Role of multiple gene copies in particulate methane monooxygenase
activity in the methane-oxidizing bacterium Methylococcus capsulatus
Bath.";
Microbiology 145:1235-1244(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E.,
Ravel J., Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R.,
Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J.,
Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S.,
Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R.,
Eisen J.A.;
"Genomic insights into methanotrophy: the complete genome sequence of
Methylococcus capsulatus (Bath).";
PLoS Biol. 2:1616-1628(2004).
[4]
PROTEIN SEQUENCE OF 6-33, AND SUBUNIT.
PubMed=9525893; DOI=10.1074/jbc.273.14.7957;
Nguyen H.H., Elliott S.J., Yip J.H., Chan S.I.;
"The particulate methane monooxygenase from methylococcus capsulatus
(Bath) is a novel copper-containing three-subunit enzyme. Isolation
and characterization.";
J. Biol. Chem. 273:7957-7966(1998).
[5]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7646068; DOI=10.1006/abbi.1995.1413;
Shiemke A.K., Cook S.A., Miley T., Singleton P.;
"Detergent solubilization of membrane-bound methane monooxygenase
requires plastoquinol analogs as electron donors.";
Arch. Biochem. Biophys. 321:421-428(1995).
[6]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=12379148; DOI=10.1042/BJ20020823;
Basu P., Katterle B., Andersson K.K., Dalton H.;
"The membrane-associated form of methane mono-oxygenase from
Methylococcus capsulatus (Bath) is a copper/iron protein.";
Biochem. J. 369:417-427(2003).
[7]
ELECTRON MICROSCOPY, AND SUBUNIT.
PubMed=16101279; DOI=10.1021/bi050820u;
Kitmitto A., Myronova N., Basu P., Dalton H.;
"Characterization and structural analysis of an active particulate
methane monooxygenase trimer from Methylococcus capsulatus (Bath).";
Biochemistry 44:10954-10965(2005).
[8]
FUNCTION, CRYOELECTRON MICROSCOPY, AND SUBUNIT.
PubMed=17002291; DOI=10.1021/bi061294p;
Myronova N., Kitmitto A., Collins R.F., Miyaji A., Dalton H.;
"Three-dimensional structure determination of a protein supercomplex
that oxidizes methane to formaldehyde in Methylococcus capsulatus
(Bath).";
Biochemistry 45:11905-11914(2006).
[9]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=15674245; DOI=10.1038/nature03311;
Lieberman R.L., Rosenzweig A.C.;
"Crystal structure of a membrane-bound metalloenzyme that catalyses
the biological oxidation of methane.";
Nature 434:177-182(2005).
[10]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=22013879; DOI=10.1021/bi200801z;
Smith S.M., Rawat S., Telser J., Hoffman B.M., Stemmler T.L.,
Rosenzweig A.C.;
"Crystal structure and characterization of particulate methane
monooxygenase from Methylocystis species strain M.";
Biochemistry 50:10231-10240(2011).
-!- FUNCTION: Non-catalytic subunit of the methane monooxygenase that
is responsible for the initial oxygenation of methane to methanol
in methanotrophs. At least in vitro, specific quinols can replace
NADH as reductants. {ECO:0000269|PubMed:10376840,
ECO:0000269|PubMed:17002291}.
-!- CATALYTIC ACTIVITY: Methane + quinol + O(2) = methanol + quinone +
H(2)O. {ECO:0000269|PubMed:7646068}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Vmax=24.2 nmol/min/mg enzyme (with NADH as reductant)
{ECO:0000269|PubMed:7646068};
Vmax=4.4 nmol/min/mg enzyme (with decyl-plastoquinol as
reductant) {ECO:0000269|PubMed:7646068};
Vmax=2.9 nmol/min/mg enzyme (with duroquinol as reductant)
{ECO:0000269|PubMed:7646068};
Note=Kinetic parameters have been established with the pMMO
heteromeric complex.;
-!- SUBUNIT: M.capsulatus has two forms of methane monooxygenase, a
soluble (sMMO) and a membrane-bound (particulate) type (pMMO). The
particulate type is a nonamer composed of three alpha:beta:gamma
heterotrimeric protomers assembled into a cylindrical structure;
the beta and gamma subunits comprise the bulk of the membrane-
spanning regions and the soluble regions are derived primarily
from alpha subunits which form two antiparallel beta-barrel-like
structures each. This assembly, also called pMMO hydroxylase
(pMMO-H), is proposed to associate with methanol dehydrogenase
(MDH), also designated as pMMO-R, to form the pMMO-C complex which
seems to have greater methane monooxygenase activity.
{ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245,
ECO:0000269|PubMed:16101279, ECO:0000269|PubMed:17002291,
ECO:0000269|PubMed:22013879, ECO:0000269|PubMed:9525893}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12379148,
ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}; Multi-
pass membrane protein {ECO:0000269|PubMed:12379148,
ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}.
Note=Located in intracellular membranes.
-!- MISCELLANEOUS: Products of both gene copies, pmoA1 and pmoA2, are
required for full cellular activity.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L40804; AAB49821.1; -; Genomic_DNA.
EMBL; U94337; AAB51065.1; -; Genomic_DNA.
EMBL; AE017282; AAU91114.1; -; Genomic_DNA.
EMBL; AE017282; AAU92182.1; -; Genomic_DNA.
RefSeq; WP_010961050.1; NC_002977.6.
PDB; 1YEW; X-ray; 2.80 A; B/F/J=1-247.
PDB; 3RGB; X-ray; 2.80 A; B/F/J=1-247.
PDBsum; 1YEW; -.
PDBsum; 3RGB; -.
ProteinModelPortal; Q607G3; -.
STRING; 243233.MCA2854; -.
EnsemblBacteria; AAU91114; AAU91114; MCA2854.
EnsemblBacteria; AAU92182; AAU92182; MCA1797.
KEGG; mca:MCA1797; -.
KEGG; mca:MCA2854; -.
eggNOG; ENOG4105E7Z; Bacteria.
eggNOG; ENOG4110CTU; LUCA.
HOGENOM; HOG000029228; -.
KO; K10944; -.
OMA; DWKDRQW; -.
OrthoDB; POG091H1JD3; -.
BioCyc; MetaCyc:MONOMER-3881; -.
BRENDA; 1.14.18.3; 3305.
EvolutionaryTrace; Q607G3; -.
Proteomes; UP000006821; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015050; C:methane monooxygenase complex; ISS:JCVI.
GO; GO:0015049; F:methane monooxygenase activity; ISS:JCVI.
GO; GO:0015947; P:methane metabolic process; ISS:JCVI.
Gene3D; 1.20.1450.10; -; 1.
InterPro; IPR037001; NH3/CH4_mOase_suA_sf.
InterPro; IPR003393; NH3_CH4_mOase_A.
Pfam; PF02461; AMO; 1.
TIGRFAMs; TIGR03080; CH4_NH3mon_ox_A; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Membrane;
Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 247 Particulate methane monooxygenase beta
subunit.
/FTId=PRO_0000419131.
TRANSMEM 23 43 Helical. {ECO:0000255}.
TRANSMEM 59 79 Helical. {ECO:0000255}.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TRANSMEM 111 131 Helical. {ECO:0000255}.
TRANSMEM 145 165 Helical. {ECO:0000255}.
TRANSMEM 215 235 Helical. {ECO:0000255}.
CONFLICT 17 17 Missing (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 173 173 Y -> N (in Ref. 1 and 2; AAB49821).
{ECO:0000305}.
HELIX 13 43 {ECO:0000244|PDB:3RGB}.
STRAND 48 50 {ECO:0000244|PDB:3RGB}.
HELIX 52 54 {ECO:0000244|PDB:3RGB}.
HELIX 59 68 {ECO:0000244|PDB:3RGB}.
HELIX 70 83 {ECO:0000244|PDB:3RGB}.
HELIX 88 106 {ECO:0000244|PDB:3RGB}.
HELIX 107 111 {ECO:0000244|PDB:3RGB}.
HELIX 116 119 {ECO:0000244|PDB:3RGB}.
HELIX 125 136 {ECO:0000244|PDB:3RGB}.
HELIX 141 164 {ECO:0000244|PDB:3RGB}.
HELIX 165 168 {ECO:0000244|PDB:3RGB}.
STRAND 170 173 {ECO:0000244|PDB:3RGB}.
STRAND 176 179 {ECO:0000244|PDB:3RGB}.
HELIX 180 187 {ECO:0000244|PDB:3RGB}.
TURN 200 205 {ECO:0000244|PDB:1YEW}.
TURN 208 210 {ECO:0000244|PDB:1YEW}.
HELIX 215 238 {ECO:0000244|PDB:3RGB}.
SEQUENCE 247 AA; 28425 MW; 3341AA1A46A53F8F CRC64;
MSAAQSAVRS HAEAVQVSRT IDWMALFVVF FVIVGSYHIH AMLTMGDWDF WSDWKDRRLW
VTVTPIVLVT FPAAVQSYLW ERYRLPWGAT VCVLGLLLGE WINRYFNFWG WTYFPINFVF
PASLVPGAII LDTVLMLSGS YLFTAIVGAM GWGLIFYPGN WPIIAPLHVP VEYNGMLMSI
ADIQGYNYVR TGTPEYIRMV EKGTLRTFGK DVAPVSAFFS AFMSILIYFM WHFIGRWFSN
ERFLQST


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