PMOA_METCA
ID PMOA_METCA Reviewed; 247 AA.
AC Q607G3; G1U9W5; O05112; Q49103;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Particulate methane monooxygenase beta subunit;
DE EC=1.14.18.3;
DE AltName: Full=Methane monooxygenase A subunit;
DE AltName: Full=Particulate methane monooxygenase 27 kDa subunit;
DE AltName: Full=Particulate methane monooxygenase hydroxylase 26 kDa subunit;
DE AltName: Full=Particulate methane monooxygenase hydroxylase beta subunit;
DE Short=pMMO-H beta subunit;
GN Name=pmoA1; Synonyms=pmoA; OrderedLocusNames=MCA1797;
GN and
GN Name=pmoA2; OrderedLocusNames=MCA2854;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=7768803; DOI=10.1128/jb.177.11.3071-3079.1995;
RA Semrau J.D., Chistoserdov A., Lebron J., Costello A., Davagnino J.,
RA Kenna E., Holmes A.J., Finch R., Murrell J.C., Lidstrom M.E.;
RT "Particulate methane monooxygenase genes in methanotrophs.";
RL J. Bacteriol. 177:3071-3079(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=10376840; DOI=10.1099/13500872-145-5-1235;
RA Stolyar S., Costello A.M., Peeples T.L., Lidstrom M.E.;
RT "Role of multiple gene copies in particulate methane monooxygenase activity
RT in the methane-oxidizing bacterium Methylococcus capsulatus Bath.";
RL Microbiology 145:1235-1244(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
RN [4]
RP PROTEIN SEQUENCE OF 6-33, AND SUBUNIT.
RX PubMed=9525893; DOI=10.1074/jbc.273.14.7957;
RA Nguyen H.H., Elliott S.J., Yip J.H., Chan S.I.;
RT "The particulate methane monooxygenase from methylococcus capsulatus (Bath)
RT is a novel copper-containing three-subunit enzyme. Isolation and
RT characterization.";
RL J. Biol. Chem. 273:7957-7966(1998).
RN [5]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7646068; DOI=10.1006/abbi.1995.1413;
RA Shiemke A.K., Cook S.A., Miley T., Singleton P.;
RT "Detergent solubilization of membrane-bound methane monooxygenase requires
RT plastoquinol analogs as electron donors.";
RL Arch. Biochem. Biophys. 321:421-428(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12379148; DOI=10.1042/bj20020823;
RA Basu P., Katterle B., Andersson K.K., Dalton H.;
RT "The membrane-associated form of methane mono-oxygenase from Methylococcus
RT capsulatus (Bath) is a copper/iron protein.";
RL Biochem. J. 369:417-427(2003).
RN [7]
RP ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=16101279; DOI=10.1021/bi050820u;
RA Kitmitto A., Myronova N., Basu P., Dalton H.;
RT "Characterization and structural analysis of an active particulate methane
RT monooxygenase trimer from Methylococcus capsulatus (Bath).";
RL Biochemistry 44:10954-10965(2005).
RN [8]
RP FUNCTION, CRYOELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=17002291; DOI=10.1021/bi061294p;
RA Myronova N., Kitmitto A., Collins R.F., Miyaji A., Dalton H.;
RT "Three-dimensional structure determination of a protein supercomplex that
RT oxidizes methane to formaldehyde in Methylococcus capsulatus (Bath).";
RL Biochemistry 45:11905-11914(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15674245; DOI=10.1038/nature03311;
RA Lieberman R.L., Rosenzweig A.C.;
RT "Crystal structure of a membrane-bound metalloenzyme that catalyses the
RT biological oxidation of methane.";
RL Nature 434:177-182(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22013879; DOI=10.1021/bi200801z;
RA Smith S.M., Rawat S., Telser J., Hoffman B.M., Stemmler T.L.,
RA Rosenzweig A.C.;
RT "Crystal structure and characterization of particulate methane
RT monooxygenase from Methylocystis species strain M.";
RL Biochemistry 50:10231-10240(2011).
CC -!- FUNCTION: Non-catalytic subunit of the methane monooxygenase that is
CC responsible for the initial oxygenation of methane to methanol in
CC methanotrophs. At least in vitro, specific quinols can replace NADH as
CC reductants. {ECO:0000269|PubMed:10376840, ECO:0000269|PubMed:17002291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + methane + O2 = a quinone + H2O + methanol;
CC Xref=Rhea:RHEA:30355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16183, ChEBI:CHEBI:17790, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124; EC=1.14.18.3;
CC Evidence={ECO:0000269|PubMed:7646068};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=24.2 nmol/min/mg enzyme (with NADH as reductant)
CC {ECO:0000269|PubMed:7646068};
CC Vmax=4.4 nmol/min/mg enzyme (with decyl-plastoquinol as reductant)
CC {ECO:0000269|PubMed:7646068};
CC Vmax=2.9 nmol/min/mg enzyme (with duroquinol as reductant)
CC {ECO:0000269|PubMed:7646068};
CC Note=Kinetic parameters have been established with the pMMO
CC heteromeric complex.;
CC -!- SUBUNIT: M.capsulatus has two forms of methane monooxygenase, a soluble
CC (sMMO) and a membrane-bound (particulate) type (pMMO). The particulate
CC type is a nonamer composed of three alpha:beta:gamma heterotrimeric
CC protomers assembled into a cylindrical structure; the beta and gamma
CC subunits comprise the bulk of the membrane-spanning regions and the
CC soluble regions are derived primarily from alpha subunits which form
CC two antiparallel beta-barrel-like structures each. This assembly, also
CC called pMMO hydroxylase (pMMO-H), is proposed to associate with
CC methanol dehydrogenase (MDH), also designated as pMMO-R, to form the
CC pMMO-C complex which seems to have greater methane monooxygenase
CC activity. {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245,
CC ECO:0000269|PubMed:16101279, ECO:0000269|PubMed:17002291,
CC ECO:0000269|PubMed:22013879, ECO:0000269|PubMed:9525893}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12379148,
CC ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12379148,
CC ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879}. Note=Located
CC in intracellular membranes.
CC -!- MISCELLANEOUS: Products of both gene copies, pmoA1 and pmoA2, are
CC required for full cellular activity.
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DR EMBL; L40804; AAB49821.1; -; Genomic_DNA.
DR EMBL; U94337; AAB51065.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU91114.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU92182.1; -; Genomic_DNA.
DR RefSeq; WP_010961050.1; NC_002977.6.
DR PDB; 1YEW; X-ray; 2.80 A; B/F/J=1-247.
DR PDB; 3RGB; X-ray; 2.80 A; B/F/J=1-247.
DR PDB; 7EV9; EM; 2.60 A; B/F/J=1-247.
DR PDB; 7S4H; EM; 2.14 A; B/F/J=1-247.
DR PDB; 7S4I; EM; 2.26 A; B/F/J=1-247.
DR PDB; 7S4J; EM; 2.16 A; B/F/J=1-247.
DR PDB; 7S4K; EM; 2.36 A; B/F/J=1-247.
DR PDB; 7T4O; EM; 3.65 A; B/F/J=1-247.
DR PDB; 7T4P; EM; 3.62 A; B/F/J=1-247.
DR PDBsum; 1YEW; -.
DR PDBsum; 3RGB; -.
DR PDBsum; 7EV9; -.
DR PDBsum; 7S4H; -.
DR PDBsum; 7S4I; -.
DR PDBsum; 7S4J; -.
DR PDBsum; 7S4K; -.
DR PDBsum; 7T4O; -.
DR PDBsum; 7T4P; -.
DR AlphaFoldDB; Q607G3; -.
DR SMR; Q607G3; -.
DR STRING; 243233.MCA1797; -.
DR EnsemblBacteria; AAU91114; AAU91114; MCA2854.
DR EnsemblBacteria; AAU92182; AAU92182; MCA1797.
DR KEGG; mca:MCA1797; -.
DR KEGG; mca:MCA2854; -.
DR eggNOG; ENOG502Z9FM; Bacteria.
DR HOGENOM; CLU_1123603_0_0_6; -.
DR OMA; MHFMLLA; -.
DR OrthoDB; 1041245at2; -.
DR BioCyc; MetaCyc:MON-3881; -.
DR BRENDA; 1.14.18.3; 3305.
DR EvolutionaryTrace; Q607G3; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015050; C:methane monooxygenase complex; ISS:JCVI.
DR GO; GO:0015049; F:methane monooxygenase activity; ISS:JCVI.
DR GO; GO:0015947; P:methane metabolic process; ISS:JCVI.
DR Gene3D; 1.20.1450.10; -; 1.
DR InterPro; IPR037001; NH3/CH4_mOase_suA_sf.
DR InterPro; IPR003393; NH3_CH4_mOase_A.
DR Pfam; PF02461; AMO; 1.
DR TIGRFAMs; TIGR03080; CH4_NH3mon_ox_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..247
FT /note="Particulate methane monooxygenase beta subunit"
FT /id="PRO_0000419131"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Y -> N (in Ref. 1 and 2; AAB49821)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 12..33
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:7EV9"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:7EV9"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:1YEW"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1YEW"
FT HELIX 212..237
FT /evidence="ECO:0007829|PDB:7EV9"
SQ 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
