PMOB_METCA
ID PMOB_METCA Reviewed; 414 AA.
AC G1UBD1; O08059; Q49104; Q607G4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Particulate methane monooxygenase alpha subunit;
DE EC=1.14.18.3;
DE AltName: Full=Methane monooxygenase B subunit;
DE AltName: Full=Particulate methane monooxygenase 45 kDa subunit;
DE AltName: Full=Particulate methane monooxygenase 47 kDa subunit;
DE AltName: Full=Particulate methane monooxygenase hydroxylase 45 kDa subunit;
DE AltName: Full=Particulate methane monooxygenase hydroxylase alpha subunit;
DE Short=pMMO-H alpha subunit;
DE Flags: Precursor;
GN Name=pmoB1; Synonyms=pmoB; OrderedLocusNames=MCA1796;
GN and
GN Name=pmoB2; OrderedLocusNames=MCA2853;
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], AND PROTEIN SEQUENCE OF 33-52.
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 33-65, 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, SUBUNIT, AND COFACTOR.
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 FUNCTION, AND MUTAGENESIS OF HIS-48; HIS-137 AND HIS-139.
RX PubMed=20410881; DOI=10.1038/nature08992;
RA Balasubramanian R., Smith S.M., Rawat S., Yatsunyk L.A., Stemmler T.L.,
RA Rosenzweig A.C.;
RT "Oxidation of methane by a biological dicopper centre.";
RL Nature 465:115-119(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 33-414 IN COMPLEX WITH COPPER
RP IONS, SUBCELLULAR LOCATION, SUBUNIT, AND COFACTOR.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 33-414 IN COMPLEX WITH COPPER
RP IONS, SUBUNIT, AND COFACTOR.
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: Methane monooxygenase is responsible for the initial
CC oxygenation of methane to methanol in methanotrophs. At least in vitro,
CC specific quinols can replace NADH as reductants.
CC {ECO:0000269|PubMed:10376840, ECO:0000269|PubMed:17002291,
CC ECO:0000269|PubMed:20410881}.
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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245,
CC ECO:0000269|PubMed:22013879};
CC Note=Binds 3 copper ions per subunit. Two of these (copper ion 1 and 3)
CC form a binuclear cluster. {ECO:0000269|PubMed:12379148,
CC ECO:0000269|PubMed:15674245, ECO:0000269|PubMed:22013879};
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}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12379148, ECO:0000269|PubMed:15674245}.
CC Note=Located in intracellular membranes.
CC -!- CAUTION: A dicopper center located in the alpha/pmoB subunit is
CC proposed as active site, in part based on mutagenesis studies using a
CC soluble pmoB construct in which its two cupredoxin domains have been
CC artificially bridged. However, the construct has only 10% methane
CC oxidation activity compared with the intact membrane-bound pMMO.
CC {ECO:0000305}.
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DR EMBL; L40804; AAB49822.1; -; Genomic_DNA.
DR EMBL; U94337; AAB51066.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU91115.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU92191.1; -; Genomic_DNA.
DR PIR; B57266; B57266.
DR RefSeq; WP_010961049.1; NC_002977.6.
DR PDB; 1YEW; X-ray; 2.80 A; A/E/I=33-414.
DR PDB; 3RGB; X-ray; 2.80 A; A/E/I=1-414.
DR PDB; 7EV9; EM; 2.60 A; A/E/I=1-414.
DR PDB; 7S4H; EM; 2.14 A; A/E/I=1-414.
DR PDB; 7S4I; EM; 2.26 A; A/E/I=1-414.
DR PDB; 7S4J; EM; 2.16 A; A/E/I=1-414.
DR PDB; 7S4K; EM; 2.36 A; A/E/I=1-414.
DR PDB; 7T4O; EM; 3.65 A; A/E/I=1-414.
DR PDB; 7T4P; EM; 3.62 A; A/E/I=1-414.
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; G1UBD1; -.
DR SMR; G1UBD1; -.
DR STRING; 243233.MCA1796; -.
DR PRIDE; G1UBD1; -.
DR EnsemblBacteria; AAU91115; AAU91115; MCA2853.
DR EnsemblBacteria; AAU92191; AAU92191; MCA1796.
DR KEGG; mca:MCA1796; -.
DR KEGG; mca:MCA2853; -.
DR eggNOG; ENOG502Z96N; Bacteria.
DR HOGENOM; CLU_660275_0_0_6; -.
DR OMA; ERSQEPF; -.
DR OrthoDB; 650121at2; -.
DR BioCyc; MetaCyc:MON-3882; -.
DR BRENDA; 1.14.18.3; 3305.
DR EvolutionaryTrace; G1UBD1; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.710; -; 1.
DR Gene3D; 2.60.120.570; -; 1.
DR Gene3D; 2.60.40.1580; -; 1.
DR InterPro; IPR006833; NH3_CH4_mOase_B.
DR InterPro; IPR023303; NH3_CH4_mOase_suB_C.
DR InterPro; IPR023141; NH3_CH4_mOase_suB_hlx_hairpin.
DR InterPro; IPR023301; NH3_CH4_mOase_suB_N.
DR Pfam; PF04744; Monooxygenase_B; 1.
DR TIGRFAMs; TIGR03079; CH4_NH3mon_ox_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Membrane; Metal-binding;
KW Monooxygenase; NAD; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:7768803,
FT ECO:0000269|PubMed:9525893"
FT CHAIN 33..414
FT /note="Particulate methane monooxygenase alpha subunit"
FT /id="PRO_5000142832"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 33..172
FT /note="Cupredoxin domain used to construct soluble pmoB
FT (spmoB)"
FT REGION 265..414
FT /note="Cupredoxin domain used to construct soluble pmoB
FT (spmoB)"
FT BINDING 33
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT BINDING 48
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT BINDING 72
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT BINDING 137
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT BINDING 139
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT BINDING 139
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15674245,
FT ECO:0000269|PubMed:22013879, ECO:0007744|PDB:1YEW,
FT ECO:0007744|PDB:3RGB"
FT MUTAGEN 48
FT /note="H->N: Impairs activity of soluble pmoB construct."
FT /evidence="ECO:0000269|PubMed:20410881"
FT MUTAGEN 137
FT /note="H->A: Abolishes activity of soluble pmoB construct;
FT when associated with A-139."
FT /evidence="ECO:0000269|PubMed:20410881"
FT MUTAGEN 139
FT /note="H->A: Abolishes activity of soluble pmoB construct;
FT when associated with A-137."
FT /evidence="ECO:0000269|PubMed:20410881"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3RGB"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 94..105
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:7EV9"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 148..161
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:7EV9"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 185..206
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 230..257
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 281..294
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 296..306
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:7EV9"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:7EV9"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:7EV9"
FT STRAND 400..412
FT /evidence="ECO:0007829|PDB:7EV9"
SQ SEQUENCE 414 AA; 46079 MW; 66AFC0C663F869BA CRC64;
MKTIKDRIAK WSAIGLLSAV AATAFYAPSA SAHGEKSQAA FMRMRTIHWY DLSWSKEKVK
INETVEIKGK FHVFEGWPET VDEPDVAFLN VGMPGPVFIR KESYIGGQLV PRSVRLEIGK
TYDFRVVLKA RRPGDWHVHT MMNVQGGGPI IGPGKWITVE GSMSEFRNPV TTLTGQTVDL
ENYNEGNTYF WHAFWFAIGV AWIGYWSRRP IFIPRLLMVD AGRADELVSA TDRKVAMGFL
AATILIVVMA MSSANSKYPI TIPLQAGTMR GMKPLELPAP TVSVKVEDAT YRVPGRAMRM
KLTITNHGNS PIRLGEFYTA SVRFLDSDVY KDTTGYPEDL LAEDGLSVSD NSPLAPGETR
TVDVTASDAA WEVYRLSDII YDPDSRFAGL LFFFDATGNR QVVQIDAPLI PSFM
