MEMG_METCA
ID MEMG_METCA Reviewed; 170 AA.
AC P11987; Q609N4; Q9RLQ5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Methane monooxygenase component A gamma chain;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
GN Name=mmoZ; OrderedLocusNames=MCA1198;
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=2505721; DOI=10.1007/bf00456094;
RA Stainthorpe A.C., Murrell J.C., Salmond G.P.C., Dalton H., Lees V.;
RT "Molecular analysis of methane monooxygenase from Methylococcus capsulatus
RT (Bath).";
RL Arch. Microbiol. 152:154-159(1989).
RN [2]
RP SEQUENCE REVISION TO 21-22.
RA McDonald I., Murrell J.C.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 2-40.
RA Mullens I.A., Dalton H.;
RT "Cloning of the gamma-subunit methane monooxygenase from Methylococcus
RT capsulatus.";
RL Biotechnology (N.Y.) 5:490-493(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 166-170.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=2205538; DOI=10.1016/0378-1119(90)90158-n;
RA Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.;
RT "The methane monooxygenase gene cluster of Methylococcus capsulatus
RT (Bath).";
RL Gene 91:27-34(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8255292; DOI=10.1038/366537a0;
RA Rosenzweig A.C., Frederick C.A., Lippard S.J., Nordlund P.;
RT "Crystal structure of a bacterial non-haem iron hydroxylase that catalyses
RT the biological oxidation of methane.";
RL Nature 366:537-543(1993).
CC -!- FUNCTION: Responsible for the initial oxygenation of methane to
CC methanol in methanotrophs. It also catalyzes the monohydroxylation of a
CC variety of unactivated alkenes, alicyclic, aromatic and heterocyclic
CC compounds.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + methane + NADH + O2 = H2O + methanol + NAD(+);
CC Xref=Rhea:RHEA:13637, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.25;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+);
CC Xref=Rhea:RHEA:13641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16183, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.25;
CC -!- SUBUNIT: M.capsulatus has two forms of methane monooxygenase, a soluble
CC and a membrane-bound type. The soluble type consists of four components
CC (A to D): protein A, comprising three chains, in an alpha-2, beta-2,
CC gamma-2 configuration, is a nonheme iron protein containing an unusual
CC mu-hydroxo bridge structure at its active site and interacts with both
CC oxygen and methane.
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DR EMBL; M90050; AAF04157.2; -; Genomic_DNA.
DR EMBL; AE017282; AAU92724.1; -; Genomic_DNA.
DR PIR; JL0102; JL0102.
DR RefSeq; WP_010960485.1; NC_002977.6.
DR PDB; 1FYZ; X-ray; 2.15 A; E/F=1-170.
DR PDB; 1FZ0; X-ray; 2.07 A; E/F=1-170.
DR PDB; 1FZ1; X-ray; 1.96 A; E/F=1-170.
DR PDB; 1FZ2; X-ray; 2.15 A; E/F=1-170.
DR PDB; 1FZ3; X-ray; 2.03 A; E/F=1-170.
DR PDB; 1FZ4; X-ray; 2.38 A; E/F=1-170.
DR PDB; 1FZ5; X-ray; 2.40 A; E/F=1-170.
DR PDB; 1FZ6; X-ray; 2.05 A; E/F=1-170.
DR PDB; 1FZ7; X-ray; 1.96 A; E/F=1-170.
DR PDB; 1FZ8; X-ray; 2.10 A; E/F=1-170.
DR PDB; 1FZ9; X-ray; 2.30 A; E/F=1-170.
DR PDB; 1FZH; X-ray; 2.60 A; E/F=1-170.
DR PDB; 1FZI; X-ray; 3.30 A; E/F=1-170.
DR PDB; 1MMO; X-ray; 2.20 A; G/H=4-165.
DR PDB; 1MTY; X-ray; 1.70 A; G/H=4-165.
DR PDB; 1XMF; X-ray; 2.32 A; E/F=2-170.
DR PDB; 1XMG; X-ray; 2.10 A; E/F=2-170.
DR PDB; 1XMH; X-ray; 2.32 A; E/F=2-170.
DR PDB; 1XU3; X-ray; 2.30 A; E/F=1-170.
DR PDB; 1XU5; X-ray; 1.96 A; E/F=1-170.
DR PDB; 1XVB; X-ray; 1.80 A; E/F=1-170.
DR PDB; 1XVC; X-ray; 2.00 A; E/F=1-170.
DR PDB; 1XVD; X-ray; 2.30 A; E/F=1-170.
DR PDB; 1XVE; X-ray; 2.40 A; E/F=1-170.
DR PDB; 1XVF; X-ray; 2.00 A; E/F=1-170.
DR PDB; 1XVG; X-ray; 1.96 A; E/F=1-170.
DR PDB; 4GAM; X-ray; 2.90 A; C/H/M/R=1-170.
DR PDBsum; 1FYZ; -.
DR PDBsum; 1FZ0; -.
DR PDBsum; 1FZ1; -.
DR PDBsum; 1FZ2; -.
DR PDBsum; 1FZ3; -.
DR PDBsum; 1FZ4; -.
DR PDBsum; 1FZ5; -.
DR PDBsum; 1FZ6; -.
DR PDBsum; 1FZ7; -.
DR PDBsum; 1FZ8; -.
DR PDBsum; 1FZ9; -.
DR PDBsum; 1FZH; -.
DR PDBsum; 1FZI; -.
DR PDBsum; 1MMO; -.
DR PDBsum; 1MTY; -.
DR PDBsum; 1XMF; -.
DR PDBsum; 1XMG; -.
DR PDBsum; 1XMH; -.
DR PDBsum; 1XU3; -.
DR PDBsum; 1XU5; -.
DR PDBsum; 1XVB; -.
DR PDBsum; 1XVC; -.
DR PDBsum; 1XVD; -.
DR PDBsum; 1XVE; -.
DR PDBsum; 1XVF; -.
DR PDBsum; 1XVG; -.
DR PDBsum; 4GAM; -.
DR AlphaFoldDB; P11987; -.
DR BMRB; P11987; -.
DR SMR; P11987; -.
DR DIP; DIP-59863N; -.
DR IntAct; P11987; 1.
DR STRING; 243233.MCA1198; -.
DR EnsemblBacteria; AAU92724; AAU92724; MCA1198.
DR KEGG; mca:MCA1198; -.
DR eggNOG; ENOG5030P72; Bacteria.
DR HOGENOM; CLU_1568905_0_0_6; -.
DR OMA; DSLWIEA; -.
DR OrthoDB; 1742115at2; -.
DR BioCyc; MetaCyc:MON-3863; -.
DR BRENDA; 1.14.13.25; 3305.
DR EvolutionaryTrace; P11987; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0106317; F:methane monooxygenase NADH activity; IEA:UniProtKB-EC.
DR GO; GO:0106318; F:methane monooxygenase NADPH activity; IEA:UniProtKB-EC.
DR GO; GO:0015947; P:methane metabolic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1280.10; -; 1.
DR Gene3D; 1.20.1280.30; -; 1.
DR InterPro; IPR004222; Me_mOase_g.
DR InterPro; IPR015952; Me_mOase_g_dom1.
DR InterPro; IPR015953; Me_mOase_g_dom2.
DR InterPro; IPR036123; Me_mOase_sf_g.
DR Pfam; PF02964; MeMO_Hyd_G; 1.
DR PIRSF; PIRSF018503; Me_mOase_g; 1.
DR SUPFAM; SSF47152; SSF47152; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Monooxygenase; NADP;
KW One-carbon metabolism; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..170
FT /note="Methane monooxygenase component A gamma chain"
FT /id="PRO_0000096409"
FT CONFLICT 21
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 48..52
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1XVB"
SQ SEQUENCE 170 AA; 19847 MW; 6030AF38130BA497 CRC64;
MAKLGIHSND TRDAWVNKIA QLNTLEKAAE MLKQFRMDHT TPFRNSYELD NDYLWIEAKL
EEKVAVLKAR AFNEVDFRHK TAFGEDAKSV LDGTVAKMNA AKDKWEAEKI HIGFRQAYKP
PIMPVNYFLD GERQLGTRLM ELRNLNYYDT PLEELRKQRG VRVVHLQSPH
