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   27-MAR-2024, entry version 145.
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; Pseudomonadota; 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   PDB; 7TC7; EM; 2.90 A; G/H=1-170.
DR   PDB; 7TC8; EM; 2.40 A; G/H=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   PDBsum; 7TC7; -.
DR   PDBsum; 7TC8; -.
DR   AlphaFoldDB; P11987; -.
DR   BMRB; P11987; -.
DR   SMR; P11987; -.
DR   DIP; DIP-59863N; -.
DR   IntAct; P11987; 1.
DR   STRING; 243233.MCA1198; -.
DR   KEGG; mca:MCA1198; -.
DR   eggNOG; ENOG5030P72; Bacteria.
DR   HOGENOM; CLU_1568905_0_0_6; -.
DR   BioCyc; MetaCyc:MONOMER-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; Methane monooxygenase, gamma chain, domain 1; 1.
DR   Gene3D; 1.20.1280.30; Methane monooxygenase, gamma chain, domain 2; 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; Methane monooxygenase hydrolase, gamma subunit; 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
//