ID   MEMG_METTR              Reviewed;         169 AA.
AC   P27355;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-SEP-2023, entry version 97.
DE   RecName: Full=Methane monooxygenase component A gamma chain;
DE            EC=1.14.13.25;
DE   AltName: Full=Methane hydroxylase;
GN   Name=mmoZ;
OS   Methylosinus trichosporium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylocystaceae; Methylosinus.
OX   NCBI_TaxID=426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35070 / NCIMB 11131 / ACM 3311 / OB3b;
RX   PubMed=1904125; DOI=10.1111/j.1365-2958.1991.tb02114.x;
RA   Cardy D.L.N., Laidler V., Salmond G.P.C., Murrell J.C.;
RT   "Molecular analysis of the methane monooxygenase (MMO) gene cluster of
RT   Methylosinus trichosporium OB3b.";
RL   Mol. Microbiol. 5:335-342(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-12.
RX   PubMed=1845980; DOI=10.1016/s0021-9258(18)52470-4;
RA   Fox B.G., Liu Y., Dege J.E., Lipscomb J.D.;
RT   "Complex formation between the protein components of methane monooxygenase
RT   from Methylosinus trichosporium OB3b. Identification of sites of component
RT   interaction.";
RL   J. Biol. Chem. 266:540-550(1991).
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.trichosporium has two forms of methane monooxygenase, a
CC       soluble and a membrane-bound type. The soluble type consists of four
CC       components (A to D): protein A, comprising three chains, in an alpha-2,
CC       beta-2, gamma-2 configuration, is a nonheme iron protein containing an
CC       unusual mu-hydroxo bridge structure at its active site and interacts
CC       with both oxygen and methane.
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DR   EMBL; X55394; CAA39071.1; -; Genomic_DNA.
DR   PIR; S15210; C39049.
DR   PDB; 1MHY; X-ray; 2.00 A; G=1-169.
DR   PDB; 1MHZ; X-ray; 2.70 A; G=1-169.
DR   PDBsum; 1MHY; -.
DR   PDBsum; 1MHZ; -.
DR   AlphaFoldDB; P27355; -.
DR   SMR; P27355; -.
DR   BioCyc; MetaCyc:MONOMER-3869; -.
DR   BRENDA; 1.14.13.25; 3322.
DR   EvolutionaryTrace; P27355; -.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1845980"
FT   CHAIN           2..169
FT                   /note="Methane monooxygenase component A gamma chain"
FT                   /id="PRO_0000096410"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           11..21
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           26..40
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   TURN            49..53
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           54..72
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           75..80
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           88..100
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           105..119
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   TURN            120..123
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           126..144
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   TURN            145..149
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   HELIX           153..160
FT                   /evidence="ECO:0007829|PDB:1MHY"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:1MHY"
SQ   SEQUENCE   169 AA;  19326 MW;  460D4D8D234C2229 CRC64;
     MAKREPIHDN SIRTEWEAKI AKLTSVDQAT KFIQDFRLAY TSPFRKSYDI DVDYQYIERK
     IEEKLSVLKT EKLPVADLIT KATTGEDRAA VEATWIAKIK AAKSKYEADG IHIEFRQLYK
     PPVLPVNVFL RTDAALGTVL MEIRNTDYYG TPLEGLRKEP GVKVLHLQA
//