MEMB_METTR
ID MEMB_METTR Reviewed; 394 AA.
AC P27354;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Methane monooxygenase component A beta chain;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
GN Name=mmoY;
OS Methylosinus trichosporium.
OC Bacteria; Proteobacteria; 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 2-16.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55394; CAA39069.1; -; Genomic_DNA.
DR PIR; S15208; S15208.
DR PDB; 1MHY; X-ray; 2.00 A; B=1-394.
DR PDB; 1MHZ; X-ray; 2.70 A; B=1-394.
DR PDBsum; 1MHY; -.
DR PDBsum; 1MHZ; -.
DR AlphaFoldDB; P27354; -.
DR SMR; P27354; -.
DR BioCyc; MetaCyc:MON-3868; -.
DR BRENDA; 1.14.13.25; 3322.
DR EvolutionaryTrace; P27354; -.
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:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01058; AAMH_B; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012078; MP_mOase_hydro.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR PIRSF; PIRSF000040; MMOH_comp; 1.
DR SUPFAM; SSF47240; SSF47240; 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..394
FT /note="Methane monooxygenase component A beta chain"
FT /id="PRO_0000096408"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:1MHY"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1MHZ"
FT HELIX 109..133
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 141..145
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 148..172
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 176..206
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 280..302
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 313..338
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:1MHY"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:1MHY"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:1MHZ"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:1MHY"
SQ SEQUENCE 394 AA; 45020 MW; FA6C8F0970F28B90 CRC64;
MSQPQSSQVT KRGLTDPERA AIIAAAVPDH ALDTQRKYHY FIQPRWKPLS EYEQLSCYAQ
PNPDWIAGGL DWGDWTQKFH GGRPSWGNES TELRTTDWYR HRDPARRWHH PYVKDKSEEA
RYTQRFLAAY SSEGSIRTID PYWRDEILNK YFGALLYSEY GLFNAHSSVG RDCLSDTIRQ
TAVFAALDKV DNAQMIQMER LFIAKLVPGF DASTDVPKKI WTTDPIYSGA RATVQEIWQG
VQDWNEILWA GHAVMIATFG QFARREFFQR LATVYGDTLT PFFTAQSQTY FQTTRGAIDD
LFVYCLANDS EFGAHNRTFL NAWTEHYLAS SVAALKDFVG LYAKVEKSRA DRSRRRLRGA
AASSAIGRSI TPDKIGFRVD VDQKVDAVLA GYKN
