MEMA_METTR
ID MEMA_METTR Reviewed; 526 AA.
AC P27353;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Methane monooxygenase component A alpha chain;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
GN Name=mmoX;
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 SEQUENCE REVISION.
RA McDonald I.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 2 iron ions.;
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 -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; X55394; CAA39068.2; -; Genomic_DNA.
DR PIR; S15207; S15207.
DR PDB; 1MHY; X-ray; 2.00 A; D=1-526.
DR PDB; 1MHZ; X-ray; 2.70 A; D=1-526.
DR PDB; 6VK4; X-ray; 2.35 A; A/E=1-526.
DR PDB; 6VK5; X-ray; 1.86 A; A/E=1-526.
DR PDB; 6VK6; X-ray; 1.52 A; A=1-526.
DR PDB; 6VK7; X-ray; 2.12 A; A=1-526.
DR PDB; 6VK8; X-ray; 2.03 A; A/E=1-526.
DR PDB; 6YD0; X-ray; 1.95 A; D=1-526.
DR PDB; 6YDI; X-ray; 1.95 A; D=1-526.
DR PDB; 6YDU; X-ray; 1.95 A; D=1-526.
DR PDB; 6YY3; X-ray; 2.00 A; D=1-526.
DR PDBsum; 1MHY; -.
DR PDBsum; 1MHZ; -.
DR PDBsum; 6VK4; -.
DR PDBsum; 6VK5; -.
DR PDBsum; 6VK6; -.
DR PDBsum; 6VK7; -.
DR PDBsum; 6VK8; -.
DR PDBsum; 6YD0; -.
DR PDBsum; 6YDI; -.
DR PDBsum; 6YDU; -.
DR PDBsum; 6YY3; -.
DR AlphaFoldDB; P27353; -.
DR SMR; P27353; -.
DR BRENDA; 1.14.13.25; 3322.
DR EvolutionaryTrace; P27353; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Metal-binding;
KW Monooxygenase; NADP; One-carbon metabolism; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1845980"
FT CHAIN 2..526
FT /note="Methane monooxygenase component A alpha chain"
FT /id="PRO_0000096406"
FT ACT_SITE 151
FT /evidence="ECO:0000255"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 64..83
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 97..127
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 131..161
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 261..292
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 377..382
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:6YD0"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 469..473
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6VK6"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6VK6"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:6VK6"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:6VK6"
SQ SEQUENCE 526 AA; 59954 MW; A56F4AAD0A55726B CRC64;
MAISLATKAA TDALKVNRAP VGVEPQEVHK WLQSFNWDFK ENRTKYPTKY HMANETKEQF
KVIAKEYARM EAAKDERQFG TLLDGLTRLG AGNKVHPRWG ETMKVISNFL EVGEYNAIAA
SAMLWDSATA AEQKNGYLAQ VLDEIRHTHQ CAFINHYYSK HYHDPAGHND ARRTRAIGPL
WKGMKRVFAD GFISGDAVEC SVNLQLVGEA CFTNPLIVAV TEWASANGDE ITPTVFLSVE
TDELRHMANG YQTVVSIAND PASAKFLNTD LNNAFWTQQK YFTPVLGYLF EYGSKFKVEP
WVKTWNRWVY EDWGGIWIGR LGKYGVESPA SLRDAKRDAY WAHHDLALAA YAMWPLGFAR
LALPDEEDQA WFEANYPGWA DHYGKIFNEW KKLGYEDPKS GFIPYQWLLA NGHDVYIDRV
SQVPFIPSLA KGTGSLRVHE FNGKKHSLTD DWGERQWLIE PERYECHNVF EQYEGRELSE
VIAEGHGVRS DGKTLIAQPH TRGDNLWTLE DIKRAGCVFP DPLAKF
