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-MAY-2023, entry version 114. 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; 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 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}. 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; 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 PDB; 7M8Q; X-ray; 2.08 A; A/E=12-526. DR PDB; 7M8R; X-ray; 2.22 A; A/E=12-526. DR PDB; 7S6Q; X-ray; 1.96 A; A/E=12-526. DR PDB; 7S6R; X-ray; 1.89 A; A/E=12-526. DR PDB; 7S6T; X-ray; 1.82 A; A/E=12-526. DR PDB; 7S7H; X-ray; 2.40 A; A/E=12-526. 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 PDBsum; 7M8Q; -. DR PDBsum; 7M8R; -. DR PDBsum; 7S6Q; -. DR PDBsum; 7S6R; -. DR PDBsum; 7S6T; -. DR PDBsum; 7S7H; -. 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 CDD; cd01057; AAMH_A; 1. DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; Ferritin-like; 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 //