MEMB_METCA
ID MEMB_METCA Reviewed; 389 AA.
AC P18798; Q609N7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Methane monooxygenase component A beta chain;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
GN Name=mmoY; OrderedLocusNames=MCA1195;
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-41.
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 142-145 AND C-TERMINUS.
RA McDonald I., Murrell J.C.;
RL Submitted (OCT-1999) 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 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.
CC -!- INTERACTION:
CC P18798; P22869: mmoX; NbExp=5; IntAct=EBI-9023802, EBI-9023796;
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DR EMBL; M90050; AAB62393.2; -; Genomic_DNA.
DR EMBL; AE017282; AAU92727.1; -; Genomic_DNA.
DR PIR; A61412; A61412.
DR PIR; JL0101; JL0101.
DR RefSeq; WP_010960483.1; NC_002977.6.
DR PDB; 1FYZ; X-ray; 2.15 A; C/D=1-389.
DR PDB; 1FZ0; X-ray; 2.07 A; C/D=1-389.
DR PDB; 1FZ1; X-ray; 1.96 A; C/D=1-389.
DR PDB; 1FZ2; X-ray; 2.15 A; C/D=1-389.
DR PDB; 1FZ3; X-ray; 2.03 A; C/D=1-389.
DR PDB; 1FZ4; X-ray; 2.38 A; C/D=1-389.
DR PDB; 1FZ5; X-ray; 2.40 A; C/D=1-389.
DR PDB; 1FZ6; X-ray; 2.05 A; C/D=1-389.
DR PDB; 1FZ7; X-ray; 1.96 A; C/D=1-389.
DR PDB; 1FZ8; X-ray; 2.10 A; C/D=1-389.
DR PDB; 1FZ9; X-ray; 2.30 A; C/D=1-389.
DR PDB; 1FZH; X-ray; 2.60 A; C/D=1-389.
DR PDB; 1FZI; X-ray; 3.30 A; C/D=1-389.
DR PDB; 1MMO; X-ray; 2.20 A; B/C=6-389.
DR PDB; 1MTY; X-ray; 1.70 A; B/C=6-362.
DR PDB; 1XMF; X-ray; 2.32 A; C/D=2-389.
DR PDB; 1XMG; X-ray; 2.10 A; C/D=2-389.
DR PDB; 1XMH; X-ray; 2.32 A; C/D=2-389.
DR PDB; 1XU3; X-ray; 2.30 A; C/D=1-389.
DR PDB; 1XU5; X-ray; 1.96 A; C/D=1-389.
DR PDB; 1XVB; X-ray; 1.80 A; C/D=1-389.
DR PDB; 1XVC; X-ray; 2.00 A; C/D=1-389.
DR PDB; 1XVD; X-ray; 2.30 A; C/D=1-389.
DR PDB; 1XVE; X-ray; 2.40 A; C/D=1-389.
DR PDB; 1XVF; X-ray; 2.00 A; C/D=1-389.
DR PDB; 1XVG; X-ray; 1.96 A; C/D=1-389.
DR PDB; 4GAM; X-ray; 2.90 A; B/G/L/Q=1-389.
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 AlphaFoldDB; P18798; -.
DR BMRB; P18798; -.
DR SMR; P18798; -.
DR DIP; DIP-59862N; -.
DR IntAct; P18798; 1.
DR STRING; 243233.MCA1195; -.
DR EnsemblBacteria; AAU92727; AAU92727; MCA1195.
DR KEGG; mca:MCA1195; -.
DR eggNOG; ENOG502Z7Z9; Bacteria.
DR HOGENOM; CLU_690417_0_0_6; -.
DR OMA; KFHGGRP; -.
DR OrthoDB; 561064at2; -.
DR BioCyc; MetaCyc:MON-3862; -.
DR BRENDA; 1.14.13.25; 3305.
DR EvolutionaryTrace; P18798; -.
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: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; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2505721"
FT CHAIN 2..389
FT /note="Methane monooxygenase component A beta chain"
FT /id="PRO_0000096407"
FT CONFLICT 370
FT /note="R -> A (in Ref. 1; AAB62393)"
FT /evidence="ECO:0000305"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1XMH"
FT HELIX 106..129
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 173..203
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1MMO"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 276..299
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 310..335
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 349..366
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:1MTY"
SQ SEQUENCE 389 AA; 45133 MW; 1737FEA30EEA9875 CRC64;
MSMLGERRRG LTDPEMAAVI LKALPEAPLD GNNKMGYFVT PRWKRLTEYE ALTVYAQPNA
DWIAGGLDWG DWTQKFHGGR PSWGNETTEL RTVDWFKHRD PLRRWHAPYV KDKAEEWRYT
DRFLQGYSAD GQIRAMNPTW RDEFINRYWG AFLFNEYGLF NAHSQGAREA LSDVTRVSLA
FWGFDKIDIA QMIQLERGFL AKIVPGFDES TAVPKAEWTN GEVYKSARLA VEGLWQEVFD
WNESAFSVHA VYDALFGQFV RREFFQRLAP RFGDNLTPFF INQAQTYFQI AKQGVQDLYY
NCLGDDPEFS DYNRTVMRNW TGKWLEPTIA ALRDFMGLFA KLPAGTTDKE EITASLYRVV
DDWIEDYASR IDFKADRDQI VKAVLAGLK
