MEMA_METCA
ID MEMA_METCA Reviewed; 527 AA.
AC P22869; Q609N8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Methane monooxygenase component A alpha chain;
DE EC=1.14.13.25;
DE AltName: Full=Methane hydroxylase;
GN Name=mmoX; OrderedLocusNames=MCA1194;
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 1-6.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=2205538; DOI=10.1016/0378-1119(90)90158-n;
RA Stainthorpe A.C., Lees V., Salmond G.P.C., Dalton H., Murrell J.C.;
RT "The methane monooxygenase gene cluster of Methylococcus capsulatus
RT (Bath).";
RL Gene 91:27-34(1990).
RN [2]
RP SEQUENCE REVISION TO 84; 306 AND 444.
RA McDonald I., Murrell J.C.;
RL Submitted (MAY-2000) 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9432288; DOI=10.1016/1074-5521(95)90222-8;
RA Rosenzweig A.C., Nordlund P., Takahara P.M., Frederick C.A., Lippard S.J.;
RT "Geometry of the soluble methane monooxygenase catalytic diiron center in
RT two oxidation states.";
RL Chem. Biol. 2:409-418(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=9329079;
RX DOI=10.1002/(sici)1097-0134(199710)29:2<141::aid-prot2>3.0.co;2-g;
RA Rosenzweig A.C., Brandstetter H., Whittington D.A., Nordlund P.,
RA Lippard S.J., Frederick C.A.;
RT "Crystal structures of the methane monooxygenase hydroxylase from
RT Methylococcus capsulatus (Bath): implications for substrate gating and
RT component interactions.";
RL Proteins 29:141-152(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=11456616; DOI=10.1021/ja003240n;
RA Whittington D.A., Lippard S.J.;
RT "Crystal structures of the soluble methane monooxygenase hydroxylase from
RT Methylococcus capsulatus (Bath) demonstrating geometrical variability at
RT the dinuclear iron active site.";
RL J. Am. Chem. Soc. 123:827-838(2001).
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.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 P22869; P18798: mmoY; NbExp=5; IntAct=EBI-9023796, EBI-9023802;
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; M90050; AAB62392.3; -; Genomic_DNA.
DR EMBL; AE017282; AAU92736.1; -; Genomic_DNA.
DR PIR; JQ0702; JQ0702.
DR RefSeq; WP_010960482.1; NC_002977.6.
DR PDB; 1FYZ; X-ray; 2.15 A; A/B=1-527.
DR PDB; 1FZ0; X-ray; 2.07 A; A/B=1-527.
DR PDB; 1FZ1; X-ray; 1.96 A; A/B=1-527.
DR PDB; 1FZ2; X-ray; 2.15 A; A/B=1-527.
DR PDB; 1FZ3; X-ray; 2.03 A; A/B=1-527.
DR PDB; 1FZ4; X-ray; 2.38 A; A/B=1-527.
DR PDB; 1FZ5; X-ray; 2.40 A; A/B=1-527.
DR PDB; 1FZ6; X-ray; 2.05 A; A/B=1-527.
DR PDB; 1FZ7; X-ray; 1.96 A; A/B=1-527.
DR PDB; 1FZ8; X-ray; 2.10 A; A/B=1-527.
DR PDB; 1FZ9; X-ray; 2.30 A; A/B=1-527.
DR PDB; 1FZH; X-ray; 2.60 A; A/B=1-527.
DR PDB; 1FZI; X-ray; 3.30 A; A/B=1-527.
DR PDB; 1MMO; X-ray; 2.20 A; D/E=15-526.
DR PDB; 1MTY; X-ray; 1.70 A; D/E=15-526.
DR PDB; 1XMF; X-ray; 2.32 A; A/B=1-527.
DR PDB; 1XMG; X-ray; 2.10 A; A/B=1-527.
DR PDB; 1XMH; X-ray; 2.32 A; A/B=1-527.
DR PDB; 1XU3; X-ray; 2.30 A; A/B=1-527.
DR PDB; 1XU5; X-ray; 1.96 A; A/B=1-527.
DR PDB; 1XVB; X-ray; 1.80 A; A/B=1-527.
DR PDB; 1XVC; X-ray; 2.00 A; A/B=1-527.
DR PDB; 1XVD; X-ray; 2.30 A; A/B=1-527.
DR PDB; 1XVE; X-ray; 2.40 A; A/B=1-527.
DR PDB; 1XVF; X-ray; 2.00 A; A/B=1-527.
DR PDB; 1XVG; X-ray; 1.96 A; A/B=1-527.
DR PDB; 4GAM; X-ray; 2.90 A; A/F/K/P=1-527.
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; P22869; -.
DR BMRB; P22869; -.
DR SMR; P22869; -.
DR DIP; DIP-59861N; -.
DR IntAct; P22869; 3.
DR STRING; 243233.MCA1194; -.
DR DrugBank; DB04592; 3-Bromo-3-buten-1-ol.
DR DrugBank; DB04637; 6-Bromo-1-hexanol.
DR EnsemblBacteria; AAU92736; AAU92736; MCA1194.
DR KEGG; mca:MCA1194; -.
DR eggNOG; COG3350; Bacteria.
DR HOGENOM; CLU_040795_0_0_6; -.
DR OMA; RTGFTMQ; -.
DR OrthoDB; 147428at2; -.
DR BioCyc; MetaCyc:MON-3861; -.
DR BRENDA; 1.14.13.25; 3305.
DR EvolutionaryTrace; P22869; -.
DR Proteomes; UP000006821; Chromosome.
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;
KW Reference proteome.
FT CHAIN 1..527
FT /note="Methane monooxygenase component A alpha chain"
FT /id="PRO_0000096405"
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 BINDING 144
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT BINDING 209
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT BINDING 246
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT CONFLICT 306
FT /note="N -> D (in Ref. 2; AAB62392)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="Q -> E (in Ref. 2; AAB62392)"
FT /evidence="ECO:0000305"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 64..83
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 97..127
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 131..161
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 231..257
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1XMF"
FT HELIX 262..292
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:1XVB"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1XMG"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:4GAM"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1MTY"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:1MTY"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:1MTY"
FT HELIX 522..525
FT /evidence="ECO:0007829|PDB:1MTY"
SQ SEQUENCE 527 AA; 60646 MW; 953438FDF5208374 CRC64;
MALSTATKAA TDALAANRAP TSVNAQEVHR WLQSFNWDFK NNRTKYATKY KMANETKEQF
KLIAKEYARM EAVKDERQFG SLQDALTRLN AGVRVHPKWN ETMKVVSNFL EVGEYNAIAA
TGMLWDSAQA AEQKNGYLAQ VLDEIRHTHQ CAYVNYYFAK NGQDPAGHND ARRTRTIGPL
WKGMKRVFSD GFISGDAVEC SLNLQLVGEA CFTNPLIVAV TEWAAANGDE ITPTVFLSIE
TDELRHMANG YQTVVSIAND PASAKYLNTD LNNAFWTQQK YFTPVLGMLF EYGSKFKVEP
WVKTWNRWVY EDWGGIWIGR LGKYGVESPR SLKDAKQDAY WAHHDLYLLA YALWPTGFFR
LALPDQEEME WFEANYPGWY DHYGKIYEEW RARGCEDPSS GFIPLMWFIE NNHPIYIDRV
SQVPFCPSLA KGASTLRVHE YNGQMHTFSD QWGERMWLAE PERYECQNIF EQYEGRELSE
VIAELHGLRS DGKTLIAQPH VRGDKLWTLD DIKRLNCVFK NPVKAFN
