MMOD_METCA
ID MMOD_METCA Reviewed; 103 AA.
AC P22867; Q609N3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Methane monooxygenase component D;
GN Name=mmoD; OrderedLocusNames=MCA1199;
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].
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 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 [3]
RP PROTEIN SEQUENCE OF 1-5, MASS SPECTROMETRY, AND CHARACTERIZATION.
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath;
RX PubMed=11709550; DOI=10.1074/jbc.m107712200;
RA Merkx M., Lippard S.J.;
RT "Why OrfY? Characterization of MMOD, a long overlooked component of the
RT soluble methane monooxygenase from Methylococcus capsulatus.";
RL J. Biol. Chem. 277:5858-5865(2002).
CC -!- SUBUNIT: The soluble methane monooxygenase (sMMO) consists of four
CC components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ),
CC B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD).
CC -!- MASS SPECTROMETRY: Mass=11942.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11709550};
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DR EMBL; M90050; AAF04159.1; -; Genomic_DNA.
DR EMBL; AE017282; AAU92723.1; -; Genomic_DNA.
DR PIR; JQ0700; JQ0700.
DR RefSeq; WP_010960486.1; NC_002977.6.
DR AlphaFoldDB; P22867; -.
DR SMR; P22867; -.
DR STRING; 243233.MCA1199; -.
DR EnsemblBacteria; AAU92723; AAU92723; MCA1199.
DR KEGG; mca:MCA1199; -.
DR eggNOG; ENOG50335AI; Bacteria.
DR HOGENOM; CLU_2260423_0_0_6; -.
DR OrthoDB; 2073252at2; -.
DR BioCyc; MetaCyc:MON-3866; -.
DR BRENDA; 1.14.13.25; 3305.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR InterPro; IPR017256; MmoD.
DR TIGRFAMs; TIGR04550; sMetMonox_MmoD; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..103
FT /note="Methane monooxygenase component D"
FT /id="PRO_0000096509"
SQ SEQUENCE 103 AA; 11942 MW; A91924768A568FB0 CRC64;
MVESAFQPFS GDADEWFEEP RPQAGFFPSA DWHLLKRDET YAAYAKDLDF MWRWVIVREE
RIVQEGCSIS LESSIRAVTH VLNYFGMTEQ RAPAEDRTGG VQH