DHML_METEA
ID DHML_METEA Reviewed; 186 AA.
AC P00372; C5ATK7; Q60146;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Methylamine dehydrogenase light chain;
DE Short=MADH;
DE EC=1.4.9.1;
DE AltName: Full=Methylamine dehydrogenase (amicyanin);
DE Flags: Precursor;
GN Name=mauA; OrderedLocusNames=MexAM1_META1p2773;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1653226; DOI=10.1128/jb.173.18.5901-5908.1991;
RA Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E.;
RT "Genetic organization of methylamine utilization genes from
RT Methylobacterium extorquens AM1.";
RL J. Bacteriol. 173:5901-5908(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021187; DOI=10.1128/jb.176.13.4052-4065.1994;
RA Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E.;
RT "Genetic organization of the mau gene cluster in Methylobacterium
RT extorquens AM1: complete nucleotide sequence and generation and
RT characteristics of mau mutants.";
RL J. Bacteriol. 176:4052-4065(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-186.
RX PubMed=2121141; DOI=10.1016/s0006-291x(05)80195-0;
RA Chistoserdov A.Y., Tsygankov Y.D., Lidstrom M.E.;
RT "Cloning and sequencing of the structural gene for the small subunit of
RT methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence
RT for two tryptophan residues involved in the active center.";
RL Biochem. Biophys. Res. Commun. 172:211-216(1990).
RN [5]
RP PROTEIN SEQUENCE OF 58-186.
RX PubMed=6841324; DOI=10.1093/oxfordjournals.jbchem.a134144;
RA Ishii Y., Hase T., Fukumori Y., Matsubara H., Tobari J.;
RT "Amino acid sequence studies of the light subunit of methylamine
RT dehydrogenase from Pseudomonas AM1: existence of two residues binding the
RT prosthetic group.";
RL J. Biochem. 93:107-119(1983).
RN [6]
RP PRESENCE OF UNUSUAL LEADER SEQUENCE.
RX PubMed=1885555; DOI=10.1128/jb.173.18.5909-5913.1991;
RA Chistoserdov A.Y., Lidstrom M.E.;
RT "The small-subunit polypeptide of methylamine dehydrogenase from
RT Methylobacterium extorquens AM1 has an unusual leader sequence.";
RL J. Bacteriol. 173:5909-5913(1991).
RN [7]
RP CHARACTERIZATION OF COFACTOR.
RX PubMed=2028257; DOI=10.1126/science.2028257;
RA McIntire W.S., Wemmer D.E., Chistoserdov A.Y., Lidstrom M.E.;
RT "A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as
RT the redox prosthetic group in methylamine dehydrogenase.";
RL Science 252:817-824(1991).
CC -!- FUNCTION: Methylamine dehydrogenase carries out the oxidation of
CC methylamine. Electrons are passed from methylamine dehydrogenase to
CC amicyanin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + methylamine + 2 oxidized [amicyanin] = formaldehyde + 2
CC H(+) + NH4(+) + 2 reduced [amicyanin]; Xref=Rhea:RHEA:30207,
CC Rhea:RHEA-COMP:11100, Rhea:RHEA-COMP:11101, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:49552, ChEBI:CHEBI:59338; EC=1.4.9.1;
CC -!- COFACTOR:
CC Name=tryptophan tryptophylquinone residue; Xref=ChEBI:CHEBI:20251;
CC Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
CC cofactor.;
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation; formaldehyde
CC from methylamine: step 1/1.
CC -!- SUBUNIT: Heterotetramer of two light and two heavy chains.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- PTM: Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the
CC indole ring of a tryptophan to form tryptophylquinone followed by
CC covalent cross-linking with another tryptophan residue.
CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase light chain
CC family. {ECO:0000305}.
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DR EMBL; M57963; AAA68894.1; -; Genomic_DNA.
DR EMBL; L26406; AAB46936.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS40531.1; -; Genomic_DNA.
DR EMBL; M58517; AAA25379.1; -; Genomic_DNA.
DR PIR; A36676; DEPSNL.
DR RefSeq; WP_012753046.1; NC_012808.1.
DR AlphaFoldDB; P00372; -.
DR SMR; P00372; -.
DR STRING; 272630.MexAM1_META1p2773; -.
DR EnsemblBacteria; ACS40531; ACS40531; MexAM1_META1p2773.
DR KEGG; mea:Mex_1p2773; -.
DR eggNOG; ENOG502ZHBX; Bacteria.
DR HOGENOM; CLU_116271_0_0_5; -.
DR OMA; CDYWRHC; -.
DR OrthoDB; 1619371at2; -.
DR BioCyc; MetaCyc:MON-3906; -.
DR UniPathway; UPA00895; UER00870.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
DR GO; GO:0052876; F:methylamine dehydrogenase (amicyanin) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.60.30.10; -; 1.
DR InterPro; IPR016008; Amine_DH_Ltc.
DR InterPro; IPR036560; MADH/AADH_L_sf.
DR InterPro; IPR013504; MADH/AADH_Ltc_C_dom.
DR InterPro; IPR004229; MeN_DH_Ltc.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF02975; Me-amine-dh_L; 1.
DR PIRSF; PIRSF000192; Amine_dh_beta; 1.
DR SUPFAM; SSF57561; SSF57561; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR TIGRFAMs; TIGR02659; TTQ_MADH_Lt; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Oxidoreductase; Periplasm; Signal; Transport; TTQ.
FT SIGNAL 1..57
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:6841324"
FT CHAIN 58..186
FT /note="Methylamine dehydrogenase light chain"
FT /id="PRO_0000025572"
FT MOD_RES 112
FT /note="Tryptophylquinone"
FT DISULFID 78..143
FT /evidence="ECO:0000250"
FT DISULFID 84..116
FT /evidence="ECO:0000250"
FT DISULFID 91..176
FT /evidence="ECO:0000250"
FT DISULFID 93..141
FT /evidence="ECO:0000250"
FT DISULFID 101..132
FT /evidence="ECO:0000250"
FT DISULFID 133..164
FT /evidence="ECO:0000250"
FT CROSSLNK 112..163
FT /note="Tryptophan tryptophylquinone (Trp-Trp)"
FT VARIANT 106
FT /note="K -> L"
FT CONFLICT 74
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 186 AA; 20085 MW; 4F8504FEFF0331D9 CRC64;
MLGKSQFDDL FEKMSRKVAG HTSRRGFIGR VGTAVAGVAL VPLLPVDRRG RVSRANAAES
AGDPRGKWKP QDNDVQSCDY WRHCSIDGNI CDCSGGSLTS CPPGTKLASS SWVASCYNPT
DKQSYLISYR DCCGANVSGR CACLNTEGEL PVYRPEFGND IIWCFGAEDD AMTYHCTISP
IVGKAS
