ID   DHML_METME              Reviewed;         187 AA.
AC   Q59543;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
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;
OS   Methylophilus methylotrophus (Bacterium W3A1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=17;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021188; DOI=10.1128/jb.176.13.4073-4080.1994;
RA   Chistoserdov A.Y., McIntire W.S., Mathews F.S., Lidstrom M.E.;
RT   "Organization of the methylamine utilization (mau) genes in Methylophilus
RT   methylotrophus W3A1-NS.";
RL   J. Bacteriol. 176:4073-4080(1994).
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         Evidence={ECO:0000250};
CC       Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
CC       cofactor. {ECO:0000250};
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 not 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; L26407; AAB46951.1; -; Genomic_DNA.
DR   PIR; T10073; T10073.
DR   AlphaFoldDB; Q59543; -.
DR   SMR; Q59543; -.
DR   STRING; 1122236.KB905144_gene2355; -.
DR   BioCyc; MetaCyc:MON-3908; -.
DR   UniPathway; UPA00895; UER00870.
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   Pfam; PF02975; Me-amine-dh_L; 1.
DR   PIRSF; PIRSF000192; Amine_dh_beta; 1.
DR   SUPFAM; SSF57561; SSF57561; 1.
DR   TIGRFAMs; TIGR02659; TTQ_MADH_Lt; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Oxidoreductase; Periplasm; Signal;
KW   Transport; TTQ.
FT   SIGNAL          1..57
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..187
FT                   /note="Methylamine dehydrogenase light chain"
FT                   /id="PRO_0000025574"
FT   MOD_RES         113
FT                   /note="Tryptophylquinone"
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..144
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        94..142
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..165
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        113..164
FT                   /note="Tryptophan tryptophylquinone (Trp-Trp)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20237 MW;  E33FEBAE30CC5CED CRC64;
     MKKDTGFDSK IEKLARTTAS KTGRRGFIGR LGGFLVGSAL LPLLPVDRRS RLGGEVQAAT
     TGNLTRSGFK PQDKDPKACE YWRHCTIDGN LCDCCGGTLT SCPPGSSLSP SSWVASCYNP
     GDQQTYLIAY RDCCGKQTCG RCNCVNTQGE LPVYRPEFNN DIVWCFGADN DAMTYHCTIS
     PIVGKAS