ID   DHML_METFK              Reviewed;         186 AA.
AC   Q50425; Q1H3W6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 115.
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=Mfla_0551;
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7635847; DOI=10.1128/jb.177.15.4575-4578.1995;
RA   Gak E.R., Chistoserdov A.Y., Lidstrom M.E.;
RT   "Cloning, sequencing, and mutation of a gene for azurin in Methylobacillus
RT   flagellatum KT.";
RL   J. Bacteriol. 177:4575-4578(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; L37427; AAC41474.1; -; Genomic_DNA.
DR   EMBL; CP000284; ABE48821.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50425; -.
DR   SMR; Q50425; -.
DR   STRING; 265072.Mfla_0551; -.
DR   EnsemblBacteria; ABE48821; ABE48821; Mfla_0551.
DR   KEGG; mfa:Mfla_0551; -.
DR   eggNOG; ENOG502ZHBX; Bacteria.
DR   HOGENOM; CLU_116271_0_0_4; -.
DR   OMA; CDYWRHC; -.
DR   UniPathway; UPA00895; UER00870.
DR   Proteomes; UP000002440; 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   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;
KW   Reference proteome; Signal; Transport; TTQ.
FT   SIGNAL          1..57
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..186
FT                   /note="Methylamine dehydrogenase light chain"
FT                   /id="PRO_0000025573"
FT   MOD_RES         112
FT                   /note="Tryptophylquinone"
FT                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
SQ   SEQUENCE   186 AA;  20174 MW;  E94721FDA794B523 CRC64;
     MKKNTGFDSG IEKLARKTAS KTGRRSFIGK LGGFLVGSAL LPLLPVDRRG RMNEAHAETK
     GVLGREGYKP QDKDPKSCDY WRHCSIDGNL CDCCGGSLTS CPPGTELSPS SWVASCFNPG
     DGQTYLIAYR DCCGKQTCGR CNCVNVQGEL PVYRPEFNND IVWCFGADND AMTYHCTVSP
     IVGKAS