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 09-APR-2025, entry version 155. 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; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; 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=2 oxidized [amicyanin] + methylamine + H2O = 2 reduced CC [amicyanin] + formaldehyde + NH4(+) + 2 H(+); 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; mea:Mex_1p2773; -. DR eggNOG; ENOG502ZHBX; Bacteria. DR HOGENOM; CLU_116271_0_0_5; -. DR OrthoDB; 7628766at2; -. DR BioCyc; MetaCyc:MONOMER-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:aliphatic 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; Methylamine/Aralkylamine dehydrogenase light chain; 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 NCBIfam; TIGR01409; TAT_signal_seq; 1. DR NCBIfam; TIGR02659; TTQ_MADH_Lt; 1. DR Pfam; PF02975; Me-amine-dh_L; 1. DR PIRSF; PIRSF000192; Amine_dh_beta; 1. DR SUPFAM; SSF57561; Methylamine dehydrogenase, L chain; 1. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Electron transport; KW Oxidoreductase; Periplasm; Reference proteome; 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 //