ID DHMH_PARVE Reviewed; 426 AA. AC P23006; Q60052; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 04-NOV-2026, entry version 124. DE RecName: Full=Methylamine dehydrogenase heavy chain; DE Short=MADH; DE EC=1.4.9.1; DE AltName: Full=Methylamine dehydrogenase (amicyanin); DE Flags: Precursor; GN Name=mauB; Synonyms=madA; OS Paracoccus versutus (Thiobacillus versutus). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Paracoccus. OX NCBI_TaxID=34007; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8407797; DOI=10.1128/jb.175.19.6254-6259.1993; RA Huitema F., van Beeumen J., van Driessche G., Duine J.A., Canters G.W.; RT "Cloning and sequencing of the gene coding for the large subunit of RT methylamine dehydrogenase from Thiobacillus versutus."; RL J. Bacteriol. 175:6254-6259(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=2792083; DOI=10.1002/j.1460-2075.1989.tb08339.x; RA Vellieux F.M.D., Huitema F., Groendijk H., Kalk K.H., Jzn J.F., RA Jongejan J.A., Duine J.A., Petratos K., Drenth J., Hol W.G.J.; RT "Structure of quinoprotein methylamine dehydrogenase at 2.25-A RT resolution."; RL EMBO J. 8:2171-2178(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=2085423; DOI=10.1107/s010876819000636x; RA Vellieux F.M.D., Kalk K.H., Hol W.G.J.; RT "Structure determination of quinoprotein methylamine dehydrogenase from RT Thiobacillus versutus."; RL Acta Crystallogr. B 46:806-823(1990). 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 -!- SUBUNIT: Tetramer of two light and two heavy chains. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy 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; L08575; AAA72335.1; -; Genomic_DNA. DR PIR; A36934; A36934. DR RefSeq; WP_036750437.1; NZ_CP035286.1. DR PDB; 1MAE; X-ray; 2.80 A; H=58-423. DR PDB; 1MAF; X-ray; 2.60 A; H=58-423. DR PDB; 2MAD; X-ray; 2.25 A; H=58-423. DR PDB; 3C75; X-ray; 2.50 A; H/J=1-426. DR AlphaFoldDB; P23006; -. DR SMR; P23006; -. DR eggNOG; COG3391; Bacteria. DR BioCyc; MetaCyc:MONOMER-3901; -. DR EvolutionaryTrace; P23006; -. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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:0030416; P:methylamine metabolic process; IEA:InterPro. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR013476; MeN_DH_Hvc. DR InterPro; IPR009451; Metamine_DH_Hvc. DR InterPro; IPR011044; Quino_amine_DH_bsu. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR NCBIfam; TIGR02658; TTQ_MADH_Hv; 1. DR PANTHER; PTHR47197:SF3; DIHYDRO-HEME D1 DEHYDROGENASE; 1. DR PANTHER; PTHR47197; PROTEIN NIRF; 1. DR Pfam; PF06433; Me-amine-dh_H; 1. DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Electron transport; Oxidoreductase; KW Periplasm; Signal; Transport. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT CHAIN 32..426 FT /note="Methylamine dehydrogenase heavy chain" FT /id="PRO_0000025581" FT REGION 32..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..64 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 221..236 FT HELIX 54..67 FT /evidence="ECO:0007829|PDB:3C75" FT HELIX 79..82 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 93..95 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 97..105 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 106..109 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 110..117 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 132..141 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 144..154 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 161..167 FT /evidence="ECO:0007829|PDB:3C75" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 188..195 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 207..210 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 211..217 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 220..228 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 231..236 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 239..245 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 274..276 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 286..293 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:3C75" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 320..322 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:3C75" FT HELIX 328..330 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 332..339 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 349..356 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 362..372 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 374..377 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 380..382 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 390..393 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 394..399 FT /evidence="ECO:0007829|PDB:3C75" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:3C75" FT STRAND 418..420 FT /evidence="ECO:0007829|PDB:3C75" SQ SEQUENCE 426 AA; 46388 MW; 4ECDF8F6A7AE8696 CRC64; MASARESTPR YLTLIGATLA CSALALGAAQ AQTEPAEPEA PAETAAADAA GQTEGQRGAA EAAAALAAGE ADEPVILEAP APDARRVYIQ DPAHFAAITQ QFVIDGSTGR ILGMTDGGFL PHPVAAEDGS FFAQASTVFE RIARGKRTDY VEVFDPVTFL PIADIELPDA PRFLVGTYQW MNALTPDNKN LLFYQFSPAP AVGVVDLEGK TFDRMLDVPD CYHIFPASPT VFYMNCRDGS LARVDFADGE TKVTNTEVFH TEDELLINHP AFSLRSGRLV WPTYTGKIFQ ADLTAEGATF RAPIEALTEA ERADDWRPGG WQQTAYHRQS DRIYLLVDQR DEWKHKAASR FVVVLNAETG ERINKIELGH EIDSINVSQD AEPLLYALSA GTQTLHIYDA ATGEELRSVD QLGRGPQIIT THDMDS //