ID DHMH_PARDE Reviewed; 417 AA. AC P29894; Q79D76; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 13-SEP-2023, entry version 118. 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; OS Paracoccus denitrificans. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Paracoccus. OX NCBI_TaxID=266; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1590782; DOI=10.1016/s0006-291x(05)80007-5; RA Chistoserdov A.Y., Boyd J., Mathews F.S., Lidstrom M.E.; RT "The genetic organization of the mau gene cluster of the facultative RT autotroph Paracoccus denitrificans."; RL Biochem. Biophys. Res. Commun. 184:1181-1189(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69. RC STRAIN=ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627; RX PubMed=7957249; DOI=10.1111/j.1432-1033.1994.tb20042.x; RA van Spanning R.J.M., van der Palen C.J., Slotboom D.J., Reijnders W.N., RA Stouthamer A.H., Duine J.A.; RT "Expression of the mau genes involved in methylamine metabolism in RT Paracoccus denitrificans is under control of a LysR-type transcriptional RT activator."; RL Eur. J. Biochem. 226:201-210(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=1409575; DOI=10.1002/prot.340140214; RA Chen L., Mathews F.S., Davidson V.L., Huizinga E.G., Vellieux F.M.D., RA Hol W.G.J.; RT "Three-dimensional structure of the quinoprotein methylamine dehydrogenase RT from Paracoccus denitrificans determined by molecular replacement at 2.8-A RT resolution."; RL Proteins 14:288-299(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMICYANIN. RX PubMed=1599920; DOI=10.1021/bi00136a006; RA Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., RA Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.; RT "Crystal structure of an electron-transfer complex between methylamine RT dehydrogenase and amicyanin."; RL Biochemistry 31:4959-4964(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=8140419; DOI=10.1126/science.8140419; RA Chen L., Durley R., Mathews F.S., Davidson V.L.; RT "Structure of an electron transfer complex: methylamine dehydrogenase, RT amicyanin, and cytochrome c551i."; RL Science 264:86-90(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 -!- SUBUNIT: Tetramer of two light and two heavy chains. CC {ECO:0000269|PubMed:1599920}. 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; M90099; AAA25580.1; -; Genomic_DNA. DR EMBL; U12464; AAA56724.1; -; Genomic_DNA. DR PIR; JH0660; JH0660. DR PDB; 1MG2; X-ray; 2.25 A; A/E/I/M=28-417. DR PDB; 1MG3; X-ray; 2.40 A; A/E/I/M=28-417. DR PDB; 2BBK; X-ray; 1.75 A; H/J=63-417. DR PDB; 2GC4; X-ray; 1.90 A; A/E/I/M=32-417. DR PDB; 2GC7; X-ray; 1.90 A; A/E/I/M=32-417. DR PDB; 2J55; X-ray; 2.15 A; H/J=32-417. DR PDB; 2J56; X-ray; 2.10 A; H/J=32-417. DR PDB; 2J57; X-ray; 2.25 A; G/H/I/J=32-417. DR PDB; 2MTA; X-ray; 2.40 A; H=45-417. DR PDBsum; 1MG2; -. DR PDBsum; 1MG3; -. DR PDBsum; 2BBK; -. DR PDBsum; 2GC4; -. DR PDBsum; 2GC7; -. DR PDBsum; 2J55; -. DR PDBsum; 2J56; -. DR PDBsum; 2J57; -. DR PDBsum; 2MTA; -. DR AlphaFoldDB; P29894; -. DR SMR; P29894; -. DR DIP; DIP-6253N; -. DR IntAct; P29894; 1. DR DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL. DR BioCyc; MetaCyc:MONOMER-3909; -. DR BRENDA; 1.4.9.1; 3341. DR SABIO-RK; P29894; -. DR EvolutionaryTrace; P29894; -. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. 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: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 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..28 FT /note="Or 26" FT /evidence="ECO:0000255" FT CHAIN 29..417 FT /note="Methylamine dehydrogenase heavy chain" FT /id="PRO_0000025580" FT DISULFID 212..227 FT HELIX 40..58 FT /evidence="ECO:0007829|PDB:2GC4" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:2BBK" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 88..96 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 101..108 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 113..116 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 123..132 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 135..145 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:2BBK" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 179..186 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 198..201 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 202..208 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 239..241 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 266..269 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 270..275 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 278..284 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:2BBK" FT HELIX 301..305 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 320..323 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 324..331 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 341..348 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 349..351 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 354..364 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 366..369 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 382..385 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 386..391 FT /evidence="ECO:0007829|PDB:2BBK" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 397..401 FT /evidence="ECO:0007829|PDB:2BBK" FT STRAND 410..412 FT /evidence="ECO:0007829|PDB:2BBK" SQ SEQUENCE 417 AA; 45440 MW; 8187A8B694208BE2 CRC64; MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA RAAAADLAAG QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG RVIGMIDGGF LPNPVVADDG SFIAHASTVF SRIARGERTD YVEVFDPVTL LPTADIELPD APRFLVGTYP WMTSLTPDGK TLLFYQFSPA PAVGVVDLEG KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE GTPEITHTEV FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS VNQLGHGPQV ITTADMG //