DHMH_PARDE
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 03-AUG-2022, entry version 114.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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}.
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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:MON-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; -; 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 Pfam; PF06433; Me-amine-dh_H; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR TIGRFAMs; TIGR02658; TTQ_MADH_Hv; 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
