DHML_PARDE
ID DHML_PARDE Reviewed; 188 AA.
AC P22619;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 131.
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;
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 158-188.
RC STRAIN=ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785;
RX PubMed=2261991; DOI=10.1016/0014-5793(90)81475-4;
RA van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F.,
RA Stouthamer A.H.;
RT "Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and
RT the resultant effect on methylamine oxidation.";
RL FEBS Lett. 275:217-220(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 64-188.
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) OF 64-188 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 -!- 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 {ECO:0000269|PubMed:1599920}.
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; M90098; AAA25578.1; -; Genomic_DNA.
DR EMBL; X55665; CAA39198.1; -; Genomic_DNA.
DR PIR; JH0661; JH0661.
DR RefSeq; WP_011750953.1; NZ_PPGA01000007.1.
DR PDB; 1MG2; X-ray; 2.25 A; B/F/J/N=58-188.
DR PDB; 1MG3; X-ray; 2.40 A; B/F/J/N=58-188.
DR PDB; 2BBK; X-ray; 1.75 A; L/M=64-188.
DR PDB; 2GC4; X-ray; 1.90 A; B/F/J/N=58-188.
DR PDB; 2GC7; X-ray; 1.90 A; B/F/J/N=58-188.
DR PDB; 2J55; X-ray; 2.15 A; L/M=58-188.
DR PDB; 2J56; X-ray; 2.10 A; L/M=58-188.
DR PDB; 2J57; X-ray; 2.25 A; K/L/M/N=58-188.
DR PDB; 2MTA; X-ray; 2.40 A; L=64-188.
DR PDB; 3ORV; X-ray; 1.91 A; C/E=58-188.
DR PDB; 3PXS; X-ray; 2.22 A; C/E=58-188.
DR PDB; 3PXT; X-ray; 2.16 A; C/E=58-188.
DR PDB; 3PXW; X-ray; 2.11 A; C/E=58-188.
DR PDB; 3RLM; X-ray; 2.13 A; C/E=58-188.
DR PDB; 3RMZ; X-ray; 1.72 A; C/E=58-188.
DR PDB; 3RN0; X-ray; 1.91 A; C/E=58-188.
DR PDB; 3SLE; X-ray; 2.52 A; C/E=58-188.
DR PDB; 4FA1; X-ray; 2.18 A; C/E=58-188.
DR PDB; 4FA4; X-ray; 2.14 A; C/E=58-188.
DR PDB; 4FA5; X-ray; 1.94 A; C/E=58-188.
DR PDB; 4FA9; X-ray; 2.09 A; C/E=58-188.
DR PDB; 4FAN; X-ray; 2.08 A; C/E=58-188.
DR PDB; 4FAV; X-ray; 2.08 A; C/E=58-188.
DR PDB; 4FB1; X-ray; 2.15 A; C/E=58-188.
DR PDB; 4K3I; X-ray; 2.00 A; C/E=58-188.
DR PDB; 4Y5R; X-ray; 2.80 A; C/E=64-188.
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 PDBsum; 3ORV; -.
DR PDBsum; 3PXS; -.
DR PDBsum; 3PXT; -.
DR PDBsum; 3PXW; -.
DR PDBsum; 3RLM; -.
DR PDBsum; 3RMZ; -.
DR PDBsum; 3RN0; -.
DR PDBsum; 3SLE; -.
DR PDBsum; 4FA1; -.
DR PDBsum; 4FA4; -.
DR PDBsum; 4FA5; -.
DR PDBsum; 4FA9; -.
DR PDBsum; 4FAN; -.
DR PDBsum; 4FAV; -.
DR PDBsum; 4FB1; -.
DR PDBsum; 4K3I; -.
DR PDBsum; 4Y5R; -.
DR AlphaFoldDB; P22619; -.
DR SMR; P22619; -.
DR DIP; DIP-6254N; -.
DR IntAct; P22619; 1.
DR DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL.
DR OMA; CDYWRHC; -.
DR BioCyc; MetaCyc:MON-3910; -.
DR BRENDA; 1.4.9.1; 3341.
DR SABIO-RK; P22619; -.
DR UniPathway; UPA00895; UER00870.
DR EvolutionaryTrace; P22619; -.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Oxidoreductase;
KW Periplasm; Signal; Transport; TTQ.
FT SIGNAL 1..57
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 58..188
FT /note="Methylamine dehydrogenase light chain"
FT /id="PRO_0000025575"
FT MOD_RES 114
FT /note="Tryptophylquinone"
FT /evidence="ECO:0000269|PubMed:1409575"
FT DISULFID 80..145
FT DISULFID 86..118
FT DISULFID 93..178
FT DISULFID 95..143
FT DISULFID 103..134
FT DISULFID 135..166
FT CROSSLNK 114..165
FT /note="Tryptophan tryptophylquinone (Trp-Trp)"
FT /evidence="ECO:0000269|PubMed:1409575"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1MG3"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3RMZ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3RMZ"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2BBK"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:3RMZ"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 125..137
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3RMZ"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2BBK"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3RMZ"
SQ SEQUENCE 188 AA; 20393 MW; E3D9DE4454268BE8 CRC64;
MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG RVSRANAADA
PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL TNCPPGTKLA TASWVASCYN
PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI
SPIVGKAS
