DHMH_PARVE
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 03-AUG-2022, entry version 113.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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 (2.25 ANGSTROMS).
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 (2.25 ANGSTROMS).
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=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 -!- 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_QUMX01000042.1.
DR PDB; 1MAE; X-ray; 2.80 A; H=59-400.
DR PDB; 1MAF; X-ray; 2.60 A; H=59-400.
DR PDB; 2MAD; X-ray; 2.25 A; H=59-400.
DR PDB; 3C75; X-ray; 2.50 A; H/J=1-426.
DR PDBsum; 1MAE; -.
DR PDBsum; 1MAF; -.
DR PDBsum; 2MAD; -.
DR PDBsum; 3C75; -.
DR AlphaFoldDB; P23006; -.
DR SMR; P23006; -.
DR STRING; 34007.IT40_03135; -.
DR eggNOG; COG3391; Bacteria.
DR OrthoDB; 302683at2; -.
DR BioCyc; MetaCyc:MON-3901; -.
DR EvolutionaryTrace; P23006; -.
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..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 DISULFID 221..236
FT HELIX 54..67
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..108
FT /evidence="ECO:0007829|PDB:3C75"
FT STRAND 111..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 TURN 328..331
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
