DHMH_METFK
ID DHMH_METFK Reviewed; 400 AA.
AC Q50420; Q1H3W9; Q50413;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 25-MAY-2022, entry version 107.
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; OrderedLocusNames=Mfla_0548;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9202457; DOI=10.1099/00221287-143-6-1827;
RA Gak E.R., Tsygankov Y.D., Chistoserdov A.Y.;
RT "Organization of methylamine utilization genes (mau) in 'Methylobacillus
RT flagellatum ' KT and analysis of mau mutants.";
RL Microbiology 143:1827-1835(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68 AND 332-400.
RX PubMed=7635847; DOI=10.1128/jb.177.15.4575-4578.1995;
RA Gak E.R., Chistoserdov A.Y., Lidstrom M.E.;
RT "Cloning, sequencing, and mutation of a gene for azurin in Methylobacillus
RT flagellatum KT.";
RL J. Bacteriol. 177:4575-4578(1995).
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}.
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DR EMBL; AF188997; AAC41469.2; -; Genomic_DNA.
DR EMBL; CP000284; ABE48818.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50420; -.
DR SMR; Q50420; -.
DR STRING; 265072.Mfla_0548; -.
DR EnsemblBacteria; ABE48818; ABE48818; Mfla_0548.
DR KEGG; mfa:Mfla_0548; -.
DR eggNOG; COG3391; Bacteria.
DR HOGENOM; CLU_059384_0_0_4; -.
DR OMA; WAPGGWQ; -.
DR Proteomes; UP000002440; Chromosome.
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 3: Inferred from homology;
KW Electron transport; Oxidoreductase; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..400
FT /note="Methylamine dehydrogenase heavy chain"
FT /id="PRO_0000025578"
SQ SEQUENCE 400 AA; 44330 MW; 6ACCF91ADF6979B6 CRC64;
MTTFQPGRLA GQLAATALLA ATCSAFAADA PTTVPSSLGA IGTTPTLDNI TMEPGLPSDA
KRVYVLDPGH FHVTTTVYTI DGNKNNLLGM TDTGKLANVM LSSDGKFFVT SNTTYSRIAR
GKRDDYVEVI DAQSHKVLAD IDIPEGRFLT GVMNRMASLS TDNKYMLFQQ FAPSPAVGLV
DLEKKSFVKM MDIPDCYQIF PVPNQSFYMH CRDGSLQQFG YDDKGNLKPM KPTKVFHGED
DYLFVNPYYS NGSGRLVWPT YEGRIFQAKL TDKKVDFMKP FELFTEAEKK ANWRPGGWQV
VAYHKARNEI YVLADQRAKW THVTASRYVF VVDGTTGKRL RRIDLGHEID GISVTQDANP
NLYAVSAEAK TLFTFNAVTG KETGKVDELG RAPTISLTMD