DHMH_METEA
ID DHMH_METEA Reviewed; 410 AA.
AC Q49124; C5ATK4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=MexAM1_META1p2770;
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021187; DOI=10.1128/jb.176.13.4052-4065.1994;
RA Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., Lidstrom M.E.;
RT "Genetic organization of the mau gene cluster in Methylobacterium
RT extorquens AM1: complete nucleotide sequence and generation and
RT characteristics of mau mutants.";
RL J. Bacteriol. 176:4052-4065(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB46933.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L26406; AAB46933.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001510; ACS40528.1; -; Genomic_DNA.
DR RefSeq; WP_012753043.1; NC_012808.1.
DR AlphaFoldDB; Q49124; -.
DR SMR; Q49124; -.
DR STRING; 272630.MexAM1_META1p2770; -.
DR EnsemblBacteria; ACS40528; ACS40528; MexAM1_META1p2770.
DR KEGG; mea:Mex_1p2770; -.
DR eggNOG; COG3391; Bacteria.
DR HOGENOM; CLU_059384_0_0_5; -.
DR OMA; WAPGGWQ; -.
DR OrthoDB; 302683at2; -.
DR BioCyc; MetaCyc:MON-3905; -.
DR Proteomes; UP000009081; 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; Signal; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..410
FT /note="Methylamine dehydrogenase heavy chain"
FT /id="PRO_0000025577"
SQ SEQUENCE 410 AA; 44504 MW; C4597F914DA93652 CRC64;
MTHAYTKVRQ ALCYGSATLG AAALAALIAA GSAAAAESHG VATAKAAAAD LAAGKADDPV
VLKAAPINAR RVFVYDPKHF AAISQFYMID GDTARVVGTA DGGFLSNPVV ASDGSFFGQA
STVYERIARG KRTDYVELLD PQTNNPIADI ELPNSPRFLV GTYPWMTALT PNNKTLLFYQ
FSPQPAVGVV DLAGKKFDRM IEVPDCYHIF PSSNDTFFMH CRDGSLLKVG IGADGKSQTK
RTEIFHKENE YLINHPAYSP KSGRLVWPTY TGKIFQIDLS SQDAKFLPAI EAFTDAEKKE
GWAPGGWQQV AYHRESDRIF LLGDQRAASK HKAPSRFLFV IDAKTGKRIN KIELKHEIDS
VGVSQDAKPQ LYALSTGDKA LYIFDPETGK EVSSVNQLGA GPQVVMTSDM