MAUG_METEA
ID MAUG_METEA Reviewed; 353 AA.
AC Q49128; C5ATL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Methylamine utilization protein MauG;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=mauG; OrderedLocusNames=MexAM1_META1p2776;
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: Involved in methylamine metabolism. Essential for the
CC maturation of the beta subunit of MADH, presumably via a step in the
CC biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of
CC MADH.
CC -!- PATHWAY: One-carbon metabolism; methylamine degradation.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000305}.
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DR EMBL; L26406; AAB46939.1; -; Genomic_DNA.
DR EMBL; CP001510; ACS40534.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49128; -.
DR SMR; Q49128; -.
DR STRING; 272630.MexAM1_META1p2776; -.
DR PeroxiBase; 5005; MexMauG.
DR EnsemblBacteria; ACS40534; ACS40534; MexAM1_META1p2776.
DR KEGG; mea:Mex_1p2776; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_3_1_5; -.
DR OMA; YKFANVG; -.
DR UniPathway; UPA00895; -.
DR Proteomes; UP000009081; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030416; P:methylamine metabolic process; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR InterPro; IPR022394; Methylamine_utilis_MauG.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR TIGRFAMs; TIGR03791; TTQ_mauG; 1.
DR PROSITE; PS51007; CYTC; 2.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..353
FT /note="Methylamine utilization protein MauG"
FT /id="PRO_0000006600"
FT BINDING 88
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 91
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 92
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 234
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 237
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 238
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 292
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 353 AA; 38146 MW; BC88E1E7A107DD67 CRC64;
MRAILPIPVL IAWAMVVCGG AYAVTTCSGA ATATADASQQ DLAALKARFR RPESVPHPKA
NPLTPEKVAL GKALFFDPRL SRSGSVSCAT CHNPSLGWSD GLTRAVGFGM VPLPRRTPPV
LNLAWGTAFQ WDGRADSLEA QARMPITAPD EMNMSMDLVV ERLKAVPGYA PLFRNAFGSE
EPIGARHVTA ALATFQRTLV SGEAPFDRWA LGDESAIGAD AKRGFALFTG KAGCAACHST
WRFTDDSFHD IGLKAGNDLG RGKFAPPSVT AMRYAFKTPS LRDLRMEGPY MHDGQLGSLE
AVLDHYIKGG EKRPSLSFEM KPFEMSERER RDLVAFLETL KAEPAAITLP QLP
