ID   MAUG_METME              Reviewed;         335 AA.
AC   Q50233;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Methylamine utilization protein MauG;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=mauG;
OS   Methylophilus methylotrophus (Bacterium W3A1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=17;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8021188; DOI=10.1128/jb.176.13.4073-4080.1994;
RA   Chistoserdov A.Y., McIntire W.S., Mathews F.S., Lidstrom M.E.;
RT   "Organization of the methylamine utilization (mau) genes in Methylophilus
RT   methylotrophus W3A1-NS.";
RL   J. Bacteriol. 176:4073-4080(1994).
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; L26407; AAB46952.1; -; Genomic_DNA.
DR   PIR; T10074; T10074.
DR   AlphaFoldDB; Q50233; -.
DR   SMR; Q50233; -.
DR   PeroxiBase; 5006; MmeMauG.
DR   UniPathway; UPA00895; -.
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   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   TIGRFAMs; TIGR03791; TTQ_mauG; 1.
DR   PROSITE; PS51007; CYTC; 2.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW   Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..335
FT                   /note="Methylamine utilization protein MauG"
FT                   /id="PRO_0000006602"
FT   BINDING         69
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         72
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         73
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         216
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         219
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         220
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         273
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   335 AA;  37265 MW;  F65684907C3DACB0 CRC64;
     MLFRHLVLII STLMVANTAW SANLPPREKF KRPDSIPAPL SNPLTLEKAT LGKTLFFDQR
     LSRSGGMACA TCHSPDQRWS DGRTLPLQAE SVSNARRTPT VLNSAWLSAL MWDGRATTLE
     EQAVLPITTA HEMNFDLASL VSRLQRIEGY RPLFTQAFGD DSISQQRITQ ALASFQRTLV
     SNIAPFDRWV AGDEQAISES AKRGFAVFND KNKANCVACH SSWRFTDDSF HDIGLPSKDL
     GRGAKVPSQV TLMQHAFKTP SLRDLSIDGP YMHDGSIRGL KTVIKHYKSE AIQRESLSKD
     MQKFELSNLE ESDLIAFIQS LDGGALKIQA PMMPE