MAUG_METFK
ID MAUG_METFK Reviewed; 333 AA.
AC Q50426; Q1H3W5; Q50421; Q9RAN2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Methylamine utilization protein MauG;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=mauG; OrderedLocusNames=Mfla_0552;
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].
RA Zhang X., Chistoserdov A.Y., McIntire W.S.;
RT "Correct sequence for Methylobacillus flagellatum KT MauG gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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 1-245 AND 275-333.
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: 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; AF114265; AAF03761.1; -; Genomic_DNA.
DR EMBL; CP000284; ABE48822.1; -; Genomic_DNA.
DR EMBL; L37427; AAC41475.1; -; Genomic_DNA.
DR EMBL; L37429; AAC41470.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50426; -.
DR SMR; Q50426; -.
DR STRING; 265072.Mfla_0552; -.
DR PeroxiBase; 5011; MflaMauG.
DR EnsemblBacteria; ABE48822; ABE48822; Mfla_0552.
DR KEGG; mfa:Mfla_0552; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_3_2_4; -.
DR OMA; YKFANVG; -.
DR UniPathway; UPA00895; -.
DR Proteomes; UP000002440; 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 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 Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..333
FT /note="Methylamine utilization protein MauG"
FT /id="PRO_0000006601"
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 214
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 217
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 218
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 271
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 CONFLICT 174
FT /note="S -> R (in Ref. 1; AAF03761 and 3; AAC41475)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> N (in Ref. 3; AAC41475)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> F (in Ref. 3; AAC41475)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..243
FT /note="GAR -> CAG (in Ref. 3; AAC41475)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="I -> V (in Ref. 1; AAF03761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37172 MW; 15733B1F6AE61167 CRC64;
MRFCSVFLVF GLAAAMGVSH AADLPPRESY QRPADIPSPP DNPLTIEKAA LGKTLFFDPR
LSRDGSMSCA TCHNPGMRWS DGRILPLRAD GVEHARRTPT VLNSAWLTTL MWDGRATSLE
DQAILPITTA HEMNFEMPLL LNRLKDVAGY APLFARAFGD AEITEKRLTQ ALASFQRTLV
SKLAPFDVWV EGDESAMSER AKRGFAVFKG KARCATCHSS WRFTDDSFHD IGLPSLDPGR
GARVPPQVTI MQHAFKTPTL RDLPRNGPFM HDGSMHSLDE VIRHYEQGGL QRPSISAEMK
RFELTETERE YLIEFIHTLD GGLLDIEPPQ LPE
