MAUG_PARDP
ID MAUG_PARDP Reviewed; 387 AA.
AC Q51658; A1BBA3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Methylamine utilization protein MauG;
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=mauG; OrderedLocusNames=Pden_4736;
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7601147; DOI=10.1111/j.1432-1033.1995.tb20629.x;
RA van der Palen C.J., Slotboom D.J., Jongejan L., Reijnders W.N., Harms N.,
RA Duine J.A., van Spanning R.J.;
RT "Mutational analysis of mau genes involved in methylamine metabolism in
RT Paracoccus denitrificans.";
RL Eur. J. Biochem. 230:860-871(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; U15028; AAA86467.1; -; Genomic_DNA.
DR EMBL; CP000491; ABL72797.1; -; Genomic_DNA.
DR PIR; S65959; S65959.
DR RefSeq; WP_011750956.1; NC_008688.1.
DR PDB; 3L4M; X-ray; 2.02 A; A/B=21-387.
DR PDB; 3L4O; X-ray; 2.05 A; A/B=21-387.
DR PDB; 3ORV; X-ray; 1.91 A; A/B=21-387.
DR PDB; 3PXS; X-ray; 2.22 A; A/B=21-387.
DR PDB; 3PXT; X-ray; 2.16 A; A/B=21-387.
DR PDB; 3PXW; X-ray; 2.11 A; A/B=21-387.
DR PDB; 3RLM; X-ray; 2.13 A; A/B=21-387.
DR PDB; 3RMZ; X-ray; 1.72 A; A/B=21-387.
DR PDB; 3RN0; X-ray; 1.91 A; A/B=21-387.
DR PDB; 3RN1; X-ray; 1.93 A; A/B=21-387.
DR PDB; 3SJL; X-ray; 1.63 A; A/B=21-387.
DR PDB; 3SLE; X-ray; 2.52 A; A/B=21-387.
DR PDB; 3SVW; X-ray; 1.86 A; A/B=21-387.
DR PDB; 3SWS; X-ray; 1.86 A; A/B=21-387.
DR PDB; 3SXT; X-ray; 1.81 A; A/B=21-387.
DR PDB; 4FA1; X-ray; 2.18 A; A/B=21-387.
DR PDB; 4FA4; X-ray; 2.14 A; A/B=21-387.
DR PDB; 4FA5; X-ray; 1.94 A; A/B=21-387.
DR PDB; 4FA9; X-ray; 2.09 A; A/B=21-387.
DR PDB; 4FAN; X-ray; 2.08 A; A/B=21-387.
DR PDB; 4FAV; X-ray; 2.08 A; A/B=21-387.
DR PDB; 4FB1; X-ray; 2.15 A; A/B=21-387.
DR PDB; 4K3I; X-ray; 2.00 A; A/B=21-387.
DR PDB; 4L1Q; X-ray; 1.92 A; A/B=21-387.
DR PDB; 4L3G; X-ray; 2.05 A; A/B=21-387.
DR PDB; 4L3H; X-ray; 1.79 A; A/B=21-387.
DR PDB; 4O1Q; X-ray; 2.59 A; A/B=21-387.
DR PDB; 4Y5R; X-ray; 2.80 A; A/B=26-380.
DR PDBsum; 3L4M; -.
DR PDBsum; 3L4O; -.
DR PDBsum; 3ORV; -.
DR PDBsum; 3PXS; -.
DR PDBsum; 3PXT; -.
DR PDBsum; 3PXW; -.
DR PDBsum; 3RLM; -.
DR PDBsum; 3RMZ; -.
DR PDBsum; 3RN0; -.
DR PDBsum; 3RN1; -.
DR PDBsum; 3SJL; -.
DR PDBsum; 3SLE; -.
DR PDBsum; 3SVW; -.
DR PDBsum; 3SWS; -.
DR PDBsum; 3SXT; -.
DR PDBsum; 4FA1; -.
DR PDBsum; 4FA4; -.
DR PDBsum; 4FA5; -.
DR PDBsum; 4FA9; -.
DR PDBsum; 4FAN; -.
DR PDBsum; 4FAV; -.
DR PDBsum; 4FB1; -.
DR PDBsum; 4K3I; -.
DR PDBsum; 4L1Q; -.
DR PDBsum; 4L3G; -.
DR PDBsum; 4L3H; -.
DR PDBsum; 4O1Q; -.
DR PDBsum; 4Y5R; -.
DR AlphaFoldDB; Q51658; -.
DR SMR; Q51658; -.
DR IntAct; Q51658; 1.
DR MINT; Q51658; -.
DR STRING; 318586.Pden_4736; -.
DR PeroxiBase; 3540; PdeMauG.
DR PRIDE; Q51658; -.
DR EnsemblBacteria; ABL72797; ABL72797; Pden_4736.
DR KEGG; pde:Pden_4736; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_0_1_5; -.
DR OMA; NTRDTNP; -.
DR BRENDA; 1.4.9.1; 3341.
DR UniPathway; UPA00895; -.
DR EvolutionaryTrace; Q51658; -.
DR Proteomes; UP000000361; Plasmid pPD1222.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Plasmid; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..387
FT /note="Methylamine utilization protein MauG"
FT /id="PRO_0000006603"
FT BINDING 51
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 54
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 55
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 221
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 224
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 225
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 300
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 HELIX 26..38
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3RMZ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:3SJL"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4L3H"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3SJL"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3SJL"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:3SJL"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:3SJL"
SQ SEQUENCE 387 AA; 42230 MW; DDC9618235D6838E CRC64;
MLRLACLAPL AILIPAAGTA EQARPADDAL AALGAQLFVD PALSRNATQS CATCHDPARA
FTDPREGKAG LAVSVGDDGQ SHGDRNTPTL GYAALVPAFH RDANGKYKGG QFWDGRADDL
KQQAGQPMLN PVEMAMPDRA AVAARLRDDP AYRTGFEALF GKGVLDDPER AFDAAAEALA
AYQATGEFSP FDSKYDRVMR GEEKFTPLEE FGYTVFITWN CRLCHMQRKQ GVAERETFTN
FEYHNIGLPV NETAREASGL GADHVDHGLL ARPGIEDPAQ SGRFKVPSLR NVAVTGPYMH
NGVFTDLRTA ILFYNKYTSR RPEAKINPET GAPWGEPEVA RNLSLAELQS GLMLDDGRVD
ALVAFLETLT DRRYEPLLEE SRAAQKD
