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Q51658 (MAUG_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylamine utilization protein MauG

EC=1.-.-.-
Gene names
Name:mauG
Ordered Locus Names:Pden_4736
Encoded onPlasmid pPD1222
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length387 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.

Pathway

One-carbon metabolism; methylamine degradation.

Subcellular location

Periplasm.

Post-translational modification

Binds 2 heme groups per subunit Potential.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Plasmid
Gene Ontology (GO)
   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 387367Methylamine utilization protein MauG
PRO_0000006603

Sites

Metal binding551Iron (heme 1 axial ligand) By similarity
Metal binding2251Iron (heme 2 axial ligand) By similarity
Metal binding3001Iron (heme 1 axial ligand) By similarity
Binding site511Heme 1 (covalent) By similarity
Binding site541Heme 1 (covalent) By similarity
Binding site2211Heme 2 (covalent) By similarity
Binding site2241Heme 2 (covalent) By similarity

Secondary structure

................................................................... 387
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q51658 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DDC9618235D6838E

FASTA38742,230
        10         20         30         40         50         60 
MLRLACLAPL AILIPAAGTA EQARPADDAL AALGAQLFVD PALSRNATQS CATCHDPARA 

        70         80         90        100        110        120 
FTDPREGKAG LAVSVGDDGQ SHGDRNTPTL GYAALVPAFH RDANGKYKGG QFWDGRADDL 

       130        140        150        160        170        180 
KQQAGQPMLN PVEMAMPDRA AVAARLRDDP AYRTGFEALF GKGVLDDPER AFDAAAEALA 

       190        200        210        220        230        240 
AYQATGEFSP FDSKYDRVMR GEEKFTPLEE FGYTVFITWN CRLCHMQRKQ GVAERETFTN 

       250        260        270        280        290        300 
FEYHNIGLPV NETAREASGL GADHVDHGLL ARPGIEDPAQ SGRFKVPSLR NVAVTGPYMH 

       310        320        330        340        350        360 
NGVFTDLRTA ILFYNKYTSR RPEAKINPET GAPWGEPEVA RNLSLAELQS GLMLDDGRVD 

       370        380 
ALVAFLETLT DRRYEPLLEE SRAAQKD 

« Hide

References

« Hide 'large scale' references
[1]"Mutational analysis of mau genes involved in methylamine metabolism in Paracoccus denitrificans."
van der Palen C.J., Slotboom D.J., Jongejan L., Reijnders W.N., Harms N., Duine J.A., van Spanning R.J.
Eur. J. Biochem. 230:860-871(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15028 Genomic DNA. Translation: AAA86467.1.
CP000491 Genomic DNA. Translation: ABL72797.1.
PIRS65959.
RefSeqYP_918493.1. NC_008688.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4MX-ray2.02A/B21-387[»]
3L4OX-ray2.05A/B21-387[»]
3ORVX-ray1.91A/B21-387[»]
3PXSX-ray2.22A/B21-387[»]
3PXTX-ray2.16A/B21-387[»]
3PXWX-ray2.11A/B21-387[»]
3RLMX-ray2.13A/B21-387[»]
3RMZX-ray1.72A/B21-387[»]
3RN0X-ray1.91A/B21-387[»]
3RN1X-ray1.93A/B21-387[»]
3SJLX-ray1.63A/B21-387[»]
3SLEX-ray2.52A/B21-387[»]
3SVWX-ray1.86A/B21-387[»]
3SWSX-ray1.86A/B21-387[»]
3SXTX-ray1.81A/B21-387[»]
4FA1X-ray2.18A/B21-387[»]
4FA4X-ray2.14A/B21-387[»]
4FA5X-ray1.94A/B21-387[»]
4FA9X-ray2.09A/B21-387[»]
4FANX-ray2.08A/B21-387[»]
4FAVX-ray2.08A/B21-387[»]
4FB1X-ray2.15A/B21-387[»]
4K3IX-ray2.00A/B21-387[»]
4L1QX-ray1.92A/B21-387[»]
4L3GX-ray2.05A/B21-387[»]
4L3HX-ray1.79A/B21-387[»]
4O1QX-ray2.59A/B21-387[»]
ProteinModelPortalQ51658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ51658. 1 interaction.
STRING318586.Pden_4736.

Protein family/group databases

PeroxiBase3540. PdeMauG.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL72797; ABL72797; Pden_4736.
GeneID4583239.
KEGGpde:Pden_4736.
PATRIC22860697. VBIParDen97112_4700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1858.
HOGENOMHOG000173944.
OMALTDRRYE.
OrthoDBEOG6FV81D.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-4779-MONOMER.
UniPathwayUPA00895.

Family and domain databases

Gene3D1.10.760.10. 3 hits.
InterProIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
[Graphical view]
PfamPF03150. CCP_MauG. 1 hit.
[Graphical view]
SUPFAMSSF46626. SSF46626. 3 hits.
PROSITEPS51007. CYTC. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ51658.

Entry information

Entry nameMAUG_PARDP
AccessionPrimary (citable) accession number: Q51658
Secondary accession number(s): A1BBA3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways