Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methylamine utilization protein MauG

Gene

mauG

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511Heme 1 (covalent)PROSITE-ProRule annotation
Binding sitei54 – 541Heme 1 (covalent)PROSITE-ProRule annotation
Metal bindingi55 – 551Iron (heme 1 axial ligand)PROSITE-ProRule annotation
Binding sitei221 – 2211Heme 2 (covalent)PROSITE-ProRule annotation
Binding sitei224 – 2241Heme 2 (covalent)PROSITE-ProRule annotation
Metal bindingi225 – 2251Iron (heme 2 axial ligand)PROSITE-ProRule annotation
Metal bindingi300 – 3001Iron (heme 1 axial ligand)PROSITE-ProRule annotation

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciPDEN318586:GCVQ-4779-MONOMER.
BRENDAi1.4.9.1. 3341.
UniPathwayiUPA00895.

Protein family/group databases

PeroxiBasei3540. PdeMauG.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylamine utilization protein MauG (EC:1.-.-.-)
Gene namesi
Name:mauG
Ordered Locus Names:Pden_4736
Encoded oniPlasmid pPD12220 Publication
OrganismiParacoccus denitrificans (strain Pd 1222)
Taxonomic identifieri318586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
ProteomesiUP000000361 Componenti: Plasmid pPD1222

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 387367Methylamine utilization protein MauGPRO_0000006603Add
BLAST

Post-translational modificationi

Binds 2 heme groups per subunit.Curated

Interactioni

Protein-protein interaction databases

IntActiQ51658. 1 interaction.
STRINGi318586.Pden_4736.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 3813Combined sources
Helixi41 – 433Combined sources
Helixi51 – 544Combined sources
Helixi57 – 593Combined sources
Helixi93 – 953Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi117 – 1193Combined sources
Helixi120 – 12910Combined sources
Turni131 – 1344Combined sources
Helixi139 – 14810Combined sources
Helixi150 – 16011Combined sources
Helixi164 – 1663Combined sources
Helixi168 – 18316Combined sources
Helixi186 – 1883Combined sources
Helixi194 – 1996Combined sources
Helixi207 – 21812Combined sources
Helixi220 – 2234Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi229 – 2313Combined sources
Beta strandi242 – 2454Combined sources
Helixi252 – 2587Combined sources
Helixi268 – 2714Combined sources
Helixi278 – 2803Combined sources
Helixi292 – 2943Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi304 – 3063Combined sources
Helixi307 – 3137Combined sources
Helixi314 – 3174Combined sources
Helixi322 – 3254Combined sources
Turni328 – 3303Combined sources
Beta strandi331 – 3333Combined sources
Beta strandi341 – 3433Combined sources
Helixi345 – 3484Combined sources
Helixi356 – 36712Combined sources
Helixi372 – 3787Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ51658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51658.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1858.
HOGENOMiHOG000173944.
OMAiNEISCAS.
OrthoDBiEOG6FV81D.

Family and domain databases

Gene3Di1.10.760.10. 3 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 3 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q51658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLACLAPL AILIPAAGTA EQARPADDAL AALGAQLFVD PALSRNATQS
60 70 80 90 100
CATCHDPARA FTDPREGKAG LAVSVGDDGQ SHGDRNTPTL GYAALVPAFH
110 120 130 140 150
RDANGKYKGG QFWDGRADDL KQQAGQPMLN PVEMAMPDRA AVAARLRDDP
160 170 180 190 200
AYRTGFEALF GKGVLDDPER AFDAAAEALA AYQATGEFSP FDSKYDRVMR
210 220 230 240 250
GEEKFTPLEE FGYTVFITWN CRLCHMQRKQ GVAERETFTN FEYHNIGLPV
260 270 280 290 300
NETAREASGL GADHVDHGLL ARPGIEDPAQ SGRFKVPSLR NVAVTGPYMH
310 320 330 340 350
NGVFTDLRTA ILFYNKYTSR RPEAKINPET GAPWGEPEVA RNLSLAELQS
360 370 380
GLMLDDGRVD ALVAFLETLT DRRYEPLLEE SRAAQKD
Length:387
Mass (Da):42,230
Last modified:November 1, 1996 - v1
Checksum:iDDC9618235D6838E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15028 Genomic DNA. Translation: AAA86467.1.
CP000491 Genomic DNA. Translation: ABL72797.1.
PIRiS65959.
RefSeqiWP_011750956.1. NC_008688.1.
YP_918493.1. NC_008688.1.

Genome annotation databases

EnsemblBacteriaiABL72797; ABL72797; Pden_4736.
KEGGipde:Pden_4736.
PATRICi22860697. VBIParDen97112_4700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15028 Genomic DNA. Translation: AAA86467.1.
CP000491 Genomic DNA. Translation: ABL72797.1.
PIRiS65959.
RefSeqiWP_011750956.1. NC_008688.1.
YP_918493.1. NC_008688.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ51658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ51658. 1 interaction.
STRINGi318586.Pden_4736.

Protein family/group databases

PeroxiBasei3540. PdeMauG.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL72797; ABL72797; Pden_4736.
KEGGipde:Pden_4736.
PATRICi22860697. VBIParDen97112_4700.

Phylogenomic databases

eggNOGiCOG1858.
HOGENOMiHOG000173944.
OMAiNEISCAS.
OrthoDBiEOG6FV81D.

Enzyme and pathway databases

UniPathwayiUPA00895.
BioCyciPDEN318586:GCVQ-4779-MONOMER.
BRENDAi1.4.9.1. 3341.

Miscellaneous databases

EvolutionaryTraceiQ51658.

Family and domain databases

Gene3Di1.10.760.10. 3 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 3 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pd 1222.

Entry informationi

Entry nameiMAUG_PARDP
AccessioniPrimary (citable) accession number: Q51658
Secondary accession number(s): A1BBA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.