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P22619

- DHML_PARDE

UniProt

P22619 - DHML_PARDE

Protein

Methylamine dehydrogenase light chain

Gene

mauA

Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.

    Catalytic activityi

    Methylamine + H2O + amicyanin = formaldehyde + ammonia + reduced amicyanin.

    Cofactori

    Contains 1 tryptophan tryptophylquinone per subunit.

    Pathwayi

    GO - Molecular functioni

    1. amine dehydrogenase activity Source: InterPro
    2. methylamine dehydrogenase (amicyanin) activity Source: UniProtKB-EC

    GO - Biological processi

    1. amine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3910.
    SABIO-RKP22619.
    UniPathwayiUPA00895; UER00870.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylamine dehydrogenase light chain (EC:1.4.9.1)
    Short name:
    MADH
    Alternative name(s):
    Methylamine dehydrogenase (amicyanin)
    Gene namesi
    Name:mauA
    OrganismiParacoccus denitrificans
    Taxonomic identifieri266 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

    Subcellular locationi

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5757Tat-type signalSequence AnalysisAdd
    BLAST
    Chaini58 – 188131Methylamine dehydrogenase light chainPRO_0000025575Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi80 ↔ 145
    Disulfide bondi86 ↔ 118
    Disulfide bondi93 ↔ 178
    Disulfide bondi95 ↔ 143
    Disulfide bondi103 ↔ 134
    Cross-linki114 ↔ 165Tryptophan tryptophylquinone (Trp-Trp)1 Publication
    Modified residuei114 – 1141Tryptophylquinone1 Publication
    Disulfide bondi135 ↔ 166

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
    Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.

    Keywords - PTMi

    Disulfide bond, TTQ

    Interactioni

    Subunit structurei

    Heterotetramer of two light and two heavy chains.1 Publication

    Protein-protein interaction databases

    DIPiDIP-6254N.
    IntActiP22619. 1 interaction.

    Structurei

    Secondary structure

    1
    188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi66 – 683
    Beta strandi73 – 753
    Helixi83 – 853
    Beta strandi89 – 924
    Helixi93 – 964
    Beta strandi100 – 1034
    Beta strandi114 – 1207
    Turni121 – 1244
    Beta strandi125 – 13713
    Beta strandi142 – 1465
    Helixi157 – 1593
    Beta strandi161 – 1633
    Helixi170 – 1723
    Beta strandi175 – 1806
    Beta strandi183 – 1853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MG2X-ray2.25B/F/J/N58-188[»]
    1MG3X-ray2.40B/F/J/N58-188[»]
    2BBKX-ray1.75L/M64-188[»]
    2GC4X-ray1.90B/F/J/N58-188[»]
    2GC7X-ray1.90B/F/J/N58-188[»]
    2J55X-ray2.15L/M58-188[»]
    2J56X-ray2.10L/M58-188[»]
    2J57X-ray2.25K/L/M/N58-188[»]
    2MTAX-ray2.40L64-188[»]
    3ORVX-ray1.91C/E58-188[»]
    3PXSX-ray2.22C/E58-188[»]
    3PXTX-ray2.16C/E58-188[»]
    3PXWX-ray2.11C/E58-188[»]
    3RLMX-ray2.13C/E58-188[»]
    3RMZX-ray1.72C/E58-188[»]
    3RN0X-ray1.91C/E58-188[»]
    4FA1X-ray2.18C/E58-188[»]
    4FA4X-ray2.14C/E58-188[»]
    4FA5X-ray1.94C/E58-188[»]
    4FA9X-ray2.09C/E58-188[»]
    4FANX-ray2.08C/E58-188[»]
    4FAVX-ray2.08C/E58-188[»]
    4FB1X-ray2.15C/E58-188[»]
    4K3IX-ray2.00C/E58-188[»]
    ProteinModelPortaliP22619.
    SMRiP22619. Positions 65-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22619.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.30.10. 1 hit.
    InterProiIPR016008. Amine_DH_Ltc.
    IPR013504. MADH/AADH_Ltc_C_dom.
    IPR004229. MeN_DH_Ltc.
    [Graphical view]
    PfamiPF02975. Me-amine-dh_L. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000192. Amine_dh_beta. 1 hit.
    SUPFAMiSSF57561. SSF57561. 1 hit.
    TIGRFAMsiTIGR02659. TTQ_MADH_Lt. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P22619-1 [UniParc]FASTAAdd to Basket

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    MLGNFRFDDM VEKLSRRVAG QTSRRSVIGK LGTAMLGIGL VPLLPVDRRG    50
    RVSRANAADA PAGTDPRAKW VPQDNDIQAC DYWRHCSIDG NICDCSGGSL 100
    TNCPPGTKLA TASWVASCYN PTDGQSYLIA YRDCCGYNVS GRCPCLNTEG 150
    ELPVYRPEFA NDIIWCFGAE DDAMTYHCTI SPIVGKAS 188
    Length:188
    Mass (Da):20,393
    Last modified:April 1, 1993 - v2
    Checksum:iE3D9DE4454268BE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90098 Genomic DNA. Translation: AAA25578.1.
    X55665 Genomic DNA. Translation: CAA39198.1.
    PIRiJH0661.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90098 Genomic DNA. Translation: AAA25578.1 .
    X55665 Genomic DNA. Translation: CAA39198.1 .
    PIRi JH0661.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MG2 X-ray 2.25 B/F/J/N 58-188 [» ]
    1MG3 X-ray 2.40 B/F/J/N 58-188 [» ]
    2BBK X-ray 1.75 L/M 64-188 [» ]
    2GC4 X-ray 1.90 B/F/J/N 58-188 [» ]
    2GC7 X-ray 1.90 B/F/J/N 58-188 [» ]
    2J55 X-ray 2.15 L/M 58-188 [» ]
    2J56 X-ray 2.10 L/M 58-188 [» ]
    2J57 X-ray 2.25 K/L/M/N 58-188 [» ]
    2MTA X-ray 2.40 L 64-188 [» ]
    3ORV X-ray 1.91 C/E 58-188 [» ]
    3PXS X-ray 2.22 C/E 58-188 [» ]
    3PXT X-ray 2.16 C/E 58-188 [» ]
    3PXW X-ray 2.11 C/E 58-188 [» ]
    3RLM X-ray 2.13 C/E 58-188 [» ]
    3RMZ X-ray 1.72 C/E 58-188 [» ]
    3RN0 X-ray 1.91 C/E 58-188 [» ]
    4FA1 X-ray 2.18 C/E 58-188 [» ]
    4FA4 X-ray 2.14 C/E 58-188 [» ]
    4FA5 X-ray 1.94 C/E 58-188 [» ]
    4FA9 X-ray 2.09 C/E 58-188 [» ]
    4FAN X-ray 2.08 C/E 58-188 [» ]
    4FAV X-ray 2.08 C/E 58-188 [» ]
    4FB1 X-ray 2.15 C/E 58-188 [» ]
    4K3I X-ray 2.00 C/E 58-188 [» ]
    ProteinModelPortali P22619.
    SMRi P22619. Positions 65-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6254N.
    IntActi P22619. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00895 ; UER00870 .
    BioCyci MetaCyc:MONOMER-3910.
    SABIO-RK P22619.

    Miscellaneous databases

    EvolutionaryTracei P22619.

    Family and domain databases

    Gene3Di 2.60.30.10. 1 hit.
    InterProi IPR016008. Amine_DH_Ltc.
    IPR013504. MADH/AADH_Ltc_C_dom.
    IPR004229. MeN_DH_Ltc.
    [Graphical view ]
    Pfami PF02975. Me-amine-dh_L. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000192. Amine_dh_beta. 1 hit.
    SUPFAMi SSF57561. SSF57561. 1 hit.
    TIGRFAMsi TIGR02659. TTQ_MADH_Lt. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans."
      Chistoserdov A.Y., Boyd J., Mathews F.S., Lidstrom M.E.
      Biochem. Biophys. Res. Commun. 184:1181-1189(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation."
      van Spanning R.J.M., Wansell C.W., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.
      FEBS Lett. 275:217-220(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-188.
      Strain: ATCC 19367 / NBRC 13301 / NCIMB 8944 / NRRL B-3785.
    3. "Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8-A resolution."
      Chen L., Mathews F.S., Davidson V.L., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.
      Proteins 14:288-299(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 64-188.
    4. "Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin."
      Chen L., Durley R., Poliks B.J., Hamada K., Chen Z., Mathews F.S., Davidson V.L., Satow Y., Huizinga E.G., Vellieux F.M.D., Hol W.G.J.
      Biochemistry 31:4959-4964(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 64-188 IN COMPLEX WITH AMICYANIN.
    5. "Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i."
      Chen L., Durley R., Mathews F.S., Davidson V.L.
      Science 264:86-90(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiDHML_PARDE
    AccessioniPrimary (citable) accession number: P22619
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

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

    External Data

    Dasty 3