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P29894

- DHMH_PARDE

UniProt

P29894 - DHMH_PARDE

Protein

Methylamine dehydrogenase heavy chain

Gene

mauB

Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (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.

    GO - Molecular functioni

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

    GO - Biological processi

    1. methylamine metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Transport

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3909.
    SABIO-RKP29894.

    Names & Taxonomyi

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

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Or 26Sequence AnalysisAdd
    BLAST
    Chaini29 – 417389Methylamine dehydrogenase heavy chainPRO_0000025580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi212 ↔ 227

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Tetramer of two light and two heavy chains.1 Publication

    Protein-protein interaction databases

    DIPiDIP-6253N.
    IntActiP29894. 1 interaction.

    Structurei

    Secondary structure

    1
    417
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi40 – 5819
    Beta strandi77 – 826
    Helixi84 – 863
    Beta strandi88 – 969
    Turni97 – 1004
    Beta strandi101 – 1088
    Beta strandi113 – 1164
    Beta strandi123 – 13210
    Beta strandi135 – 14511
    Turni147 – 1493
    Beta strandi152 – 1587
    Helixi170 – 1723
    Beta strandi173 – 1753
    Beta strandi179 – 1868
    Beta strandi188 – 1903
    Beta strandi192 – 1976
    Turni198 – 2014
    Beta strandi202 – 2087
    Beta strandi211 – 2199
    Beta strandi222 – 2276
    Beta strandi232 – 2365
    Beta strandi239 – 2413
    Beta strandi244 – 2474
    Beta strandi263 – 2653
    Turni266 – 2694
    Beta strandi270 – 2756
    Beta strandi278 – 2847
    Beta strandi296 – 2994
    Helixi301 – 3055
    Beta strandi308 – 3103
    Beta strandi312 – 3143
    Beta strandi316 – 3194
    Turni320 – 3234
    Beta strandi324 – 3318
    Beta strandi341 – 3488
    Turni349 – 3513
    Beta strandi354 – 36411
    Beta strandi366 – 3694
    Beta strandi372 – 3743
    Beta strandi376 – 3816
    Turni382 – 3854
    Beta strandi386 – 3916
    Turni392 – 3943
    Beta strandi397 – 4015
    Beta strandi410 – 4123

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MG2X-ray2.25A/E/I/M28-417[»]
    1MG3X-ray2.40A/E/I/M28-417[»]
    2BBKX-ray1.75H/J63-417[»]
    2GC4X-ray1.90A/E/I/M32-417[»]
    2GC7X-ray1.90A/E/I/M32-417[»]
    2J55X-ray2.15H/J32-417[»]
    2J56X-ray2.10H/J32-417[»]
    2J57X-ray2.25G/H/I/J32-417[»]
    2MTAX-ray2.40H45-417[»]
    ProteinModelPortaliP29894.
    SMRiP29894. Positions 36-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29894.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR013476. MeN_DH_Hvc.
    IPR009451. Metamine_DH_Hvc.
    IPR011044. Quino_amine_DH_bsu.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PfamiPF06433. Me-amine-dh_H. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017797. TTQ_MADH_Hv. 1 hit.
    SUPFAMiSSF50969. SSF50969. 1 hit.
    TIGRFAMsiTIGR02658. TTQ_MADH_Hv. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29894-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALPPNFMPL FRASLIGLGL GCSALALAAS AQDAPEAETQ AQETQGQAAA    50
    RAAAADLAAG QDDEPRILEA PAPDARRVYV NDPAHFAAVT QQFVIDGEAG 100
    RVIGMIDGGF LPNPVVADDG SFIAHASTVF SRIARGERTD YVEVFDPVTL 150
    LPTADIELPD APRFLVGTYP WMTSLTPDGK TLLFYQFSPA PAVGVVDLEG 200
    KAFKRMLDVP DCYHIFPTAP DTFFMHCRDG SLAKVAFGTE GTPEITHTEV 250
    FHPEDEFLIN HPAYSQKAGR LVWPTYTGKI HQIDLSSGDA KFLPAVEALT 300
    EAERADGWRP GGWQQVAYHR ALDRIYLLVD QRDEWRHKTA SRLLVVLDAK 350
    TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS 400
    VNQLGHGPQV ITTADMG 417
    Length:417
    Mass (Da):45,440
    Last modified:April 1, 1993 - v1
    Checksum:i8187A8B694208BE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90099 Genomic DNA. Translation: AAA25580.1.
    U12464 Genomic DNA. Translation: AAA56724.1.
    PIRiJH0660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90099 Genomic DNA. Translation: AAA25580.1 .
    U12464 Genomic DNA. Translation: AAA56724.1 .
    PIRi JH0660.

    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 A/E/I/M 28-417 [» ]
    1MG3 X-ray 2.40 A/E/I/M 28-417 [» ]
    2BBK X-ray 1.75 H/J 63-417 [» ]
    2GC4 X-ray 1.90 A/E/I/M 32-417 [» ]
    2GC7 X-ray 1.90 A/E/I/M 32-417 [» ]
    2J55 X-ray 2.15 H/J 32-417 [» ]
    2J56 X-ray 2.10 H/J 32-417 [» ]
    2J57 X-ray 2.25 G/H/I/J 32-417 [» ]
    2MTA X-ray 2.40 H 45-417 [» ]
    ProteinModelPortali P29894.
    SMRi P29894. Positions 36-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6253N.
    IntActi P29894. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3909.
    SABIO-RK P29894.

    Miscellaneous databases

    EvolutionaryTracei P29894.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR013476. MeN_DH_Hvc.
    IPR009451. Metamine_DH_Hvc.
    IPR011044. Quino_amine_DH_bsu.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    Pfami PF06433. Me-amine-dh_H. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017797. TTQ_MADH_Hv. 1 hit.
    SUPFAMi SSF50969. SSF50969. 1 hit.
    TIGRFAMsi TIGR02658. TTQ_MADH_Hv. 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. "Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator."
      van Spanning R.J.M., van der Palen C.J., Slotboom D.J., Reijnders W.N., Stouthamer A.H., Duine J.A.
      Eur. J. Biochem. 226:201-210(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
      Strain: ATCC 17741 / DSM 413 / NBRC 16712 / NCCB 22021 / NCIMB 11627.
    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).
    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) 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 nameiDHMH_PARDE
    AccessioniPrimary (citable) accession number: P29894
    Secondary accession number(s): Q79D76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 92 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

    Documents

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

    External Data

    Dasty 3