Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A1BB97

- A1BB97_PARDP

UniProt

A1BB97 - A1BB97_PARDP

Protein
Submitted name:

Methylamine dehydrogenase heavy chain

Gene

Pden_4730

Organism
Paracoccus denitrificans (strain Pd 1222)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei208 – 2081Acetate 2; via amide nitrogen
    Metal bindingi284 – 2841SodiumImported
    Metal bindingi287 – 2871SodiumImported
    Metal bindingi289 – 2891Sodium; via carbonyl oxygenImported

    GO - Molecular functioni

    1. amine dehydrogenase activity Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. methylamine dehydrogenase (amicyanin) activity Source: UniProtKB-EC

    GO - Biological processi

    1. methylamine metabolic process Source: InterPro

    Keywords - Molecular functioni

    OxidoreductaseImported

    Enzyme and pathway databases

    BioCyciPDEN318586:GCVQ-4773-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Methylamine dehydrogenase heavy chainImported (EC:1.4.9.1Imported)
    Gene namesi
    Ordered Locus Names:Pden_4730Imported
    Encoded oniPlasmid pPD1222Imported
    OrganismiParacoccus denitrificans (strain Pd 1222)Imported
    Taxonomic identifieri318586 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus
    ProteomesiUP000000361: Plasmid pPD1222

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232 PotentialImportedAdd
    BLAST
    Chaini33 – 417385 PotentialImportedPRO_5000183176Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    IntActiA1BB97. 2 interactions.
    STRINGi318586.Pden_4730.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L4MX-ray2.02D/F32-417[»]
    3L4OX-ray2.05D/F32-417[»]
    3ORVX-ray1.91D/F32-417[»]
    3PXSX-ray2.22D/F32-417[»]
    3PXTX-ray2.16D/F32-417[»]
    3PXWX-ray2.11D/F33-417[»]
    3RLMX-ray2.13D/F32-417[»]
    3RMZX-ray1.72D/F32-417[»]
    3RN0X-ray1.91D/F32-417[»]
    3RN1X-ray1.93D/F32-417[»]
    3SJLX-ray1.63D/F32-417[»]
    3SLEX-ray2.52D/F33-417[»]
    3SVWX-ray1.86D/F32-417[»]
    3SWSX-ray1.86D/F32-417[»]
    3SXTX-ray1.81D/F32-417[»]
    4FA1X-ray2.18D/F33-417[»]
    4FA4X-ray2.14D/F33-417[»]
    4FA5X-ray1.94D/F33-417[»]
    4FA9X-ray2.09D/F33-417[»]
    4FANX-ray2.08D/F33-417[»]
    4FAVX-ray2.08D/F33-417[»]
    4FB1X-ray2.15D/F33-417[»]
    4K3IX-ray2.00D/F33-417[»]
    4L1QX-ray1.92D/F33-417[»]
    4L3GX-ray2.05D/F33-417[»]
    4L3HX-ray1.79D/F33-417[»]
    4O1QX-ray2.59D/F33-417[»]
    ProteinModelPortaliA1BB97.
    SMRiA1BB97. Positions 36-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA1BB97.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 694Acetate binding

    Keywords - Domaini

    SignalImported

    Phylogenomic databases

    eggNOGiNOG68563.
    HOGENOMiHOG000147008.
    KOiK15229.
    OMAiDPGTQVW.
    OrthoDBiEOG60W7QQ.

    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.

    A1BB97-1 [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 SRFVVVLDAK 350
    TGERLAKFEM GHEIDSINVS QDEKPLLYAL STGDKTLYIH DAESGEELRS 400
    VNQLGHGPQV ITTADMG 417
    Length:417
    Mass (Da):45,460
    Last modified:January 23, 2007 - v1
    Checksum:i819B4EEE2AC6D340
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000491 Genomic DNA. Translation: ABL72791.1.
    RefSeqiYP_918487.1. NC_008688.1.

    Genome annotation databases

    EnsemblBacteriaiABL72791; ABL72791; Pden_4730.
    GeneIDi4583233.
    KEGGipde:Pden_4730.
    PATRICi22860685. VBIParDen97112_4694.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000491 Genomic DNA. Translation: ABL72791.1 .
    RefSeqi YP_918487.1. NC_008688.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L4M X-ray 2.02 D/F 32-417 [» ]
    3L4O X-ray 2.05 D/F 32-417 [» ]
    3ORV X-ray 1.91 D/F 32-417 [» ]
    3PXS X-ray 2.22 D/F 32-417 [» ]
    3PXT X-ray 2.16 D/F 32-417 [» ]
    3PXW X-ray 2.11 D/F 33-417 [» ]
    3RLM X-ray 2.13 D/F 32-417 [» ]
    3RMZ X-ray 1.72 D/F 32-417 [» ]
    3RN0 X-ray 1.91 D/F 32-417 [» ]
    3RN1 X-ray 1.93 D/F 32-417 [» ]
    3SJL X-ray 1.63 D/F 32-417 [» ]
    3SLE X-ray 2.52 D/F 33-417 [» ]
    3SVW X-ray 1.86 D/F 32-417 [» ]
    3SWS X-ray 1.86 D/F 32-417 [» ]
    3SXT X-ray 1.81 D/F 32-417 [» ]
    4FA1 X-ray 2.18 D/F 33-417 [» ]
    4FA4 X-ray 2.14 D/F 33-417 [» ]
    4FA5 X-ray 1.94 D/F 33-417 [» ]
    4FA9 X-ray 2.09 D/F 33-417 [» ]
    4FAN X-ray 2.08 D/F 33-417 [» ]
    4FAV X-ray 2.08 D/F 33-417 [» ]
    4FB1 X-ray 2.15 D/F 33-417 [» ]
    4K3I X-ray 2.00 D/F 33-417 [» ]
    4L1Q X-ray 1.92 D/F 33-417 [» ]
    4L3G X-ray 2.05 D/F 33-417 [» ]
    4L3H X-ray 1.79 D/F 33-417 [» ]
    4O1Q X-ray 2.59 D/F 33-417 [» ]
    ProteinModelPortali A1BB97.
    SMRi A1BB97. Positions 36-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi A1BB97. 2 interactions.
    STRINGi 318586.Pden_4730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABL72791 ; ABL72791 ; Pden_4730 .
    GeneIDi 4583233.
    KEGGi pde:Pden_4730.
    PATRICi 22860685. VBIParDen97112_4694.

    Phylogenomic databases

    eggNOGi NOG68563.
    HOGENOMi HOG000147008.
    KOi K15229.
    OMAi DPGTQVW.
    OrthoDBi EOG60W7QQ.

    Enzyme and pathway databases

    BioCyci PDEN318586:GCVQ-4773-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei A1BB97.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Functional importance of tyrosine 294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with histidine ."
      Abu Tarboush N., Jensen L.M., Feng M., Tachikawa H., Wilmot C.M., Davidson V.L.
      Biochemistry 49:9783-9791(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 32-417.
    3. "In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex."
      Jensen L.M., Sanishvili R., Davidson V.L., Wilmot C.M.
      Science 327:1392-1394(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 32-417.
    4. "Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation."
      Yukl E.T., Goblirsch B.R., Davidson V.L., Wilmot C.M.
      Biochemistry 50:2931-2938(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 33-417.
    5. "Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis."
      Tarboush N.A., Jensen L.M., Yukl E.T., Geng J., Liu A., Wilmot C.M., Davidson V.L.
      Proc. Natl. Acad. Sci. U.S.A. 108:16956-16961(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 32-417.
    6. "Mutagenesis of tryptophan199 reveals that electron hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis."
      Jensen L.M.R., Wilmot C.M.
      Submitted (APR-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 32-417.
    7. "Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of MauG."
      Jensen L.M.R., Wilmot C.M.
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 32-417.
    8. "Crystal Structure of the Quinone Form of Methylamine Dehydrogenase in Complex with the Diferric Form of MauG."
      Jensen L.M.R., Wilmot C.M.
      Submitted (JUL-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 32-417.
    9. "Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG."
      Feng M., Jensen L.M., Yukl E.T., Wei X., Liu A., Wilmot C.M., Davidson V.L.
      Biochemistry 51:1598-1606(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 32-417.
    10. "Structures of MauG in complex with quinol and quinone MADH."
      Yukl E.T., Jensen L.M., Davidson V.L., Wilmot C.M.
      Acta Crystallogr. F 69:738-743(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-417.
    11. "Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG."
      Abu Tarboush N., Yukl E.T., Shin S., Feng M., Wilmot C.M., Davidson V.L.
      Biochemistry 52:6358-6367(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 33-417.
    12. "Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis."
      Yukl E.T., Liu F., Krzystek J., Shin S., Jensen L.M., Davidson V.L., Wilmot C.M., Liu A.
      Proc. Natl. Acad. Sci. U.S.A. 110:4569-4573(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 33-417.
    13. "Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG."
      Shin S., Yukl E.T., Sehanobish E., Wilmot C.M., Davidson V.L.
      Biochemistry 53:1342-1349(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 33-417.

    Entry informationi

    Entry nameiA1BB97_PARDP
    AccessioniPrimary (citable) accession number: A1BB97
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, PlasmidImported, Reference proteomeImported

    External Data

    Dasty 3