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Q46509

- MOP_DESGI

UniProt

Q46509 - MOP_DESGI

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Protein
Aldehyde oxidoreductase
Gene
mop
Organism
Desulfovibrio gigas
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

An aldehyde + H2O + acceptor = a carboxylate + reduced acceptor.

Cofactori

Binds 1 molybdenum-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.
Binds 2 2Fe-2S clusters per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi45 – 451Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi60 – 601Iron-sulfur 1 (2Fe-2S)1 Publication
Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi103 – 1031Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi137 – 1371Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)1 Publication
Metal bindingi653 – 6531Molybdenum
Metal bindingi869 – 8691Molybdenum

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. aldehyde dehydrogenase (FAD-independent) activity Source: UniProtKB-EC
  3. electron carrier activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

    Enzyme and pathway databases

    SABIO-RKQ46509.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde oxidoreductase (EC:1.2.99.7)
    Alternative name(s):
    Molybdenum iron sulfur protein
    Gene namesi
    Name:mop
    OrganismiDesulfovibrio gigas
    Taxonomic identifieri879 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 907907Aldehyde oxidoreductase
    PRO_0000166102Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87
    Beta strandi11 – 177
    Helixi23 – 297
    Beta strandi39 – 457
    Beta strandi49 – 524
    Beta strandi55 – 584
    Helixi59 – 613
    Helixi64 – 663
    Beta strandi72 – 743
    Helixi76 – 794
    Helixi87 – 959
    Helixi104 – 11512
    Helixi123 – 13210
    Beta strandi138 – 1403
    Helixi143 – 15614
    Helixi162 – 1654
    Helixi185 – 1895
    Helixi196 – 2016
    Beta strandi208 – 2147
    Beta strandi216 – 22611
    Helixi228 – 2314
    Beta strandi236 – 2405
    Helixi242 – 2443
    Beta strandi249 – 2513
    Beta strandi267 – 2704
    Beta strandi272 – 2754
    Beta strandi281 – 2899
    Helixi290 – 2978
    Beta strandi301 – 3066
    Helixi313 – 3175
    Beta strandi330 – 34112
    Helixi343 – 3497
    Beta strandi351 – 36010
    Beta strandi372 – 3776
    Beta strandi383 – 3886
    Helixi392 – 40312
    Helixi407 – 4093
    Beta strandi410 – 4145
    Helixi423 – 4253
    Helixi430 – 44011
    Beta strandi444 – 4474
    Helixi450 – 4556
    Beta strandi463 – 4719
    Beta strandi477 – 48711
    Helixi495 – 50511
    Turni506 – 5094
    Beta strandi514 – 5229
    Turni533 – 5364
    Helixi537 – 55519
    Helixi559 – 5668
    Helixi585 – 60622
    Beta strandi609 – 62618
    Turni627 – 6293
    Beta strandi631 – 6388
    Beta strandi644 – 6474
    Beta strandi653 – 6553
    Helixi657 – 66913
    Helixi670 – 6723
    Helixi676 – 6783
    Beta strandi679 – 6813
    Turni686 – 6883
    Helixi700 – 71920
    Beta strandi724 – 7263
    Helixi729 – 7346
    Beta strandi740 – 7467
    Turni755 – 7573
    Beta strandi766 – 77813
    Turni779 – 7813
    Beta strandi784 – 79411
    Helixi801 – 82020
    Turni827 – 8293
    Beta strandi830 – 8323
    Turni833 – 8375
    Helixi841 – 8433
    Beta strandi848 – 8525
    Beta strandi858 – 8603
    Helixi861 – 8633
    Helixi870 – 8723
    Helixi875 – 88713
    Beta strandi893 – 8953
    Helixi898 – 9069

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SIJX-ray2.30A1-907[»]
    1VLBX-ray1.28A1-907[»]
    3FAHX-ray1.72A1-907[»]
    3FC4X-ray1.79A1-907[»]
    3L4PX-ray1.45A1-907[»]
    4C7YX-ray1.57A1-907[»]
    4C7ZX-ray1.55A1-907[»]
    4C80X-ray1.50A1-907[»]
    ProteinModelPortaliQ46509.
    SMRiQ46509. Positions 1-907.

    Miscellaneous databases

    EvolutionaryTraceiQ46509.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 79782Fe-2S ferredoxin-type
    Add
    BLAST

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.90.1170.50. 1 hit.
    InterProiIPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    [Graphical view]
    PfamiPF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view]
    SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF56003. SSF56003. 1 hit.
    PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q46509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIQKVITVNG IEQNLFVDAE ALLSDVLRQQ LGLTGVKVGC EQGQCGACSV    50
    ILDGKVVRAC VTKMKRVADG AQITTIEGVG QPENLHPLQK AWVLHGGAQC 100
    GFCSPGFIVS AKGLLDTNAD PSREDVRDWF QKHRNACRCT GYKPLVDAVM 150
    DAAAVINGKK PETDLEFKMP ADGRIWGSKY PRPTAVAKVT GTLDYGADLG 200
    LKMPAGTLHL AMVQAKVSHA NIKGIDTSEA LTMPGVHSVI THKDVKGKNR 250
    ITGLITFPTN KGDGWDRPIL CDEKVFQYGD CIALVCADSE ANARAAAEKV 300
    KVDLEELPAY MSGPAAAAED AIEIHPGTPN VYFEQPIVKG EDTGPIFASA 350
    DVTVEGDFYV GRQPHMPIEP DVAFAYMGDD GKCYIHSKSI GVHLHLYMIA 400
    PGVGLEPDQL VLVANPMGGT FGYKFSPTSE ALVAVAAMAT GRPVHLRYNY 450
    QQQQQYTGKR SPWEMNVKFA AKKDGTLLAM ESDWLVDHGP YSEFGDLLTL 500
    RGAQFIGAGY NIPNIRGLGR TVATNHVWGS AFRGYGAPQS MFASECLMDM 550
    LAEKLGMDPL ELRYKNAYRP GDTNPTGQEP EVFSLPDMID QLRPKYQAAL 600
    EKAQKESTAT HKKGVGISIG VYGSGLDGPD ASEAWAELNA DGTITVHTAW 650
    EDHGQGADIG CVGTAHEALR PMGVAPEKIK FTWPNTATTP NSGPSGGSRQ 700
    QVMTGNAIRV ACENLLKACE KPGGGYYTYD ELKAADKPTK ITGNWTASGA 750
    THCDAVTGLG KPFVVYMYGV FMAEVTVDVA TGQTTVDGMT LMADLGSLCN 800
    QLATDGQIYG GLAQGIGLAL SEDFEDIKKH ATLVGAGFPF IKQIPDKLDI 850
    VYVNHPRPDG PFGASGVGEL PLTSPHAAII NAIKSATGVR IYRLPAYPEK 900
    VLEALKA 907
    Length:907
    Mass (Da):97,035
    Last modified:November 1, 1996 - v1
    Checksum:i898E7EEF708A64DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77222 Genomic DNA. Translation: CAA54439.1.
    PIRiA57429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77222 Genomic DNA. Translation: CAA54439.1 .
    PIRi A57429.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SIJ X-ray 2.30 A 1-907 [» ]
    1VLB X-ray 1.28 A 1-907 [» ]
    3FAH X-ray 1.72 A 1-907 [» ]
    3FC4 X-ray 1.79 A 1-907 [» ]
    3L4P X-ray 1.45 A 1-907 [» ]
    4C7Y X-ray 1.57 A 1-907 [» ]
    4C7Z X-ray 1.55 A 1-907 [» ]
    4C80 X-ray 1.50 A 1-907 [» ]
    ProteinModelPortali Q46509.
    SMRi Q46509. Positions 1-907.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q46509.

    Miscellaneous databases

    EvolutionaryTracei Q46509.

    Family and domain databases

    Gene3Di 1.10.150.120. 1 hit.
    3.10.20.30. 1 hit.
    3.30.365.10. 6 hits.
    3.90.1170.50. 1 hit.
    InterProi IPR002888. 2Fe-2S-bd.
    IPR001041. 2Fe-2S_ferredoxin-type.
    IPR006058. 2Fe2S_fd_BS.
    IPR000674. Ald_Oxase/Xan_DH_a/b.
    IPR008274. AldOxase/xan_DH_Mopterin-bd.
    IPR012675. Beta-grasp_dom.
    [Graphical view ]
    Pfami PF01315. Ald_Xan_dh_C. 1 hit.
    PF02738. Ald_Xan_dh_C2. 1 hit.
    PF00111. Fer2. 1 hit.
    PF01799. Fer2_2. 1 hit.
    [Graphical view ]
    SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47741. SSF47741. 1 hit.
    SSF54292. SSF54292. 1 hit.
    SSF54665. SSF54665. 1 hit.
    SSF56003. SSF56003. 1 hit.
    PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
    PS51085. 2FE2S_FER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase."
      Thoenes U., Flores O.L., Neves A., Devreese B., van Beeumen J.J., Huber R., Romao M.J., Legall J., Moura J.J.G., Rodriges-Pousada C.
      Eur. J. Biochem. 220:901-910(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas."
      Romao M.J., Archer M., Moura I., Moura J.J.G., LeGall J., Engh R., Schneider M., Hof P., Huber R.
      Science 270:1170-1176(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    3. "A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes."
      Huber R., Hof P., Duarte R.O., Moura J.J.G., Moura I., Liu M.-Y., LeGall J., Hille R., Archer M., Romao M.J.
      Proc. Natl. Acad. Sci. U.S.A. 93:8846-8851(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    4. "Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A."
      Rebelo J.M., Dias J.M., Huber R., Moura J.J., Romao M.J.
      J. Biol. Inorg. Chem. 6:791-800(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).

    Entry informationi

    Entry nameiMOP_DESGI
    AccessioniPrimary (citable) accession number: Q46509
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: March 19, 2014
    This is version 89 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

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