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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...

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 oxidoreductasePRO_0000166102Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
907
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 79782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MIQKVITVNG IEQNLFVDAE ALLSDVLRQQ LGLTGVKVGC EQGQCGACSV
60 70 80 90 100
ILDGKVVRAC VTKMKRVADG AQITTIEGVG QPENLHPLQK AWVLHGGAQC
110 120 130 140 150
GFCSPGFIVS AKGLLDTNAD PSREDVRDWF QKHRNACRCT GYKPLVDAVM
160 170 180 190 200
DAAAVINGKK PETDLEFKMP ADGRIWGSKY PRPTAVAKVT GTLDYGADLG
210 220 230 240 250
LKMPAGTLHL AMVQAKVSHA NIKGIDTSEA LTMPGVHSVI THKDVKGKNR
260 270 280 290 300
ITGLITFPTN KGDGWDRPIL CDEKVFQYGD CIALVCADSE ANARAAAEKV
310 320 330 340 350
KVDLEELPAY MSGPAAAAED AIEIHPGTPN VYFEQPIVKG EDTGPIFASA
360 370 380 390 400
DVTVEGDFYV GRQPHMPIEP DVAFAYMGDD GKCYIHSKSI GVHLHLYMIA
410 420 430 440 450
PGVGLEPDQL VLVANPMGGT FGYKFSPTSE ALVAVAAMAT GRPVHLRYNY
460 470 480 490 500
QQQQQYTGKR SPWEMNVKFA AKKDGTLLAM ESDWLVDHGP YSEFGDLLTL
510 520 530 540 550
RGAQFIGAGY NIPNIRGLGR TVATNHVWGS AFRGYGAPQS MFASECLMDM
560 570 580 590 600
LAEKLGMDPL ELRYKNAYRP GDTNPTGQEP EVFSLPDMID QLRPKYQAAL
610 620 630 640 650
EKAQKESTAT HKKGVGISIG VYGSGLDGPD ASEAWAELNA DGTITVHTAW
660 670 680 690 700
EDHGQGADIG CVGTAHEALR PMGVAPEKIK FTWPNTATTP NSGPSGGSRQ
710 720 730 740 750
QVMTGNAIRV ACENLLKACE KPGGGYYTYD ELKAADKPTK ITGNWTASGA
760 770 780 790 800
THCDAVTGLG KPFVVYMYGV FMAEVTVDVA TGQTTVDGMT LMADLGSLCN
810 820 830 840 850
QLATDGQIYG GLAQGIGLAL SEDFEDIKKH ATLVGAGFPF IKQIPDKLDI
860 870 880 890 900
VYVNHPRPDG PFGASGVGEL PLTSPHAAII NAIKSATGVR IYRLPAYPEK

VLEALKA
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...
MobiDBi 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: October 1, 2014
This is version 90 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