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Q46509 (MOP_DESGI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde oxidoreductase
EC=1.2.99.7
Alternative name(s):
Molybdenum iron sulfur protein
Gene names
Name:mop
OrganismDesulfovibrio gigas
Taxonomic identifier879 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio

Protein attributes

Sequence length907 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 Mo6+ ion per subunit.

Binds 1 molybdopterin cytosine dinucleotide (MCD) subunit.

Binds 2 2Fe-2S clusters per subunit.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the xanthine dehydrogenase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 907907Aldehyde oxidoreductase
PRO_0000166102

Regions

Domain2 – 79782Fe-2S ferredoxin-type

Sites

Metal binding401Iron-sulfur 1 (2Fe-2S) Ref.2
Metal binding451Iron-sulfur 1 (2Fe-2S) Ref.2
Metal binding481Iron-sulfur 1 (2Fe-2S) Ref.2
Metal binding601Iron-sulfur 1 (2Fe-2S) Ref.2
Metal binding1001Iron-sulfur 2 (2Fe-2S) Ref.2
Metal binding1031Iron-sulfur 2 (2Fe-2S) Ref.2
Metal binding1371Iron-sulfur 2 (2Fe-2S) Ref.2
Metal binding1391Iron-sulfur 2 (2Fe-2S) Ref.2
Metal binding6531Molybdenum
Metal binding8691Molybdenum

Secondary structure

1 ....................................................................................................................................................... 907
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46509 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 898E7EEF708A64DF

FASTA90797,035
        10         20         30         40         50         60 
MIQKVITVNG IEQNLFVDAE ALLSDVLRQQ LGLTGVKVGC EQGQCGACSV ILDGKVVRAC 

        70         80         90        100        110        120 
VTKMKRVADG AQITTIEGVG QPENLHPLQK AWVLHGGAQC GFCSPGFIVS AKGLLDTNAD 

       130        140        150        160        170        180 
PSREDVRDWF QKHRNACRCT GYKPLVDAVM DAAAVINGKK PETDLEFKMP ADGRIWGSKY 

       190        200        210        220        230        240 
PRPTAVAKVT GTLDYGADLG LKMPAGTLHL AMVQAKVSHA NIKGIDTSEA LTMPGVHSVI 

       250        260        270        280        290        300 
THKDVKGKNR ITGLITFPTN KGDGWDRPIL CDEKVFQYGD CIALVCADSE ANARAAAEKV 

       310        320        330        340        350        360 
KVDLEELPAY MSGPAAAAED AIEIHPGTPN VYFEQPIVKG EDTGPIFASA DVTVEGDFYV 

       370        380        390        400        410        420 
GRQPHMPIEP DVAFAYMGDD GKCYIHSKSI GVHLHLYMIA PGVGLEPDQL VLVANPMGGT 

       430        440        450        460        470        480 
FGYKFSPTSE ALVAVAAMAT GRPVHLRYNY QQQQQYTGKR SPWEMNVKFA AKKDGTLLAM 

       490        500        510        520        530        540 
ESDWLVDHGP YSEFGDLLTL RGAQFIGAGY NIPNIRGLGR TVATNHVWGS AFRGYGAPQS 

       550        560        570        580        590        600 
MFASECLMDM LAEKLGMDPL ELRYKNAYRP GDTNPTGQEP EVFSLPDMID QLRPKYQAAL 

       610        620        630        640        650        660 
EKAQKESTAT HKKGVGISIG VYGSGLDGPD ASEAWAELNA DGTITVHTAW EDHGQGADIG 

       670        680        690        700        710        720 
CVGTAHEALR PMGVAPEKIK FTWPNTATTP NSGPSGGSRQ QVMTGNAIRV ACENLLKACE 

       730        740        750        760        770        780 
KPGGGYYTYD ELKAADKPTK ITGNWTASGA THCDAVTGLG KPFVVYMYGV FMAEVTVDVA 

       790        800        810        820        830        840 
TGQTTVDGMT LMADLGSLCN QLATDGQIYG GLAQGIGLAL SEDFEDIKKH ATLVGAGFPF 

       850        860        870        880        890        900 
IKQIPDKLDI VYVNHPRPDG PFGASGVGEL PLTSPHAAII NAIKSATGVR IYRLPAYPEK 


VLEALKA

« Hide

References

[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X77222 Genomic DNA. Translation: CAA54439.1.
PIRA57429.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SIJX-ray2.30A1-907[»]
1VLBX-ray1.28A1-907[»]
3FAHX-ray1.72A1-907[»]
3FC4X-ray1.79A1-907[»]
3L4PX-ray1.45A1-907[»]
ProteinModelPortalQ46509.
SMRQ46509. Positions 1-907.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ46509.

Family and domain databases

Gene3D1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProIPR002888. 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]
PfamPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
SMARTSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMSSF47741. 2Fe-2S_bind. 1 hit.
SSF56003. Ald_xan_DH_mo_bd. 1 hit.
SSF54665. Aldxan_dh_hamm. 1 hit.
SSF54292. Ferredoxin. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ46509.

Entry information

Entry nameMOP_DESGI
AccessionPrimary (citable) accession number: Q46509
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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