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UniProtKB/Swiss-Prot entry Q46509


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MOP_DESGI
Primary accession number Q46509
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 62)
Name and origin of the protein
Protein name Aldehyde oxidoreductase
Synonyms EC 1.2.99.7
Molybdenum iron sulfur protein
Gene name
Name: mop
From
Desulfovibrio gigas [TaxID: 879] 
Taxonomy Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8143744 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Eur. J. Biochem. 220:901-910(1994).
[2]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=7502041 [NCBI, ExPASy, EBI, Israel, Japan]
Romao M.J., Archer M., Moura I., Moura J.J.G., LeGall J., Engh R., Schneider M., Hof P., Huber R.;
"Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.";
Science 270:1170-1176(1995).
[3]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1073/pnas.93.17.8846; PubMed=8799115 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 93:8846-8851(1996).
[4]
X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS).
DOI=10.1007/s007750100255; PubMed=11713686 [NCBI, ExPASy, EBI, Israel, Japan]
Rebelo J.M., Dias J.M., Huber R., Moura J.J., Romao M.J.;
"Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A.";
J. Biol. Inorg. Chem. 6:791-800(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X77222; CAA54439.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A57429; A57429.
3D structure databases
PDB
1SIJ; X-ray; 2.30 A; A=1-907.[ExPASy / RCSB / EBI]
1VLB; X-ray; 1.28 A; A=1-907.[ExPASy / RCSB / EBI]
1ZCS; X-ray; 1.45 A; A=1-907.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SIJ; -.
1VLB; -.
1ZCS; -.
ModBase Q46509.
Ontologies
GO
GO:0033727; Molecular function: aldehyde dehydrogenase (FAD-independent) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.10.20.30; Ferredoxin_fold; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q46509.
Other
LinkHub Q46509; -.
ProtoNet Q46509.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 3D-structure; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   907  907     Aldehyde oxidoreductase. PRO_0000166102
DOMAIN   2    79  78     2Fe-2S ferredoxin-type. 
METAL   40    40        Iron-sulfur 1 (2Fe-2S). 
METAL   45    45        Iron-sulfur 1 (2Fe-2S). 
METAL   48    48        Iron-sulfur 1 (2Fe-2S). 
METAL   60    60        Iron-sulfur 1 (2Fe-2S). 
METAL   100   100        Iron-sulfur 2 (2Fe-2S). 
METAL   103   103        Iron-sulfur 2 (2Fe-2S). 
METAL   137   137        Iron-sulfur 2 (2Fe-2S). 
METAL   139   139        Iron-sulfur 2 (2Fe-2S). 
METAL   653   653        Molybdenum. 
METAL   869   869        Molybdenum. 
STRAND   2     8  7      
STRAND   11    17  7      
HELIX   23    29  7      
STRAND   39    45  7      
STRAND   49    52  4      
STRAND   55    58  4      
HELIX   59    61  3      
HELIX   64    66  3      
STRAND   72    74  3      
HELIX   76    79  4      
HELIX   87    95  9      
HELIX   104   115  12      
HELIX   123   132  10      
STRAND   138   140  3      
HELIX   143   156  14      
HELIX   162   165  4      
HELIX   185   189  5      
HELIX   196   201  6      
STRAND   208   214  7      
STRAND   216   226  11      
HELIX   228   231  4      
STRAND   236   240  5      
HELIX   242   244  3      
STRAND   249   251  3      
STRAND   267   270  4      
STRAND   272   275  4      
STRAND   281   289  9      
HELIX   290   297  8      
STRAND   301   306  6      
HELIX   313   317  5      
STRAND   330   341  12      
HELIX   343   349  7      
STRAND   351   360  10      
STRAND   372   377  6      
STRAND   383   388  6      
HELIX   392   403  12      
HELIX   407   409  3      
STRAND   410   414  5      
HELIX   423   425  3      
HELIX   430   440  11      
STRAND   444   447  4      
HELIX   450   455  6      
STRAND   463   471  9      
STRAND   477   487  11      
HELIX   495   505  11      
TURN   506   509  4      
STRAND   514   522  9      
TURN   533   536  4      
HELIX   537   555  19      
HELIX   559   566  8      
HELIX   585   606  22      
STRAND   609   626  18      
TURN   627   629  3      
STRAND   631   638  8      
STRAND   644   647  4      
STRAND   653   655  3      
HELIX   657   669  13      
HELIX   670   672  3      
HELIX   676   678  3      
STRAND   679   681  3      
TURN   686   688  3      
HELIX   700   719  20      
STRAND   724   726  3      
HELIX   729   734  6      
STRAND   740   746  7      
TURN   755   757  3      
STRAND   766   778  13      
TURN   779   781  3      
STRAND   784   794  11      
HELIX   801   820  20      
TURN   827   829  3      
STRAND   830   832  3      
TURN   833   837  5      
HELIX   841   843  3      
STRAND   848   852  5      
HELIX   861   863  3      
HELIX   870   872  3      
HELIX   875   887  13      
HELIX   898   906  9      
Sequence information
Length: 907 AA [This is the length of the unprocessed precursor] Molecular weight: 97035 Da [This is the MW of the unprocessed precursor] CRC64: 898E7EEF708A64DF [This is a checksum on the sequence]
        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 

Q46509 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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