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UniProtKB/Swiss-Prot entry Q59109


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

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Entry information
Entry name DSRA_ARCFU
Primary accession number Q59109
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Sulfite reductase, dissimilatory-type subunit alpha
Synonyms EC 1.8.99.3
Hydrogensulfite reductase subunit alpha
Gene name
Name: dsrA
OrderedLocusNames: AF_0423
From
Archaeoglobus fulgidus [TaxID: 2234] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; Archaeoglobus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-37; 65-71; 82-99; 124-141; 344-355; 362-368 AND 392-413.
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=7691984 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.;
"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes.";
J. Gen. Microbiol. 139:1817-1828(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
DOI=10.1038/37052; PubMed=9389475 [NCBI, ExPASy, EBI, Israel, Japan]
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
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
M95624; AAB17213.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000782; AAB90812.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G69302; G69302.
RefSeq NP_069259.1; -.
3D structure databases
PDB
3C7B; X-ray; 2.00 A; A/D=2-418.[ExPASy / RCSB / EBI]
PDBsum 3C7B; -.
ModBase Q59109.
Enzyme and pathway databases
BioCyc AFUL224325:AF_0423-MON; -.
MetaCyc:MON-12500; -.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0018551; Molecular function: hydrogensulfite reductase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011806; DsrA.
IPR006067; Nir_Sir_4Fe4S.
Graphical view of domain structure.
Pfam PF01077; NIR_SIR; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR02064; dsrA; 1.
PROSITE PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1483639; -.
GenomeReviews AE000782_GR; AF_0423.
KEGG afu:AF0423; -.
NMPDR fig|224325.1.peg.418; -.
TIGR AF_0423; -.
Phylogenomic databases
HOGENOM Q59109; -.
Other
ProtoNet Q59109.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; 4Fe-4S; Complete proteome; Direct protein sequencing; Heme; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   418  417     Sulfite reductase, dissimilatory-type subunit alpha. PRO_0000080025
DOMAIN   277   305  29     4Fe-4S ferredoxin-type. 
METAL   176   176        Iron (heme axial ligand) (Potential). 
METAL   182   182        Iron (heme axial ligand) (Potential). 
METAL   220   220        Iron (heme axial ligand) (Potential). 
METAL   224   224        Iron (heme axial ligand) (Potential). 
METAL   267   267        Iron-sulfur (4Fe-4S) (Potential). 
METAL   286   286        Iron-sulfur (4Fe-4S) (Potential). 
METAL   289   289        Iron-sulfur (4Fe-4S) (Potential). 
METAL   292   292        Iron-sulfur (4Fe-4S) (Potential). 
HELIX   5     8  4      
HELIX   9    11  3      
STRAND   12    15  4      
HELIX   18    35  18      
HELIX   44    58  15      
STRAND   75    79  5      
TURN   84    88  5      
HELIX   90    92  3      
STRAND   96   100  5      
HELIX   104   106  3      
STRAND   107   109  3      
HELIX   110   123  14      
STRAND   126   130  5      
STRAND   133   135  3      
STRAND   137   142  6      
HELIX   144   146  3      
HELIX   147   155  9      
STRAND   157   159  3      
STRAND   167   170  4      
HELIX   178   180  3      
HELIX   189   199  11      
HELIX   201   205  5      
STRAND   209   211  3      
STRAND   215   220  6      
HELIX   227   230  4      
STRAND   232   241  10      
HELIX   247   254  8      
HELIX   259   262  4      
HELIX   264   266  3      
STRAND   272   274  3      
STRAND   279   281  3      
TURN   283   285  3      
HELIX   291   295  5      
TURN   297   299  3      
STRAND   304   312  9      
TURN   318   320  3      
STRAND   326   332  7      
HELIX   339   355  17      
HELIX   362   369  8      
HELIX   371   377  7      
HELIX   384   386  3      
STRAND   387   389  3      
HELIX   400   402  3      
HELIX   407   415  9      
Sequence information
Length: 418 AA [This is the length of the unprocessed precursor] Molecular weight: 47525 Da [This is the MW of the unprocessed precursor] CRC64: AC12A7BFDF27EEEF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK QLEISYKDKK 

        70         80         90        100        110        120 
THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI NQPSGWFYST KALRGLCDVW 

       130        140        150        160        170        180 
EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC FEDLGNLEIP FDIGGSGSDL RTPSACMGPA 

       190        200        210        220        230        240 
LCEFACYDTL ELCYDLTMTY QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK 

       250        260        270        280        290        300 
DDIKVDQEAV KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL 

       310        320        330        340        350        360 
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD WWDEEGKFRE 

       370        380        390        400        410 
RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK DELKPSAYTE ELKKRGMW 

Q59109 in FASTA format

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