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UniProtKB/Swiss-Prot entry O28249


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

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Entry information
Entry name IORB_ARCFU
Primary accession number O28249
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 45)
Name and origin of the protein
Protein name Indolepyruvate oxidoreductase subunit iorB
Synonyms IOR
EC 1.2.7.8
Indolepyruvate ferredoxin oxidoreductase subunit beta
Gene name
Name: iorB
OrderedLocusNames: AF_2030
From
Archaeoglobus fulgidus [TaxID: 2234] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; Archaeoglobus.
Protein existence 3: Inferred from homology;
References
[1]
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
  • FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation of arylpyruvates (By similarity).
  • CATALYTIC ACTIVITY: (Indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+.
  • SUBUNIT: Heterodimer of the iorA and iorB subunits.
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
AE000782; AAB89225.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E69503; E69503.
RefSeq NP_070854.1; -.
3D structure databases
ModBase O28249.
Enzyme and pathway databases
BioCyc AFUL224325:AF_2030-MON; -.
Family and domain databases
InterPro IPR017719; Indolepyruvate_Fd_OxRdtase_bsu.
IPR002869; Pyrv_Fd/Flavodoxin_OxRdtase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.920.10; Pyrv_Fd/Flavodoxin_OxRdtase; 1.
Pfam PF01558; POR; 1.
Pfam graphical view of domain structure.
BLOCKS O28249.
Genome annotation databases
GeneID 1485256; -.
GenomeReviews AE000782_GR; AF_2030.
KEGG afu:AF2030; -.
NMPDR fig|224325.1.peg.2015; -.
TIGR AF_2030; -.
Phylogenomic databases
HOGENOM O28249; -.
Other
ProtoNet O28249.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   201  201     Indolepyruvate oxidoreductase subunit iorB. PRO_0000099931
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 21328 Da [This is the MW of the unprocessed precursor] CRC64: 2D677FEDA74D803E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLNIVVVGV GGQGALTTSG IIARAAMRAG LNVVTAETHG MAQRGGSVEV HVRIGDVRAP 

        70         80         90        100        110        120 
LIPEGGADVM IALEPAEALR YAKFLNKNTL VILNTRKIIP PSVTAGTAKY PELDEIIGEL 

       130        140        150        160        170        180 
RKVTPRVIPV NASEIAEKAG SVLATNVVVV GMLFGYYSMP FGIEHVEEAI RETMKSKIVD 

       190        200 
LNLKALKMGY NQAISGRPSA V 

O28249 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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