ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O28429


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name COOS_ARCFU
Primary accession number O28429
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2003
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 49)
Name and origin of the protein
Protein name Carbon monoxide dehydrogenase
Synonyms CODH
EC 1.2.99.2
Gene name
Name: cooS
OrderedLocusNames: AF_1849
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
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; AAB89403.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H69480; H69480.
RefSeq NP_070675.1; -.
3D structure databases
HSSP Q9F8A8; 1JJY. [HSSP ENTRY / PDB]
ModBase O28429.
Enzyme and pathway databases
BioCyc AFUL224325:AF_1849-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0006091; Biological process: generation of precursor metabolites and energy (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016101; CO_DHase_a-bundle.
IPR010047; CO_DHase_cat.
IPR004137; Prismane.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 1.
Pfam PF03063; Prismane; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005023; CODH; 1.
TIGRFAMs TIGR01702; CO_DH_cata; 1.
Genome annotation databases
GeneID 1485070; -.
GenomeReviews AE000782_GR; AF_1849.
KEGG afu:AF1849; -.
NMPDR fig|224325.1.peg.1836; -.
TIGR AF_1849; -.
Phylogenomic databases
HOGENOM O28429; -.
Other
ProtoNet O28429.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   622  622     Carbon monoxide dehydrogenase. PRO_0000157140
METAL   40    40        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   49    49        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   52    52        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   57    57        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   68    68        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   256   256        Nickel-iron-sulfur (By similarity). 
METAL   334   334        Nickel-iron-sulfur (By similarity). 
METAL   442   442        Nickel-iron-sulfur (By similarity). 
METAL   473   473        Nickel-iron-sulfur (By similarity). 
METAL   514   514        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 622 AA [This is the length of the unprocessed precursor] Molecular weight: 67496 Da [This is the MW of the unprocessed precursor] CRC64: 018304F4C49177B4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKIEGKVSEH ESINMMYERV SKEGVTNIVD RFNAQEKGRC PFCEKGLSCQ LCSMGPCRIS 

        70         80         90        100        110        120 
KDKPTGACGI DAAGMVVRNF THKNMLGTEA YTYHAIEAAK TLKATAEGKT IYEIKDVEKL 

       130        140        150        160        170        180 
KWFAKLLGIE GEDVNELAAK VADFVISDLS SLEKSRLVEI FAPEKRKELW EKLGIFPSGV 

       190        200        210        220        230        240 
FQELLTMGSS AMTNVDSNYV SLAKKSMSMS IATCMAAQIA LETIQDILFG TPMPHESHSD 

       250        260        270        280        290        300 
LGILDPEYVN IAVNGHEPFV GIALIKLAER EEIQEKARKA GAKGLRIIGF IETGQEILQR 

       310        320        330        340        350        360 
VDSPVFAGIV GNWIVQEYAL ATGCVDVFAA DMNCTLPSLP EYQRYGVKIV PVSRLVRLKG 

       370        380        390        400        410        420 
IDEGLDYEPE KAEEIAMKLI DMAIENFKQR DKSKAVKVEQ KKKIVVGFSP EAILKALNGD 

       430        440        450        460        470        480 
LNVLLDAIKK GDIKGVVALV SCTTLKNGPH DSSTVTIAKE LIKRDILVLS MGCGNAALQV 

       490        500        510        520        530        540 
AGLTSMEAVE LAGEKLKAVC KALNIPPVLS FGTCTDTGRA AYLVRLIADA LGVDVPQLPV 

       550        560        570        580        590        600 
AVTAPEYMEQ KATIDAVFAV AYGLTTHVSP VPPITGSEDA VKLFTEDVEK LTGGKVVVEE 

       610        620 
DPLKAAELLE KVIEEKRKAL GI 

O28429 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

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

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!