Skip Header

Contribute Send feedback
Read comments (?) or add your own

O28603 (O28603_ARCFU) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 78. Feed History...

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

Names and origin

Protein namesSubmitted name:
Adenylylsulfate reductase, subunit A (AprA) EMBL AAB89579.1
Gene names
Ordered Locus Names:AF_1670
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP] EMBL AAB89579.1
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding32 – 332FAD
Nucleotide binding32 – 332FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding56 – 572FAD
Nucleotide binding56 – 572FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding63 – 653FAD
Nucleotide binding63 – 653FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding72 – 743FAD
Nucleotide binding72 – 743FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding175 – 1762FAD
Nucleotide binding175 – 1762FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding234 – 2352FAD
Nucleotide binding234 – 2352FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding239 – 2424FAD
Nucleotide binding239 – 2424FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding264 – 2652AMP PDB 2FJB
Nucleotide binding273 – 2775ADP analog PDB 2FJA
Nucleotide binding397 – 3982FAD cofactor analog PDB 2FJB PDB 2FJD
Nucleotide binding398 – 3992ADP analog PDB 2FJA

Sites

Active site3981Proton donor/acceptor
Binding site741ADP analog PDB 2FJA
Binding site741Substrate
Binding site951ADP analog PDB 2FJA
Binding site951AMP PDB 2FJB
Binding site1411Substrate
Binding site1451ADP analog PDB 2FJA
Binding site1451AMP PDB 2FJB
Binding site2141FAD; via carbonyl oxygen
Binding site2341Substrate
Binding site2651ADP analog PDB 2FJA
Binding site2651FAD cofactor analog PDB 2FJB PDB 2FJD
Binding site2651Substrate
Binding site2771AMP PDB 2FJB
Binding site2821AMP; via carbonyl oxygen PDB 2FJB
Binding site2921AMP PDB 2FJB
Binding site3171ADP analog PDB 2FJA
Binding site3171AMP PDB 2FJB
Binding site3611Substrate
Binding site3651FAD PDB 2FJA
Binding site3971FAD
Binding site4391FAD cofactor analog; via amide nitrogen PDB 2FJB PDB 2FJD
Binding site4391FAD; via amide nitrogen
Binding site4491FAD
Binding site4491FAD cofactor analog PDB 2FJB PDB 2FJD
Site4491Important for catalytic activity

Sequences

Sequence LengthMass (Da)Tools
O28603 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A57091382F2E9F4A

FASTA64373,270
        10         20         30         40         50         60 
MVYYPKKYEL YKADEVPTEV VETDILIIGG GFSGCGAAYE AAYWAKLGGL KVTLVEKAAV 

        70         80         90        100        110        120 
ERSGAVAQGL SAINTYIDLT GRSERQNTLE DYVRYVTLDM MGLAREDLVA DYARHVDGTV 

       130        140        150        160        170        180 
HLFEKWGLPI WKTPDGKYVR EGQWQIMIHG ESYKPIIAEA AKMAVGEENI YERVFIFELL 

       190        200        210        220        230        240 
KDKNDPNAVA GAVGFSVREP KFYVFKAKAV ILATGGATLL FRPRSTGEAA GRTWYAIFDT 

       250        260        270        280        290        300 
GSGYYMGLKA GAMLTQFEHR FIPFRFKDGY GPVGAWFLFF KCKAKNAYGE EYIKTRAAEL 

       310        320        330        340        350        360 
EKYKPYGAAQ PIPTPLRNHQ VMLEIMDGNQ PIYMHTEEAL AELAGGDKKK LKHIYEEAFE 

       370        380        390        400        410        420 
DFLDMTVSQA LLWACQNIDP QEQPSEAAPA EPYIMGSHSG EAGFWVCGPE DLMPEEYAKL 

       430        440        450        460        470        480 
FPLKYNRMTT VKGLFAIGDC AGANPHKFSS GSFTEGRIAA KAAVRFILEQ KPNPEIDDAV 

       490        500        510        520        530        540 
VEELKKKAYA PMERFMQYKD LSTADDVNPE YILPWQGLVR LQKIMDEYAA GIATIYKTNE 

       550        560        570        580        590        600 
KMLQRALELL AFLKEDLEKL AARDLHELMR AWELVHRVWT AEAHVRHMLF RKETRWPGYY 

       610        620        630        640 
YRTDYPELND EEWKCFVCSK YDAEKDEWTF EKVPYVQVIE WSF

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
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. expand/collapse author list , 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.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution."
Fritz G., Roth A., Schiffer A., Buchert T., Bourenkov G., Bartunik H.D., Huber H., Stetter K.O., Kroneck P.M., Ermler U.
Proc. Natl. Acad. Sci. U.S.A. 99:1836-1841(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH FAD, ACTIVE SITE.
[3]"Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5'-phosphosulfate reductase based on the structural characterization of different enzymatic states."
Schiffer A., Fritz G., Kroneck P.M., Ermler U.
Biochemistry 45:2960-2967(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ADP ANALOG; AMP; FAD AND FAD COFACTOR ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB89579.1.
PIRE69458.
RefSeqNP_070498.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNRX-ray1.60A/C1-643[»]
1JNZX-ray2.50A/C1-643[»]
2FJAX-ray2.00A/C1-643[»]
2FJBX-ray1.70A/C1-643[»]
2FJDX-ray1.84A/C1-643[»]
2FJEX-ray1.80A/C1-643[»]
ProteinModelPortalO28603.
SMRO28603. Positions 2-643.
ModBaseSearch...

Protein-protein interaction databases

STRING224325.AF1670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB89579; AAB89579; AF_1670.
GeneID1484893.
KEGGafu:AF1670.

Phylogenomic databases

eggNOGCOG1053.
KOK00394.
OMAYDLGRHV.
ProtClustDBPRK06854.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-1704-MONOMER.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
InterProIPR011803. AprA.
IPR003953. FAD_bind_dom.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR02061. aprA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO28603.

Entry information

Entry nameO28603_ARCFU
AccessionPrimary (citable) accession number: O28603
Entry history
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info