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Protein
Submitted name:

Adenylylsulfate reductase, subunit B (AprB)

Gene

AF_1669

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi3 – 31Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi10 – 101Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi11 – 111Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi13 – 131Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi21 – 211Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi25 – 251Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi47 – 471Iron-sulfur (4Fe-4S) 1Combined sources
Sitei48 – 481Important for catalytic activity
Metal bindingi50 – 501Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi53 – 531Iron-sulfur (4Fe-4S) 1Combined sources
Metal bindingi57 – 571Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi58 – 581Iron-sulfur (4Fe-4S) 2Combined sources
Metal bindingi62 – 621Iron-sulfur (4Fe-4S) 2Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

4Fe-4SUniRule annotationCombined sources, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1703-MONOMER.
BRENDAi1.8.99.2. 414.

Names & Taxonomyi

Protein namesi
Submitted name:
Adenylylsulfate reductase, subunit B (AprB)Imported
Gene namesi
Ordered Locus Names:AF_1669Imported
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)Imported
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1669.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNRX-ray1.60B/D1-150[»]
1JNZX-ray2.50B/D1-150[»]
2FJAX-ray2.00B/D1-150[»]
2FJBX-ray1.70B/D1-150[»]
2FJDX-ray1.84B/D1-150[»]
2FJEX-ray1.80B/D1-150[»]
ProteinModelPortaliO28604.
SMRiO28604. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO28604.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG1146.
KOiK00395.
OMAiCPNDLMV.

Family and domain databases

InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011802. AprB.
IPR022738. AprB_C.
[Graphical view]
PfamiPF12139. APS-reductase_C. 1 hit.
PF00037. Fer4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02060. aprB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSFVNPEKC DGCKALERTA CEYICPNDLM TLDKEKMKAY NREPDMCWEC
60 70 80 90 100
YSCVKMCPQG AIDVRGYVDY SPLGGACVPM RGTSDIMWTV KYRNGKVLRF
110 120 130 140 150
KFAIRTTPWG SIQPFEGFPE PTEEALKSEL LAGEPEIIGT SEFPQVKKKA
Length:150
Mass (Da):16,938
Last modified:January 1, 1998 - v1
Checksum:i5136A55608ADC183
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89580.1.
PIRiD69458.
RefSeqiNP_070497.1. NC_000917.1.
WP_010879165.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89580; AAB89580; AF_1669.
GeneIDi1484892.
KEGGiafu:AF1669.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89580.1.
PIRiD69458.
RefSeqiNP_070497.1. NC_000917.1.
WP_010879165.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNRX-ray1.60B/D1-150[»]
1JNZX-ray2.50B/D1-150[»]
2FJAX-ray2.00B/D1-150[»]
2FJBX-ray1.70B/D1-150[»]
2FJDX-ray1.84B/D1-150[»]
2FJEX-ray1.80B/D1-150[»]
ProteinModelPortaliO28604.
SMRiO28604. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF1669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89580; AAB89580; AF_1669.
GeneIDi1484892.
KEGGiafu:AF1669.

Phylogenomic databases

eggNOGiCOG1146.
KOiK00395.
OMAiCPNDLMV.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1703-MONOMER.
BRENDAi1.8.99.2. 414.

Miscellaneous databases

EvolutionaryTraceiO28604.

Family and domain databases

InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011802. AprB.
IPR022738. AprB_C.
[Graphical view]
PfamiPF12139. APS-reductase_C. 1 hit.
PF00037. Fer4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02060. aprB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 100126Imported.
  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 IRON-SULFUR (4FE-4S).
  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 IRON-SULFUR (4FE-4S).

Entry informationi

Entry nameiO28604_ARCFU
AccessioniPrimary (citable) accession number: O28604
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 24, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.