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O28604

- O28604_ARCFU

UniProt

O28604 - O28604_ARCFU

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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: 1 out of 5- Experimental evidence at protein leveli

Functioni

Sites

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

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-1703-MONOMER.

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: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi224325.AF1669.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiAYNQEPD.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB89580.1 .
PIRi D69458.
RefSeqi NP_070497.1. NC_000917.1.
WP_010879165.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JNR X-ray 1.60 B/D 1-150 [» ]
1JNZ X-ray 2.50 B/D 1-150 [» ]
2FJA X-ray 2.00 B/D 1-150 [» ]
2FJB X-ray 1.70 B/D 1-150 [» ]
2FJD X-ray 1.84 B/D 1-150 [» ]
2FJE X-ray 1.80 B/D 1-150 [» ]
ProteinModelPortali O28604.
SMRi O28604. Positions 2-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224325.AF1669.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB89580 ; AAB89580 ; AF_1669 .
GeneIDi 1484892.
KEGGi afu:AF1669.

Phylogenomic databases

eggNOGi COG1146.
KOi K00395.
OMAi AYNQEPD.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-1703-MONOMER.

Miscellaneous databases

EvolutionaryTracei O28604.

Family and domain databases

InterProi IPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011802. AprB.
IPR022738. AprB_C.
[Graphical view ]
Pfami PF12139. APS-reductase_C. 1 hit.
PF00037. Fer4. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02060. aprB. 1 hit.
PROSITEi PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

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), 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 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: October 29, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome, Reference proteomeImported

External Data

Dasty 3