Skip Header

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

B3WM30 (B3WM30_ECOLX) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 16. Feed History...

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

Names and origin

Protein namesRecommended name:
Sulfate adenylyltransferase subunit 2 HAMAP MF_00064

EC=2.7.7.4 HAMAP MF_00064
Alternative name(s):
ATP-sulfurylase small subunit HAMAP MF_00064
Sulfate adenylate transferase HAMAP MF_00064
Gene names
Name:cysD HAMAP MF_00064 EMBL EDX30409.1
ORF Names:EcB171_0467 EMBL EDX30409.1
OrganismEscherichia coli B171 EMBL EDX30409.1
Taxonomic identifier344601 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP MF_00064 SAAS SAAS002500

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP MF_00064

Subunit structure

Heterodimer composed of CysD, the smaller subunit, and CysN By similarity. HAMAP MF_00064

Sequence similarities

Belongs to the PAPS reductase family. CysD subfamily. HAMAP MF_00064

Sequences

Sequence LengthMass (Da)Tools
B3WM30 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 825263606FC8858E

FASTA30235,203
        10         20         30         40         50         60 
MDQKRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL 

        70         80         90        100        110        120 
LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK 

       130        140        150        160        170        180 
QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES 

       190        200        210        220        230        240 
IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR IDLQPGEVIK 

       250        260        270        280        290        300 
KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG 


YF 

« Hide

References

[1]Rasko D.A., Rosovitz M.J., Kaper J.B., Myers G.S.A., Sheshadri R., Cer R.Z., Jiang L., Ravel J.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B171 EMBL EDX30409.1.
[2]Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., Ravel J., Fricke W.F., Sebastian Y.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: B171 EMBL EDX30409.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAJX02000011 Genomic DNA. Translation: EDX30409.1.

3D structure databases

ProteinModelPortalB3WM30.
SMRB3WM30. Positions 5-212.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC31231957. VBIEscCol100091_2309.

Family and domain databases

HAMAPMF_00064. Sulf_adenylyltr_sub2.
[Tree]
InterProIPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011784. SO4_adenylTrfase_ssu.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFPIRSF002936. CysDAde_trans. 1 hit.
TIGRFAMsTIGR02039. CysD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB3WM30_ECOLX
AccessionPrimary (citable) accession number: B3WM30
Entry history
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: December 14, 2011
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)