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Q54527 (Q54527_9ACTO) Unreviewed, UniProtKB/TrEMBL

Last modified July 27, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:rdmB EMBL AAA83421.1
OrganismStreptomyces purpurascens EMBL AAA83421.1
Taxonomic identifier1924 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region190 – 1912S-adenosyl-L-homocysteine binding PDB 1R00
Region190 – 1912S-adenosyl-L-methionine binding PDB 1XDS PDB 1QZZ
Region240 – 2412S-adenosyl-L-homocysteine binding PDB 1R00
Region240 – 2412S-adenosyl-L-methionine binding PDB 1XDS PDB 1QZZ

Sites

Binding site1461S-adenosyl-L-homocysteine PDB 1R00
Binding site1461S-adenosyl-L-methionine PDB 1XDS PDB 1QZZ
Binding site1711S-adenosyl-L-homocysteine PDB 1R00
Binding site1711S-adenosyl-L-methionine PDB 1QZZ
Binding site2131S-adenosyl-L-homocysteine PDB 1R00
Binding site2131S-adenosyl-L-methionine PDB 1XDS PDB 1QZZ
Binding site2551S-adenosyl-L-homocysteine PDB 1R00
Binding site2551S-adenosyl-L-methionine PDB 1XDS PDB 1QZZ

Sequences

Sequence LengthMass (Da)Tools
Q54527 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 427F37F5C59EEAD2

FASTA37439,797
        10         20         30         40         50         60 
MSSSSPGEPL EPTDQDLDVL LKNLGNLVTP MALRVAATLR LVDHLLAGAD TLAGLADRTD 

        70         80         90        100        110        120 
THPQALSRLV RHLTVVGVLE GGEKQGRPLR PTRLGMLLAD GHPAQQRAWL DLNGAVSHAD 

       130        140        150        160        170        180 
LAFTGLLDVV RTGRPAYAGR YGRPFWEDLS ADVALADSFD ALMSCDEDLA YEAPADAYDW 

       190        200        210        220        230        240 
SAVRHVLDVG GGNGGMLAAI ALRAPHLRGT LVELAGPAER ARRRFADAGL ADRVTVAEGD 

       250        260        270        280        290        300 
FFKPLPVTAD VVLLSFVLLN WSDEDALTIL RGCVRALEPG GRLLVLDRAD VEGDGADRFF 

       310        320        330        340        350        360 
STLLDLRMLT FMGGRVRTRD EVVDLAGSAG LALASERTSG STTLPFDFSI LEFTAVSEEA 

       370 
APAAQASEAL PAQE 

« Hide

References

[1]"Nucleotide sequences and expression of genes from Streptomyces purpurascens that cause the production of new anthracyclines in Streptomyces galilaeus."
Niemi J., Mantsala P.
J. Bacteriol. 177:2942-2945(1995) [PubMed: 7751313] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 25489 EMBL AAA83421.1.
[2]"Hybrid anthracycline antibiotics: production of new anthracyclines by cloned genes from Streptomyces purpurascens in Streptomyces galilaeus."
Niemi J., Ylihonko K., Hakala J., Parssinen R., Kopio A., Mantsala P.
Microbiology 140:1351-1358(1994) [PubMed: 8081500] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 25489 EMBL AAA83421.1.
[3]"Characterization of the gene cluster involved in rhodomycin biosynthesis."
Halo L., Wang Y., Mantsala P., Hakala J., Ylihonko K.
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 25489 EMBL AAA83421.1.
[4]Niemi J.T.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 25489 EMBL AAA83421.1.
[5]Halo L., Wang Y., Mantsala P., Hakala J., Ylihonko K.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 25489 EMBL AAA83421.1.
[6]"Crystal structure of aclacinomycin-10-hydroxylase, a S-adenosyl-L-methionine-dependent methyltransferase homolog involved in anthracycline biosynthesis in Streptomyces purpurascens."
Jansson A., Niemi J., Lindqvist Y., Mantsala P., Schneider G.
J. Mol. Biol. 334:269-280(2003) [PubMed: 14607118] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND S-ADENOSYL-L-METHIONINE.
[7]"Aclacinomycin 10-hydroxylase is a novel substrate-assisted hydroxylase requiring S-adenosyl-L-methionine as cofactor."
Jansson A., Koskiniemi H., Erola A., Wang J., Mantsala P., Schneider G., Niemi J.
J. Biol. Chem. 280:3636-3644(2005) [PubMed: 15548527] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10405 Genomic DNA. Translation: AAA83421.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZZX-ray2.10A1-374[»]
1R00X-ray2.50A1-374[»]
1XDSX-ray2.30A/B1-374[»]
1XDUX-ray2.70A1-374[»]
ProteinModelPortalQ54527.
SMRQ54527. Positions 10-357.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016461. O-MeTrfase_COMT_euk.
IPR001077. O_MeTrfase_2.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFPIRSF005739. O-mtase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ54527_9ACTO
AccessionPrimary (citable) accession number: Q54527
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: July 27, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)