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Reviewed, UniProtKB/Swiss-Prot Q00441 (CPXJ_SACEN)

Last modified July 13, 2010. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
6-deoxyerythronolide B hydroxylase
Short name=6-DEB hydroxylase
EC=1.14.-.-
Alternative name(s):
Erythomycin A biosynthesis hydrolase
Cytochrome P450 107A1
CYPCVIIA1
Cytochrome P450eryF
Gene names
Name:eryF
Synonyms:CYP107A1
Ordered Locus Names:SACE_0730
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Saccharopolyspora
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Protein attributesHide

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.
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General annotation (Comments)Hide

Function

Conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB.

Cofactor

Heme group.

Pathway

Antibiotic biosynthesis; erythromycin biosynthesis.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

A mutated form of this enzyme leads to the formation of deoxyerythromycin A, an antibiotic with improved pharmacological properties.

Sequence similarities

Belongs to the cytochrome P450 family.

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OntologiesHide

Keywords
   Biological processAntibiotic biosynthesis
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4044046-deoxyerythronolide B hydroxylase
PRO_0000052220

Sites

Metal binding3511Iron (heme axial ligand)

Experimental info

Sequence conflict2611P → PDQ in CAA42927. Ref.1
Sequence conflict3021G → R in CAA42927. Ref.1

Secondary structure

1 ....................................................................... 404
Helix Strand Turn

Details...

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SequencesHide

Sequence LengthMass (Da)Tools
Q00441-1 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 257ABEFC2D88B3FE

FASTA40445,099
        10         20         30         40         50         60 
MTTVPDLESD SFHVDWYRTY AELRETAPVT PVRFLGQDAW LVTGYDEAKA ALSDLRLSSD 

        70         80         90        100        110        120 
PKKKYPGVEV EFPAYLGFPE DVRNYFATNM GTSDPPTHTR LRKLVSQEFT VRRVEAMRPR 

       130        140        150        160        170        180 
VEQITAELLD EVGDSGVVDI VDRFAHPLPI KVICELLGVD EKYRGEFGRW SSEILVMDPE 

       190        200        210        220        230        240 
RAEQRGQAAR EVVNFILDLV ERRRTEPGDD LLSALIRVQD DDDGRLSADE LTSIALVLLL 

       250        260        270        280        290        300 
AGFEASVSLI GIGTYLLLTH PDQLALVRRD PSALPNAVEE ILRYIAPPET TTRFAAEEVE 

       310        320        330        340        350        360 
IGGVAIPQYS TVLVANGAAN RDPKQFPDPH RFDVTRDTRG HLSFGQGIHF CMGRPLAKLE 

       370        380        390        400 
GEVALRALFG RFPALSLGID ADDVVWRRSL LLRGIDHLPV RLDG

« Hide

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ReferencesHide

« Hide 'large scale' references
[1]"Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases."
Haydock S.F., Dowson J.A., Dhillon N., Roberts G.A., Cortes J., Leadlay P.F.
Mol. Gen. Genet. 230:120-128(1991) [PubMed: 1840640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea."
Weber J.M., Leung J.O., Swanson S.J., Idler K.B., McAlpine J.B.
Science 252:114-117(1991) [PubMed: 2011746] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed: 17369815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Structure of cytochrome P450eryF involved in erythromycin biosynthesis."
Cupp-Vickery J.L., Poulos T.L.
Nat. Struct. Biol. 2:144-153(1995) [PubMed: 7749919] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[5]"Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity."
Cupp-Vickery J., Anderson R., Hatziris Z.
Proc. Natl. Acad. Sci. U.S.A. 97:3050-3055(2000) [PubMed: 10716705] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[6]"Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF."
Cupp-Vickery J., Garcia C., Hofacre A., McGee-Estrada K.
J. Mol. Biol. 311:101-110(2001) [PubMed: 11469860] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ		X60379 Genomic DNA. Translation: CAA42927.1.
M54983 Genomic DNA. Translation: AAA26496.1.
AM420293 Genomic DNA. Translation: CAM00071.1.
PIRS18531.
RefSeqYP_001102997.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGYX-ray2.35A3-404[»]
1EUPX-ray2.10A3-404[»]
1JINX-ray2.30A3-404[»]
1JIOX-ray2.10A2-404[»]
1JIPX-ray2.00A2-404[»]
1OXAX-ray2.10A3-404[»]
1Z8OX-ray1.70A1-404[»]
1Z8PX-ray1.85A1-404[»]
1Z8QX-ray2.00A1-404[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ00441.

Genome annotation databases

GeneID4940591.
GenomeReviewsGene locus SACE_0730 in contig AM420293_GR.
KEGGsen:SACE_0730.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHBG695262.
OMALPMTVIC.
ProtClustDBCLSK644214.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
IPR017972. Cyt_P450_CS.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 2 hits.
[Graphical view]
PRINTSPR00359. BP450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...
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Entry informationHide

Entry nameCPXJ_SACEN
AccessionPrimary (citable) accession number: Q00441
Secondary accession number(s): A4F7P7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1995
Last modified: July 13, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents