Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00441

- CPXJ_SACEN

UniProt

Q00441 - CPXJ_SACEN

Protein

6-deoxyerythronolide B hydroxylase

Gene

eryF

Organism
Saccharopolyspora erythraea (strain NRRL 23338)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Cofactori

    Heme group.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi351 – 3511Iron (heme axial ligand)

    GO - Molecular functioni

    1. heme binding Source: InterPro
    2. iron ion binding Source: InterPro
    3. monooxygenase activity Source: UniProtKB-KW
    4. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Source: InterPro

    GO - Biological processi

    1. antibiotic biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00240.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-deoxyerythronolide B hydroxylase (EC:1.14.-.-)
    Short name:
    6-DEB hydroxylase
    Alternative name(s):
    CYPCVIIA1
    Cytochrome P450 107A1
    Cytochrome P450eryF
    Erythromycin A biosynthesis hydrolase
    Gene namesi
    Name:eryF
    Synonyms:CYP107A1
    Ordered Locus Names:SACE_0730
    OrganismiSaccharopolyspora erythraea (strain NRRL 23338)
    Taxonomic identifieri405948 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora
    ProteomesiUP000006728: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4044046-deoxyerythronolide B hydroxylasePRO_0000052220Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi405948.SACE_0730.

    Structurei

    Secondary structure

    1
    404
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 123
    Helixi16 – 2611
    Beta strandi28 – 347
    Beta strandi37 – 426
    Helixi45 – 539
    Helixi73 – 753
    Helixi80 – 867
    Beta strandi87 – 893
    Helixi90 – 923
    Helixi97 – 10610
    Helixi111 – 1166
    Helixi118 – 13013
    Beta strandi134 – 1396
    Helixi140 – 1434
    Turni144 – 1463
    Helixi147 – 15610
    Helixi161 – 1633
    Turni164 – 1663
    Helixi167 – 1759
    Helixi179 – 1813
    Helixi182 – 20524
    Helixi211 – 2177
    Turni221 – 2233
    Helixi228 – 25932
    Helixi261 – 2699
    Helixi271 – 2733
    Helixi274 – 28411
    Beta strandi291 – 2977
    Beta strandi299 – 3013
    Beta strandi304 – 3063
    Beta strandi311 – 3144
    Helixi316 – 3194
    Turni323 – 3253
    Beta strandi326 – 3283
    Beta strandi334 – 3363
    Beta strandi342 – 3443
    Helixi347 – 3493
    Helixi354 – 37118
    Beta strandi376 – 3794
    Helixi381 – 3833
    Beta strandi390 – 3923
    Beta strandi399 – 4013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ00441.
    SMRiQ00441. Positions 2-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00441.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000243678.
    KOiK14366.
    OMAiIKVICEL.
    OrthoDBiEOG6JB11P.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q00441-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTVPDLESD SFHVDWYRTY AELRETAPVT PVRFLGQDAW LVTGYDEAKA    50
    ALSDLRLSSD PKKKYPGVEV EFPAYLGFPE DVRNYFATNM GTSDPPTHTR 100
    LRKLVSQEFT VRRVEAMRPR VEQITAELLD EVGDSGVVDI VDRFAHPLPI 150
    KVICELLGVD EKYRGEFGRW SSEILVMDPE RAEQRGQAAR EVVNFILDLV 200
    ERRRTEPGDD LLSALIRVQD DDDGRLSADE LTSIALVLLL AGFEASVSLI 250
    GIGTYLLLTH PDQLALVRRD PSALPNAVEE ILRYIAPPET TTRFAAEEVE 300
    IGGVAIPQYS TVLVANGAAN RDPKQFPDPH RFDVTRDTRG HLSFGQGIHF 350
    CMGRPLAKLE GEVALRALFG RFPALSLGID ADDVVWRRSL LLRGIDHLPV 400
    RLDG 404
    Length:404
    Mass (Da):45,099
    Last modified:February 1, 1995 - v2
    Checksum:i257ABEFC2D88B3FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611P → PDQ in CAA42927. (PubMed:1840640)Curated
    Sequence conflicti302 – 3021G → R in CAA42927. (PubMed:1840640)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60379 Genomic DNA. Translation: CAA42927.1.
    M54983 Genomic DNA. Translation: AAA26496.1.
    AM420293 Genomic DNA. Translation: CAM00071.1.
    PIRiS18531.
    RefSeqiYP_001102997.1. NC_009142.1.

    Genome annotation databases

    EnsemblBacteriaiCAM00071; CAM00071; SACE_0730.
    GeneIDi4940591.
    KEGGisen:SACE_0730.
    PATRICi23408848. VBISacEry28377_0744.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60379 Genomic DNA. Translation: CAA42927.1 .
    M54983 Genomic DNA. Translation: AAA26496.1 .
    AM420293 Genomic DNA. Translation: CAM00071.1 .
    PIRi S18531.
    RefSeqi YP_001102997.1. NC_009142.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EGY X-ray 2.35 A 3-404 [» ]
    1EUP X-ray 2.10 A 3-404 [» ]
    1JIN X-ray 2.30 A 3-404 [» ]
    1JIO X-ray 2.10 A 2-404 [» ]
    1JIP X-ray 2.00 A 2-404 [» ]
    1OXA X-ray 2.10 A 3-404 [» ]
    1Z8O X-ray 1.70 A 1-404 [» ]
    1Z8P X-ray 1.85 A 1-404 [» ]
    1Z8Q X-ray 2.00 A 1-404 [» ]
    ProteinModelPortali Q00441.
    SMRi Q00441. Positions 2-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405948.SACE_0730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM00071 ; CAM00071 ; SACE_0730 .
    GeneIDi 4940591.
    KEGGi sen:SACE_0730.
    PATRICi 23408848. VBISacEry28377_0744.

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000243678.
    KOi K14366.
    OMAi IKVICEL.
    OrthoDBi EOG6JB11P.

    Enzyme and pathway databases

    UniPathwayi UPA00240 .

    Miscellaneous databases

    EvolutionaryTracei Q00441.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00359. BP450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NRRL 23338.
    4. "Structure of cytochrome P450eryF involved in erythromycin biosynthesis."
      Cupp-Vickery J.L., Poulos T.L.
      Nat. Struct. Biol. 2:144-153(1995) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiCPXJ_SACEN
    AccessioniPrimary (citable) accession number: Q00441
    Secondary accession number(s): A4F7P7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3