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Protein

Erythromycin C-12 hydroxylase

Gene

eryK

Organism
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme.2 Publications

Catalytic activityi

Erythromycin D + NADPH + O2 = erythromycin C + NADP+ + H2O.1 Publication

Cofactori

heme b3 PublicationsNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.3 Publications

Kineticsi

kcat is 108 min(-1).

  1. KM=8.0 µM for erythromycin D1 Publication

    Pathwayi: erythromycin biosynthesis

    This protein is involved in the pathway erythromycin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway erythromycin biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811Heme
    Binding sitei85 – 851Heme
    Binding sitei278 – 2781Substrate
    Binding sitei279 – 2791Heme
    Binding sitei337 – 3371Heme
    Metal bindingi339 – 3391Iron (heme axial ligand)

    GO - Molecular functioni

    • heme binding Source: UniProtKB
    • iron ion binding Source: InterPro
    • monooxygenase activity Source: UniProtKB
    • NADP binding Source: UniProtKB
    • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Source: UniProtKB

    GO - Biological processi

    • macrolide biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17062.
    BRENDAi1.14.13.154. 5518.
    1.14.13.185. 5518.
    UniPathwayiUPA00240.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Erythromycin C-12 hydroxylase (EC:1.14.13.154)
    Alternative name(s):
    Cytochrome P450 113A1
    Short name:
    CYP113A1
    Erythromycin D C-12 hydroxylase
    Gene namesi
    Name:eryK
    Synonyms:CYP113A1
    Ordered Locus Names:SACE_0713
    OrganismiSaccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
    Taxonomic identifieri405948 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeSaccharopolyspora
    Proteomesi
    • UP000006728 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene no longer produce erythromycin A but accumulate the B and D forms of the antibiotic.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 397397Erythromycin C-12 hydroxylasePRO_0000052229Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi405948.SeryN2_010100034365.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123Combined sources
    Helixi13 – 2614Combined sources
    Beta strandi28 – 314Combined sources
    Beta strandi37 – 393Combined sources
    Helixi42 – 509Combined sources
    Turni52 – 543Combined sources
    Beta strandi55 – 573Combined sources
    Helixi59 – 624Combined sources
    Helixi73 – 753Combined sources
    Helixi80 – 9112Combined sources
    Helixi94 – 985Combined sources
    Helixi101 – 11313Combined sources
    Beta strandi117 – 1204Combined sources
    Helixi121 – 1244Combined sources
    Turni125 – 1273Combined sources
    Helixi128 – 13811Combined sources
    Helixi142 – 1443Combined sources
    Helixi151 – 1577Combined sources
    Helixi166 – 19227Combined sources
    Helixi198 – 2047Combined sources
    Beta strandi207 – 2093Combined sources
    Helixi214 – 24532Combined sources
    Helixi248 – 2558Combined sources
    Helixi257 – 2593Combined sources
    Helixi260 – 27011Combined sources
    Beta strandi276 – 2838Combined sources
    Beta strandi285 – 2873Combined sources
    Beta strandi290 – 2923Combined sources
    Beta strandi297 – 3015Combined sources
    Helixi302 – 3065Combined sources
    Turni309 – 3113Combined sources
    Beta strandi312 – 3143Combined sources
    Helixi326 – 3283Combined sources
    Helixi330 – 3323Combined sources
    Helixi342 – 36019Combined sources
    Beta strandi363 – 3653Combined sources
    Beta strandi377 – 3837Combined sources
    Beta strandi386 – 3883Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JJNX-ray1.59A1-397[»]
    2JJOX-ray1.99A1-397[»]
    2JJPX-ray2.10A1-397[»]
    2WIOX-ray2.00A2-397[»]
    2XFHX-ray1.90A2-397[»]
    3ZKPX-ray2.00A2-397[»]
    ProteinModelPortaliP48635.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48635.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni74 – 752Substrate binding

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    KOiK14370.
    OMAiPTVREMN.
    OrthoDBiPOG091H0API.

    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.

    P48635-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTIDEVPGM ADETALLDWL GTMREKQPVW QDRYGVWHVF RHADVQTVLR
    60 70 80 90 100
    DTATFSSDPT RVIEGASPTP GMIHEIDPPE HRALRKVVSS AFTPRTISDL
    110 120 130 140 150
    EPRIRDVTRS LLADAGESFD LVDVLAFPLP VTIVAELLGL PPMDHEQFGD
    160 170 180 190 200
    WSGALVDIQM DDPTDPALAE RIADVLNPLT AYLKARCAER RADPGDDLIS
    210 220 230 240 250
    RLVLAEVDGR ALDDEEAANF STALLLAGHI TTTVLLGNIV RTLDEHPAHW
    260 270 280 290 300
    DAAAEDPGRI PAIVEEVLRY RPPFPQMQRT TTKATEVAGV PIPADVMVNT
    310 320 330 340 350
    WVLSANRDSD AHDDPDRFDP SRKSGGAAQL SFGHGVHFCL GAPLARLENR
    360 370 380 390
    VALEEIIARF GRLTVDRDDE RLRHFEQIVL GTRHLPVLAG SSPRQSA
    Length:397
    Mass (Da):43,725
    Last modified:February 22, 2012 - v3
    Checksum:i0106AF77AFAC86F0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti330 – 3301L → F (PubMed:8416893).Curated
    Sequence conflicti330 – 3301L → F in AAC45584 (PubMed:9249068).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82823 Genomic DNA. Translation: AAC45584.1.
    AM420293 Genomic DNA. Translation: CAM00054.1.
    PIRiB40634.
    RefSeqiWP_009950895.1. NZ_ABFV01000120.1.

    Genome annotation databases

    EnsemblBacteriaiCAM00054; CAM00054; SACE_0713.
    KEGGisen:SACE_0713.
    PATRICi23408812. VBISacEry28377_0726.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82823 Genomic DNA. Translation: AAC45584.1.
    AM420293 Genomic DNA. Translation: CAM00054.1.
    PIRiB40634.
    RefSeqiWP_009950895.1. NZ_ABFV01000120.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JJNX-ray1.59A1-397[»]
    2JJOX-ray1.99A1-397[»]
    2JJPX-ray2.10A1-397[»]
    2WIOX-ray2.00A2-397[»]
    2XFHX-ray1.90A2-397[»]
    3ZKPX-ray2.00A2-397[»]
    ProteinModelPortaliP48635.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi405948.SeryN2_010100034365.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAM00054; CAM00054; SACE_0713.
    KEGGisen:SACE_0713.
    PATRICi23408812. VBISacEry28377_0726.

    Phylogenomic databases

    eggNOGiENOG4106A3M. Bacteria.
    COG2124. LUCA.
    HOGENOMiHOG000243678.
    KOiK14370.
    OMAiPTVREMN.
    OrthoDBiPOG091H0API.

    Enzyme and pathway databases

    UniPathwayiUPA00240.
    BioCyciMetaCyc:MONOMER-17062.
    BRENDAi1.14.13.154. 5518.
    1.14.13.185. 5518.

    Miscellaneous databases

    EvolutionaryTraceiP48635.

    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiERYK_SACEN
    AccessioniPrimary (citable) accession number: P48635
    Secondary accession number(s): A4F7N0, O33990
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 22, 2012
    Last modified: September 7, 2016
    This is version 93 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.