ERYC2_SACEN
ID ERYC2_SACEN Reviewed; 361 AA.
AC A4F7P2; O33934; O54225;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cytochrome P450 family protein EryCII;
DE AltName: Full=Erythromycin biosynthesis protein CII;
GN Name=eryCII; OrderedLocusNames=SACE_0725;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=9353926; DOI=10.1099/00221287-143-10-3251;
RA Summers R.G., Donadio S., Staver M.J., Wendt-Pienkowski E.,
RA Hutchinson C.R., Katz L.;
RT "Sequencing and mutagenesis of genes from the erythromycin biosynthetic
RT gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose
RT and D-desosamine production.";
RL Microbiology 143:3251-3262(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=9563840; DOI=10.1007/s004380050680;
RA Salah-Bey K., Doumith M., Michel J.M., Haydock S., Cortes J., Leadlay P.F.,
RA Raynal M.C.;
RT "Targeted gene inactivation for the elucidation of deoxysugar biosynthesis
RT in the erythromycin producer Saccharopolyspora erythraea.";
RL Mol. Gen. Genet. 257:542-553(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) IN COMPLEX WITH ERYCIII, SUBUNIT,
RP AND FUNCTION.
RX PubMed=22056329; DOI=10.1016/j.jmb.2011.10.036;
RA Moncrieffe M.C., Fernandez M.J., Spiteller D., Matsumura H., Gay N.J.,
RA Luisi B.F., Leadlay P.F.;
RT "Structure of the glycosyltransferase EryCIII in complex with its
RT activating P450 homologue EryCII.";
RL J. Mol. Biol. 415:92-101(2012).
CC -!- FUNCTION: Involved in the erythromycin biosynthesis pathway. Acts by
CC forming a complex and stabilizing the desosaminyl transferase EryCIII.
CC {ECO:0000269|PubMed:22056329}.
CC -!- PATHWAY: Antibiotic biosynthesis; erythromycin biosynthesis.
CC -!- SUBUNIT: Heterotetramer composed of EryCII and EryCIII.
CC {ECO:0000269|PubMed:22056329}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- CAUTION: Although related to the cytochrome P450 family, lacks the
CC heme-binding sites. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U77454; AAB84066.1; -; Genomic_DNA.
DR EMBL; Y14332; CAA74711.1; -; Genomic_DNA.
DR EMBL; AM420293; CAM00066.1; -; Genomic_DNA.
DR PIR; S14161; S14161.
DR RefSeq; WP_009950404.1; NZ_PDBV01000001.1.
DR PDB; 2YJN; X-ray; 3.09 A; B=1-361.
DR PDBsum; 2YJN; -.
DR AlphaFoldDB; A4F7P2; -.
DR SMR; A4F7P2; -.
DR STRING; 405948.SACE_0725; -.
DR EnsemblBacteria; CAM00066; CAM00066; SACE_0725.
DR KEGG; sen:SACE_0725; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_764250_0_0_11; -.
DR OrthoDB; 1813126at2; -.
DR BioCyc; MetaCyc:MON-18408; -.
DR UniPathway; UPA00240; -.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Reference proteome.
FT CHAIN 1..361
FT /note="Cytochrome P450 family protein EryCII"
FT /id="PRO_0000418494"
FT CONFLICT 56
FT /note="Missing (in Ref. 1; AAB84066)"
FT /evidence="ECO:0000305"
FT HELIX 3..26
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 196..220
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 314..328
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 329..332
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:2YJN"
SQ SEQUENCE 361 AA; 38507 MW; FE6C52955CC966B3 CRC64;
MTTTDRAGLG RQLQMIRGLH WGYGSNGDPY PMLLCGHDDD PQRRYRSMRE SGVRRSRTET
WVVADHATAR QVLDDPAFTR ATGRTPEWMR AAGAPPAEWA QPFRDVHAAS WEGEVPDVGE
LAESFAGLLP GAGARLDLVG DFAWQVPVQG MTAVLGAAGV LRGAAWDARV SLDAQLSPQQ
LAVTEAAVAA LPADPALRAL FAGAEMTANT VVDAVLAVSA EPGLAERIAD DPAAAQRTVA
EVLRLHPALH LERRTATAEV RLGEHVIGEG EEVVVVVAAA NRDPEVFAEP DRLDVDRPDA
DRALSAHRGH PGRLEELVTA LATAALRAAA KALPGLTPSG PVVRRRRSPV LRGTNRCPVE
L
