(data stored in SCRATCH zone)

SWISSPROT: A4F651_SACEN

ID   A4F651_SACEN            Unreviewed;       469 AA.
AC   A4F651;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 65.
DE   RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN   OrderedLocusNames=SACE_0173 {ECO:0000313|EMBL:CAL99525.1};
GN   ORFNames=A8924_0559 {ECO:0000313|EMBL:PFG93325.1};
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 {ECO:0000313|EMBL:CAL99525.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99525.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99525.1};
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   [2] {ECO:0000313|EMBL:PFG93325.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93325.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|RuleBase:RU364048};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU364048};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|RuleBase:RU364048}.
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DR   EMBL; AM420293; CAL99525.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93325.1; -; Genomic_DNA.
DR   RefSeq; WP_009944947.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0173; -.
DR   EnsemblBacteria; CAL99525; CAL99525; SACE_0173.
DR   KEGG; sen:SACE_0173; -.
DR   eggNOG; ENOG4105ZTI; Bacteria.
DR   eggNOG; COG3670; LUCA.
DR   HOGENOM; HOG000254835; -.
DR   OMA; WTTAHPK; -.
DR   OrthoDB; 389495at2; -.
DR   BioCyc; SERY405948:SACE_RS00820-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; PTHR10543; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F651.
DR   SWISS-2DPAGE; A4F651.
KW   Dioxygenase {ECO:0000256|RuleBase:RU364048, ECO:0000313|EMBL:CAL99525.1};
KW   Iron {ECO:0000256|RuleBase:RU364048};
KW   Metal-binding {ECO:0000256|RuleBase:RU364048};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364048,
KW   ECO:0000313|EMBL:CAL99525.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
SQ   SEQUENCE   469 AA;  51427 MW;  5AD178B372A5AE6C CRC64;
     MTEVAEAASS APPVHLVGHL EPVPDEVEVH DLRVTGTLPR ELAGRYLRNG PNPLPGENPG
     HWFAGHGMVH GIRIRDGRAE WYRNRWVRTN LLEGRFEAGD GATLDRSVTP ANTHVIEHSG
     HLLALCEGGL PYELTAGLDT EGPRAFDGRL TNGMTAHPKE DPDTGELHFF GCGFRPPHLT
     YHRLSPAGEL VRSQVVEVPG ATMMHDFAIT ENHVIWLDLP VTFDLDLVGR ALPYRWNDDY
     GARLGVMARD GEPTVRWFEI DPCYVFHVGN AREDPAGRIV LDAVRWDRDT FRRGWSRLGG
     DGRARRDGGP AAEFSGTGRS TLHRWIFDLA SGSVREQAID DRGVEFPTLN ENRVGRDNRY
     LYTVAEQLDD SNTGAAIVKY DTATGIGETH ELGADRTAGE AVFVAAAGGR DEDDGWLLSI
     VSDRSGKSSD LVVLDATDLT AAPVATVHLP RRVPTGFHGS WIPDAELDA
//

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