(data stored in SCRATCH zone)

SWISSPROT: RIR2H_SACEN

ID   RIR2H_SACEN             Reviewed;         317 AA.
AC   A4F7B2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 78.
DE   RecName: Full=R2-like ligand binding oxidase;
DE            EC=1.-.-.-;
DE   AltName: Full=Ribonucleotide reductase R2 subunit homolog;
DE   AltName: Full=Ribonucleotide reductase small subunit homolog;
GN   OrderedLocusNames=SACE_0591;
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 [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).
CC   -!- FUNCTION: Probable oxidase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per subunit.;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 manganese ion per subunit. The iron and manganese ions
CC       form a dinuclear manganese-iron cluster. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. R2-like ligand binding oxidase subfamily. {ECO:0000305}.
DR   EMBL; AM420293; CAL99936.1; -; Genomic_DNA.
DR   RefSeq; WP_009945174.1; NZ_PDBV01000001.1.
DR   SMR; A4F7B2; -.
DR   STRING; 405948.SACE_0591; -.
DR   EnsemblBacteria; CAL99936; CAL99936; SACE_0591.
DR   KEGG; sen:SACE_0591; -.
DR   eggNOG; ENOG4108CCU; Bacteria.
DR   eggNOG; COG0208; LUCA.
DR   HOGENOM; HOG000220940; -.
DR   KO; K00526; -.
DR   OMA; GNAKFWN; -.
DR   OrthoDB; 1384440at2; -.
DR   BioCyc; SERY405948:SACE_RS02905-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd07911; RNRR2_Rv0233_like; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR033908; R2LOX.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; PTHR23409; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F7B2.
DR   SWISS-2DPAGE; A4F7B2.
KW   Iron; Manganese; Metal-binding; Oxidoreductase; Reference proteome.
FT   CHAIN           1..317
FT                   /note="R2-like ligand binding oxidase"
FT                   /id="PRO_0000375436"
FT   METAL           73
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           106
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           106
FT                   /note="Manganese"
FT                   /evidence="ECO:0000250"
FT   METAL           109
FT                   /note="Manganese; via pros nitrogen"
FT                   /evidence="ECO:0000250"
FT   METAL           172
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           207
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           210
FT                   /note="Iron; via pros nitrogen"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        76..167
FT                   /note="3-(O4'-tyrosyl)-valine (Val-Tyr)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  35737 MW;  93A95EB109A59038 CRC64;
     MTSTATFRED FHSLRAGGLN WDSLPLRLFG KGNAKFWDPA DIDFTRDAED WQGLTEEERR
     SVAMLCSQFI AGEEAVTQDL QPFMAAMAAE GRFGDEMYLT QFCFEEAKHT QVFRLWMDAV
     GLTGDLHSHV AENPGYRAIF YEELPRSLNA LHDDPSPANQ VRASVTYNHV VEGTLALTGY
     FAWQKICRSR GILPGMQEVV RRIGDDERRH MAWGTFTCRR HVAADESNWD VVQEQMQHLL
     PLAVTQIQWR PEDAPEETPF RLDIDELAAY ASDRAGRRLG AISAARGVPV EQIDVDASPE
     QLEDQFGVED AAALEKA
//

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