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 03-AUG-2022, entry version 84.
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}.
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DR EMBL; AM420293; CAL99936.1; -; Genomic_DNA.
DR RefSeq; WP_009945174.1; NZ_PDBV01000001.1.
DR PDB; 7QBP; X-ray; 1.38 A; A=2-317.
DR PDBsum; 7QBP; -.
DR AlphaFoldDB; A4F7B2; -.
DR SMR; A4F7B2; -.
DR STRING; 405948.SACE_0591; -.
DR EnsemblBacteria; CAL99936; CAL99936; SACE_0591.
DR KEGG; sen:SACE_0591; -.
DR eggNOG; COG0208; Bacteria.
DR HOGENOM; CLU_072736_0_0_11; -.
DR OMA; GNAKFWN; -.
DR OrthoDB; 1384440at2; -.
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 1: Evidence at protein level;
KW 3D-structure; Iron; Manganese; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..317
FT /note="R2-like ligand binding oxidase"
FT /id="PRO_0000375436"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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