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Database: UniProt
Entry: U2J1X4_9SPHI
LinkDB: U2J1X4_9SPHI
Original site: U2J1X4_9SPHI 
ID   U2J1X4_9SPHI            Unreviewed;       323 AA.
AC   U2J1X4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=M472_09285 {ECO:0000313|EMBL:ERJ58964.1};
OS   Sphingobacterium paucimobilis HER1398.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ58964.1, ECO:0000313|Proteomes:UP000016584};
RN   [1] {ECO:0000313|EMBL:ERJ58964.1, ECO:0000313|Proteomes:UP000016584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HER1398 {ECO:0000313|EMBL:ERJ58964.1,
RC   ECO:0000313|Proteomes:UP000016584};
RX   PubMed=23929486;
RA   White R.A.III., Suttle C.A.;
RT   "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT   (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT   Member of the Genus Sphingobacterium (Bacteroidetes).";
RL   Genome Announc. 1:e00598-13(2013).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family. {ECO:0000256|ARBA:ARBA00009303}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERJ58964.1}.
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DR   EMBL; ATDL01000015; ERJ58964.1; -; Genomic_DNA.
DR   RefSeq; WP_021070457.1; NZ_ATDL01000015.1.
DR   AlphaFoldDB; U2J1X4; -.
DR   STRING; 1346330.M472_09285; -.
DR   PATRIC; fig|1346330.5.peg.2297; -.
DR   eggNOG; COG0208; Bacteria.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000016584; Unassembled WGS sequence.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01049; RNRR2; 1.
DR   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR033909; RNR_small.
DR   InterPro; IPR030475; RNR_small_AS.
DR   InterPro; IPR000358; RNR_small_fam.
DR   PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR   PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR   Pfam; PF00268; Ribonuc_red_sm; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00368; RIBORED_SMALL; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016584}.
SQ   SEQUENCE   323 AA;  37614 MW;  0B3203B94B80ADAF CRC64;
     MMEPILQENK DRFVIFPIEH DDIWQFYKMA EASFWTAEEV DLSPDINDWH HKLTEDERYF
     ITHVLAFFAA SDGIVNENLA INFINEVQYP EARFFYGFQI MIENIHSEMY SLLIDTYVKD
     PKEKDYLLRA METIPCVQRK ADWALRWIES GSFSERLVAF AAVEGIFFSG SFCAIFWLKK
     RGLMPGLTFS NELISRDEGL HCDFACHLYN SHVENRLPTE TLRNIIQNAV AIEKEFVTEA
     LPVRLIGMNA ELMCQYIEFV ADRLLVALGE QKIWNAVNPF DFMELISLQG KTNFFERRVG
     EYQKPGVSKG NGDGRLFSLD EEF
//
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