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Database: UniProt
Entry: Q6MBH6_PARUW
LinkDB: Q6MBH6_PARUW
Original site: Q6MBH6_PARUW 
ID   Q6MBH6_PARUW            Unreviewed;       323 AA.
AC   Q6MBH6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN   ORFNames=PC_RS06490 {ECO:0000313|EMBL:CAF24073.1};
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Protochlamydia.
OX   NCBI_TaxID=264201 {ECO:0000313|EMBL:CAF24073.1, ECO:0000313|Proteomes:UP000000529};
RN   [1] {ECO:0000313|EMBL:CAF24073.1, ECO:0000313|Proteomes:UP000000529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25 {ECO:0000313|EMBL:CAF24073.1,
RC   ECO:0000313|Proteomes:UP000000529};
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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}.
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DR   EMBL; BX908798; CAF24073.1; -; Genomic_DNA.
DR   RefSeq; WP_011175898.1; NC_005861.2.
DR   AlphaFoldDB; Q6MBH6; -.
DR   STRING; 264201.pc1349; -.
DR   KEGG; pcu:PC_RS06490; -.
DR   eggNOG; COG0208; Bacteria.
DR   HOGENOM; CLU_035339_2_2_0; -.
DR   OrthoDB; 9766544at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000529; Chromosome.
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:UP000000529}.
SQ   SEQUENCE   323 AA;  37297 MW;  5138B17757D05C9A CRC64;
     MQVTEPILRE NKDRFVLFPI NHAEIWQMYK KAEASFWTAE EIDLTSDLLD WDRKLNNDEK
     YFIKHILAFF AASDGIVNEN LAVNFMSEVQ YPEARCFYGF QIMMENIHSE AYSLLIDTYI
     KDPTDKNRLF KALETIPCIS NKADWALRWI SQGSFSERLV AFAAVEGIFF SGSFCSIFWL
     KKRGLMPGLS FANELISRDE GLHCDFACLL YSQLNNKLPL ETLQAIISHA VAIEKEFVQD
     ALPVRLIGMN ATLMCQYIEF VADRLLVALG SPKLYNVDNP FDFMDLISMP GKTNFFERRV
     SEYQKSGVMS TKENHVFTIH EDF
//
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