RIR2_CHLTR
ID RIR2_CHLTR Reviewed; 346 AA.
AC O84835;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit beta;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=nrdB; OrderedLocusNames=CT_828;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; AE001273; AAC68425.1; -; Genomic_DNA.
DR PIR; E71466; E71466.
DR RefSeq; NP_220349.1; NC_000117.1.
DR RefSeq; WP_009872214.1; NC_000117.1.
DR PDB; 1SYY; X-ray; 1.70 A; A=1-346.
DR PDB; 2ANI; X-ray; 2.00 A; A=1-346.
DR PDB; 4D8F; X-ray; 2.20 A; A/B/C/D=1-346.
DR PDB; 4D8G; X-ray; 1.75 A; A/B/C/D=1-346.
DR PDB; 4M1H; X-ray; 1.70 A; A/B/C/D=1-346.
DR PDB; 4M1I; X-ray; 1.80 A; A/B/C/D=1-346.
DR PDBsum; 1SYY; -.
DR PDBsum; 2ANI; -.
DR PDBsum; 4D8F; -.
DR PDBsum; 4D8G; -.
DR PDBsum; 4M1H; -.
DR PDBsum; 4M1I; -.
DR AlphaFoldDB; O84835; -.
DR SMR; O84835; -.
DR STRING; 813.O172_04625; -.
DR EnsemblBacteria; AAC68425; AAC68425; CT_828.
DR GeneID; 884627; -.
DR KEGG; ctr:CT_828; -.
DR PATRIC; fig|272561.5.peg.914; -.
DR HOGENOM; CLU_035339_1_1_0; -.
DR InParanoid; O84835; -.
DR OMA; KVGEYQR; -.
DR BioCyc; MetaCyc:MON-15784; -.
DR BRENDA; 1.17.4.1; 1315.
DR UniPathway; UPA00326; -.
DR EvolutionaryTrace; O84835; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deoxyribonucleotide synthesis; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..346
FT /note="Ribonucleoside-diphosphate reductase subunit beta"
FT /id="PRO_0000190475"
FT ACT_SITE 129
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4M1H"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 72..98
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 107..134
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4M1H"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1SYY"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 214..244
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 251..275
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:4M1H"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:4M1H"
SQ SEQUENCE 346 AA; 40516 MW; C0ED2D7D76238F9F CRC64;
MQADILDGKQ KRVNLNSKRL VNCNQVDVNQ LVPIKYKWAW EHYLNGCANN WLPTEIPMGK
DIELWKSDRL SEDERRVILL NLGFFSTAES LVGNNIVLAI FKHVTNPEAR QYLLRQAFEE
AVHTHTFLYI CESLGLDEKE IFNAYNERAA IKAKDDFQME ITGKVLDPNF RTDSVEGLQE
FVKNLVGYYI IMEGIFFYSG FVMILSFHRQ NKMIGIGEQY QYILRDETIH LNFGIDLING
IKEENPEIWT PELQQEIVEL IKRAVDLEIE YAQDCLPRGI LGLRASMFID YVQHIADRRL
ERIGLKPIYH TKNPFPWMSE TIDLNKEKNF FETRVIEYQH AASLTW
