ID A0A0C1JXB0_9BACT Unreviewed; 780 AA.
AC A0A0C1JXB0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN Name=rnr1 {ECO:0000313|EMBL:KIC75046.1};
GN ORFNames=DB42_AQ00260 {ECO:0000313|EMBL:KIC75046.1};
OS Neochlamydia sp. EPS4.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478175 {ECO:0000313|EMBL:KIC75046.1, ECO:0000313|Proteomes:UP000031344};
RN [1] {ECO:0000313|EMBL:KIC75046.1, ECO:0000313|Proteomes:UP000031344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS4 {ECO:0000313|EMBL:KIC75046.1,
RC ECO:0000313|Proteomes:UP000031344};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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 Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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:KIC75046.1}.
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DR EMBL; JSDQ01000041; KIC75046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1JXB0; -.
DR STRING; 1478175.DB42_AQ00260; -.
DR PATRIC; fig|1478175.3.peg.868; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000031344; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 9..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 780 AA; 87944 MW; 5E9AA9F353DA9AC5 CRC64;
MKNFEGGGMF VIKRDGRKEA MKFDKITARL QKLCYALDAK HINPVLVARR VIEGVFDGVT
TSELDNLAAE VAATLTANHP DYAILAARIS ISNLHKNTNK SFSETIKALY LYVDPKSGKH
APLIAEDVYE IIQQHAELLD STLIYDRDFL YDYFGFKTLE KAYLLKMQGK VVERPQHMLM
RVAIGIHKGD IEPAMETYHL MSDRWFTQAT PTLFNAGTPT PQLSSCFLLQ MKEDSIDGIF
DTLKQCAKIS RAAGGIGLSI HGIRATGSYI RGTGGISNGV IPMLKVFNDT ARYVDQGGGK
RKGSFAVYLE PWHADIFEFL DLRKNQGKDE MRARDLFTAL WIPDLFMQRV EANQDWSLFC
PNEAAGLDAC WGDEFEKLYK QYEKEGRARR VIKAQELWFK ILEAQIETGS PYMVYKDACN
RKSNQQHLGT IQSSNLCTEI VEYTAPGEVA VCNLASLALP RFIKDGQFDY PKLFEVTQVV
TRNLNKIIDV NYYPVAEAEY SNLRHRPIGI GVQGLADAFL ILKMPFESQE AKQLNREIFE
TIYFAALTAS KDLAKIHGPY STYEGSPMSK GIFQYDMWNV VPGKRWDWPS LKAEVALYGV
RNSLLVAPMP TASTSQILGN NECFEPYTSN LYTRRVLSGE FIVVNKHLLK DLIHLGLWGE
ELKNQLIAAN GSVQSIKEIP ENIKQLYKTA WEIKQKTLVE MAAERGPFIC QSQSLNLFVK
NPTFAKLTSM HFYGWKCGLK TGMYYLRTQA AVDAIKFTLE AKPFAACSAN NKEECLACSA
//
