ID A0A270PIZ0_9PSED Unreviewed; 964 AA.
AC A0A270PIZ0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=CES87_07785 {ECO:0000313|EMBL:PAM84449.1};
OS Pseudomonas sp. ERMR1:02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1805930 {ECO:0000313|EMBL:PAM84449.1, ECO:0000313|Proteomes:UP000215719};
RN [1] {ECO:0000313|EMBL:PAM84449.1, ECO:0000313|Proteomes:UP000215719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERMR1:02 {ECO:0000313|EMBL:PAM84449.1,
RC ECO:0000313|Proteomes:UP000215719};
RA Kumar R., Acharya V., Singh D., Kumar S.;
RT "Pseudomonas sp. ERMR1:02, Genome sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAM84449.1}.
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DR EMBL; NKJI01000003; PAM84449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270PIZ0; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000215719; 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; 2.
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 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 148..237
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 107283 MW; D5B73AE8C9E88F28 CRC64;
MQTDTTRENP QGTLPQAADS NSDLSATAPG QLRVIKRNGT VVPYTDDKIT VAITKAFLAV
EGGTAAASSR IHDTVARLTE QVTATFKRRM PSGGTIHIEE IQDQVELALM RAGEQKVARD
YVIYRDGRSK ERAAHAPAEE AVNAHPSIRI TRADGTFAPL DMGRLNTIVT EACEGLEEVD
GDLIQRETLK NLYDGVALTD VNTALVMTAR TLVEREPNYS FVTARLLMDT LRAEGLGFLG
VAESATHHEM VDLYAKALPA YIAKGIEFEL LNPVLATFDL EKLGKAINHE RDQQFTYLGL
QTLYDRYFIH KDGVRFELPQ IFFMRVAMGL AIEEKHKEDR AIEFYNLLSS FDYMSSTPTL
FNAGTLRPQL SSCYLTTVPD DLSGIYHAIH DNAMLSKFAG GLGNDWTPVR ALGSYIKGTN
GKSQGVVPFL KVVNDTAVAV NQGGKRKGAV CAYLETWHMD IEEFIELRKN TGDDRRRTHD
MNTANWIPDL FMKRVFDDGP WTLFTPSEVP DLHDLTGKAF EERYEYYEAL SQYPGKIKLF
KTIQAKDLWR KMLSMLFETG HPWLTFKDPC NLRSPQQHVG VVHSSNLCTE ITLNTNKDEI
AVCNLGSINL PNHIVNGKLD TAKLERTVNT AVRMLDNVID INYYSVPQAK NSNFKHRPVG
LGIMGFQDAL YLQHIPYGSD AAVEFADKSM EAVSYFAIQA SCDLADERGA YETFQGSLWS
KGILPLDSQQ ILIEARGQKY IDVDLNETLD WAPVRARVQK GIRNSNIMAI APTATIANIT
GVSQSIEPTY QNLYVKSNLS GEFTVINPYL VRDLKARGLW DSVMINDLKY YDGSVQQIER
IPQELKELYA TAFEVDTKWI VDAASRRQKW IDQAQSLNLY IAGASGKKLD VTYRMAWYRG
LKTTYYLRAL AATSTEKSTI NTGKLNAVSS GGNHGDDSVL AAPAGPAPVP KACAIDEPDC
EACQ
//
