ID A0A344L1S2_9PSEU Unreviewed; 1001 AA.
AC A0A344L1S2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=A4R43_05185 {ECO:0000313|EMBL:AXB41996.1};
OS Amycolatopsis albispora.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB41996.1, ECO:0000313|Proteomes:UP000250434};
RN [1] {ECO:0000313|EMBL:AXB41996.1, ECO:0000313|Proteomes:UP000250434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:AXB41996.1,
RC ECO:0000313|Proteomes:UP000250434};
RA Wang H., Chen S., Wu Q.;
RT "Complete genome sequence and analysis of deep-sea sediment isolate,
RT Amycolatopsis sp. WP1.";
RL Submitted (APR-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015163; AXB41996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344L1S2; -.
DR KEGG; aab:A4R43_05185; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000250434; Chromosome.
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 22..122
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 137..226
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 907..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 110991 MW; 210711AA97D69C1A CRC64;
MSLDITETSQ RPPSVTEKTA TVRVIRRDGS VSPFDANKIS VAMTKAFLAV EGDDAAASSR
IHHLVAELTE QVEQSLLRHA GPETALHIEQ IQDQVELMLM RGEHHKVARA YVLYRDERAK
ARAAAEAASP ARDENVLHVK SADGVLRPLD WDRVAHVVGE AVAGLSDVSS EPVLTETRRN
LYDGISADEL ALAQIMAART LVEQEPNYSY VSARLLADKL RAEALSYLAG RPRQASQDEM
AGIYPGYFRD YLRRAIELEL VNPELAQFDL DRITAALRPE RDLDFGFLGL QTLYDRYFQH
HNGTRFELPQ AFFMRVAMGL AIREDDREAR AIEFYELLSS FHFMASTPTL FNSGTTRPQL
SSCFLTTVDD DLDSIFQAYK NNALLAKYSG GLGNDWTPVR GLGAHIKGTN GQSQGVVPFL
KIANDTAVAV NQGGKRKGAA CAYLETWHVD IEEFLDLRKN TGDDRRRTHD MNTANWVPDE
FLRRVEANEG WTLFSPNEVP DLHDLYGNAF AERYREYEAA AERGEIKVFR KVRAVDLWRR
MLTMLFETGH PWITFKDPCN LRSPQQHTGV VHSSNLCTEI TLNTSADEVA VCNLGSVNLL
KHVGPDGLDT ARLEKTVRTA VRMLDNVIDI NFYTIPEARR SNLRHRPIGL GLMGFQDALF
ELGLPLSSEA AVEFADRSME YISYYAISAS TDLAEERGQY QTFEGSLWSK GILPIDSMQL
LIDARRGDAL DVDTSSTLDW EPLRQRVRTV GMRNSNVMAI APTATISNIC GVGQSIEPLF
QNLFVKSNMS GDFTVVNPHL VRSLKERGLW DEVMVSDLKY FDGSLGQIDR VPDDLKALYA
TAFEVESKWL VDAASRRQKW IDQAQSLNLY IAAPSGRKLD ELYRYAWHKG LKTTYYLRAQ
SATHVEKSTL RGTDGKLNAV SATPAPAASP SPSPAPSPSP SPSPSPSPSA AVPATPSAVV
PAVPPAPVVK PKELPKVDDV DFAATDGAAC RIDDPDCEAC Q
//