ID I6AVZ3_9BACT Unreviewed; 1110 AA.
AC I6AVZ3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=OpiT1DRAFT_03694 {ECO:0000313|EMBL:EIP99184.1};
OS Opitutaceae bacterium TAV1.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278956 {ECO:0000313|EMBL:EIP99184.1, ECO:0000313|Proteomes:UP000004921};
RN [1] {ECO:0000313|EMBL:EIP99184.1, ECO:0000313|Proteomes:UP000004921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV1 {ECO:0000313|EMBL:EIP99184.1,
RC ECO:0000313|Proteomes:UP000004921};
RX PubMed=22535930; DOI=10.1128/JB.00264-12;
RA Isanapong J., Goodwin L., Bruce D., Chen A., Detter C., Han J., Han C.S.,
RA Held B., Huntemann M., Ivanova N., Land M.L., Mavromatis K., Nolan M.,
RA Pati A., Pennacchio L., Pitluck S., Szeto E., Tapia R., Woyke T.,
RA Rodrigues J.L.;
RT "High-Quality Draft Genome Sequence of the Opitutaceae Bacterium Strain
RT TAV1, a Symbiont of the Wood-Feeding Termite Reticulitermes flavipes.";
RL J. Bacteriol. 194:2744-2745(2012).
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}.
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DR EMBL; JH660698; EIP99184.1; -; Genomic_DNA.
DR AlphaFoldDB; I6AVZ3; -.
DR HOGENOM; CLU_000404_3_0_0; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004921; 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 164..254
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 280..370
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 1110 AA; 124310 MW; 71ACB6528759281D CRC64;
MNTSATASSS TRALAHDLAL KRATHAPVEQ KPSHNWRDCV PADTPLLPEI LLLTPAGETP
LDLGEIADTL GKALTNVHLA RGDTGNIFTP STRDFVGRII REAAGNLASA ALKTAPLRLS
LNDLYELIEK TLVDNNAYDI AKSVLLHRSR KLGSTGATTA QTATRVIRRN RQVVPFIPQK
IEVAIRKAFL SLQRDSSPAI DITRAVSDRV LGSRQAFIHI EEIQDIVQEE LMKTGHYKVA
EAYILYRALR SETRSAEPPA DSGSSAALPA SAADTSATMI VVQQPDGSTT LWDRTDLRLR
IEFARIGLDL CLTSDEIETE LTRSLFDQIT RKDLDQTIIL NSKTLIERDA DFAKFAGRIQ
LTYIYEEVLG WDIVRDGIGK LKTFHQAAFK KHLAHGAAIK RINPRLLDYD LEKLAAALDP
SADLELDFLG IQTLYDRYLI VDKTQKPSRR LETPQLFWMR VAMGLFLNDG DEKTGQREQR
IVSLYELYKS RRFCSSTPTL FNSGTLHSQL SSCYLYYVDD SLEGIMYRGI AENAQLSKWA
GGLGGSWTAV RGTGAHIAGT NGESQGVIPF LKLHNDQLNA VNQGGKRKGS GCAYLETWHN
DIFEFLELRK NTGDDRRRTH DMNTANWIPD LFMKRMEARE HWTLFRSNEA PDLHELYGRK
FEEAYLRYEK LAEEGKITGQ RIEALELWKK MLSMLFETGH PWITFKDACN LRSPQDHVGV
IHSSNLCTEI TLNTSNDETA VCNLGSIILE THLRPDGSID HDKLRDTIRT AVRALDNVID
INFYPTKPAE TSNRRHRPIG LGVMGLANSL YLRGHAFASP EAVEFNDEAM EAIAYYAYEA
SSDLAAERGA YSTYKGSKWD RGILPQDTVD LLEQERGVPV EVPRGGKLDW TPLRAKIARQ
GMRNSNVLAI APTATISNIT ATSPCIEPTY KNLFVKSNLS GEFIVLNPYL VRDLKARGLW
NQEMIDNLKY FDGELRDIDT IPADLKEKYR TAFGIDHKWV IDAAARRQKW IDQSQSVNLW
LETPDLKTLS HMYRHAWHVG LKTTYYLRTL GASNIEKATV SVKKEMRGVS PGVATATTSD
AATQRTYTAE QKLACSIEAM RNGGECEACQ
//
