ID A0A133YAJ6_9FIRM Unreviewed; 720 AA.
AC A0A133YAJ6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=HMPREF1872_01041 {ECO:0000313|EMBL:KXB40229.1};
OS Amygdalobacter nucleatus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Amygdalobacter.
OX NCBI_TaxID=3029274 {ECO:0000313|EMBL:KXB40229.1, ECO:0000313|Proteomes:UP000070080};
RN [1] {ECO:0000313|Proteomes:UP000070080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00274 {ECO:0000313|Proteomes:UP000070080};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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 -!- 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:KXB40229.1}.
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DR EMBL; LSCV01000031; KXB40229.1; -; Genomic_DNA.
DR RefSeq; WP_066714475.1; NZ_KQ959588.1.
DR AlphaFoldDB; A0A133YAJ6; -.
DR STRING; 1497955.HMPREF1872_01041; -.
DR PATRIC; fig|1497955.3.peg.1011; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000070080; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000070080}.
FT DOMAIN 561..583
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 720 AA; 80374 MW; 64BA2B5D4D42B1E2 CRC64;
MNNQHKEAYI SLNALTQFKD QHGHYHFDAD KEAVKLYMQA QIMPKLLKFK DIPAKLTYLV
ENNYYDEIVL AQYKFDFVVE LFQKAADFNF TFPSLMGAMK FYQSYALMTD DKQNYLETFA
DRACMNALFL GHGDAQLASC LLDDILHKRL QPATPTFLNA GKKRRGEFVS CYLLRLEDNM
ESIARGISTS LQLSKRGGGV ALCLTNLRES GAPIKGIVNQ SSGVVPVMKL LEDSFSYANQ
LGQRQGAGAV YLNVHHPDIL QFLDTKRENA DEKIRIKSLS LGVVIPDITF ELAKANKDMA
LFSPYDVERE YGKPMSDISI TDEYANLLAN PRIKKTYTSA RKLFQTIAEL HFESGYPYIL
FEDSANLRNP LKKVGRIIMS NLCSEIAQVN TASAYSEDLT FTKVGEDVCC NLASLNIAKV
MEAAPQFAEI VEHAIYGLNL VSRASDLACA PSVQKGNLGN HALGLGAMNL HGFLAENHIF
YDTEEAVDFT DIFFFCLAYH AFSASNKLAQ KVGPFANFAL SEYADGTYFQ KYLNEDKQPK
TAKVKELIKK YQLKLPTASD WRNLVERIKQ SGLANAHLLA VAPTGSISYL SSCTPSLQAV
VSPVEVRKEG KLGRVYVPAY KISADNYAYY QKGAYEVGPN ALIDIAAAAQ KHVDQAISLT
LFMTSEATTR DLNKAYIYAF KKGLSSIYYV RIRQEVLEGS EHLAEDALIS NLNECESCMI
//
