ID A0A086ZHD6_9BIFI Unreviewed; 728 AA.
AC A0A086ZHD6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=BBOH_0743 {ECO:0000313|EMBL:KFI45936.1};
OS Bifidobacterium bohemicum DSM 22767.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437606 {ECO:0000313|EMBL:KFI45936.1, ECO:0000313|Proteomes:UP000029096};
RN [1] {ECO:0000313|EMBL:KFI45936.1, ECO:0000313|Proteomes:UP000029096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22767 {ECO:0000313|EMBL:KFI45936.1,
RC ECO:0000313|Proteomes:UP000029096};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI45936.1}.
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DR EMBL; JGYP01000002; KFI45936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086ZHD6; -.
DR STRING; 1437606.BBOH_0743; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029096; 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:UP000029096}.
FT DOMAIN 580..602
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 728 AA; 82006 MW; 398FDD6398B5BBCD CRC64;
MGLTDSTLSM DNTTEDTGFD PEHDYHSLNA MLNLYDENGN IQFDADKEAE RAYVTGHVAQ
NTMKFDSTAD RLKYLIDNLY YEKDVFAQYS PEFLDRFYDH VENSGFEFET FLGAFKFYRS
YALKTFDGKQ YLEDFPQRAG AVALELAAGD ENAAIKYVDE IISGRFQPAT PTFLNLGKAQ
RGEPVSCFLV RVEDNMESIS RGINSALQLS KRGGGVALLL SNLREQGAPI KHIENQSSGV
VPVMKLLEDS FSYANQLGAR QGAGAVYLNA HHPDILRFLD TKRENADEKT RIKSLSLGVV
IPDITFELAK RKEKMALFSP YDVERVYGKP FADISVTEKY DEMVADDRIH KTYIDAREFF
MTLGEVQFES GYPYILFEDT VNRANPIDGR VTMSNLCSEI LQVQEASTYN ADLSYGHVGK
DISCNLGSLN IAKAMDAGLA QPVETAIRAL TSVSDHTHID SVPSIKRGNE EGHSIGLGQM
NLHGFLAREH MHYGSEEALD FTDMYFMTVA YHAYKASHAL AVERGTRFAD FEKSDYAKPA
GQGNYFDKYT DGRRSLEPRT EKVKALFERF GIAIPTVADW ETLRDEILRD GIYNSYLQAV
PPTGSISYIN HSTSSIHPIA SKIEIRKEGK TGRVYYPAPY MTNDNLEYFE DAYEIGWQRI
VDTYAEATQH VDQGLSLTLF FPAGVTTREL NKAQIYAWRK GIKTLYYIRI RQQALEGTEV
EGCVSCML
//
