ID A0A0F5R1B1_9BACL Unreviewed; 897 AA.
AC A0A0F5R1B1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=VE23_01525 {ECO:0000313|EMBL:KKC46089.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC46089.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC46089.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC46089.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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:KKC46089.1}.
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DR EMBL; JZEJ01000001; KKC46089.1; -; Genomic_DNA.
DR RefSeq; WP_049867128.1; NZ_JZEJ01000001.1.
DR AlphaFoldDB; A0A0F5R1B1; -.
DR PATRIC; fig|665792.3.peg.351; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000036611; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000036611}.
FT DOMAIN 143..627
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 640..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 97894 MW; D6F9A2D3A85D7221 CRC64;
MDTKAERLDG LSEKIFLDRY AWKKADPGEA AVGDTVLVLT KDDPKFPAKE VGEIIARSGR
SVTVVTRSGE RVESDVEKLA LPAERTPEEM WERLAKAMAS VEGEEARELW ENRFRSILDG
WKLVPGGRIA AGAGASEELT LFNCYVIPSP HDSRGGIMGT LTEMTEIMAR GGGVGINLSS
LRPRRAIVAG VNGASSGAVS WGGLFSYATG LIEQGGSRRG ALMLMINDWH PDLLDFITVK
QKMGEVTNAN LSVCVSNGFM QAVKEDAEWK LVFPDTRHPD YDGHWNGDLF AWKERGGTVA
PYRTVRARDV WQTIMESAWR SAEPGVVFME YYNRMSNSWY FNPIICTNPC GEQGLPGWGV
CNLSAINLSK FYDEEKHDVD WGDLGRVVQW SVRFLDNVID KTPYHFGQNE RNQKKERRVG
LGTMGLAELM IRLGIRYGSP ESLEFLDSLY RFIAREAYLA SSDIAAEKGS FPAFDAELYL
QSGFMKEMVS AFPEVAEAVR SRGIRNVTLL TQAPTGSTGT MVGTSTGIEP YFAFEYYRQS
RLGYDKQLVP IAQKWKEAHP GEELPDWFVT AMELSAEEHI RVQAAIQRWV DSSISKTANC
PADFTVEETA RLYELAYELG CKGVTIYRDG SRDTQVLSTA MGKDGAAPET EEARDSVPPL
SVDSIDREPF GGGKAGTAGP PLGTTAARSS AAAAEGGIHR AGNDDIGTGT VIDKEYRKRP
QVLCGATYKI NTPFGMAYIT INDMDGTPGE IFLNVGKAGS DVFAMAEALG RVCSLFLRYG
DHGHKVEHLI KHLKGIGGSG AIGFGANRVE SIADAVAKAL ETHAGHAVPH PVEEDVRRSQ
QRSQRADREE VSEAPPALAR SGGELSSLDL CPSCGSASLI NVEGCKTCSH CGYSRCG
//
