ID A0A1B1Q3F8_9CHLB Unreviewed; 1160 AA.
AC A0A1B1Q3F8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN Name=nrdJ {ECO:0000313|EMBL:ANT65358.1};
GN ORFNames=Ptc2401_01614 {ECO:0000313|EMBL:ANT65358.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT65358.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT65358.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT65358.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-2016) 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|ARBA:ARBA00025437, 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}.
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DR EMBL; CP016432; ANT65358.1; -; Genomic_DNA.
DR RefSeq; WP_068867553.1; NZ_CP016432.1.
DR AlphaFoldDB; A0A1B1Q3F8; -.
DR STRING; 1868325.Ptc2401_01614; -.
DR KEGG; proc:Ptc2401_01614; -.
DR PATRIC; fig|1868325.3.peg.1572; -.
DR InParanoid; A0A1B1Q3F8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000092496; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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:UP000092496}.
FT DOMAIN 31..131
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 182..712
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 778..890
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1160 AA; 128097 MW; 6DEFD10CBF4DCC9E CRC64;
MKFARRFTTK GTSVFDMFTY AKRSSVLRNP DGSKVFEMND IEVPEQWSQV ATDILAQKYF
RKTGVPQCDE HGKPLHDKKG KPVTGSENSV RQVVHRLVGC WKEWGEKHGY FTTPEDADVF
YDEVAYMLLR QMGAPNSPQW FNTGLNYAYG ISGPAQGHYH VDPATGKVCE SEDAYSRPQA
HACFIQSVQD DLVNEGGIFD LAVREARVFK FGSGSGTNFS NLRSSGEKLS GGGSSSGLMS
FLKIFDAAAG AIKSGGTTRR AAKMVIVDID HPDIEEFIEW KAREEDKVAS LVAGSRICSR
FLKAIVDEAI TNGADRTTNA QLNTLIQNAL SRGVPMSYVV RVLSLVEQGF TSLDFDEFDT
HYESEAYQTV SGQNSNNTVR VTNEFMKAVE NDELWVLKER TTGRDARSVR ARDLWNKILM
SAWKCADPGL QFDTTINDWH TSPKSGRING SNPCSEYMFL DDTACNLASL NLAHFIDLEK
GTVRIDDLRH ATRLWTVVLE ISVLMAHFPS EDIARLSYEF RTLGLGFANL GTMLMVQGIP
YDSPKALAFA GAISAIITGG AYATSAELAA DLGPFARYAE NKEDMLRVIR NHRRAAHNSS
EEEYEGLLVK PRGIDSEYCP SELYRAAGQV WDEALANGEK HGFRNAQVSV IAPTGTIGLV
MDCDTTGIEP EFAIVKFKKL AGGGYFKIVN QSVHKALQRL GYSDRQIDDI EKYCKGYGTL
EGCNALSHQW LKNKGFTDDK IEAVESQLQN VFDIRFAFNK WILGEEFCQS LGFSDDELDD
PNFNMLKALG ASDEDAAATN DYVCGTMTIE GAPHLKLEHL PVFDCAGTCG AKGQRYIRPM
AHVHMMSAVQ PFVSGAISKT VNMPATATIK EIGDVYFTAW QQMIKAITIY RDGSKLSQPL
SNTSFQDLDE VIMLGTEDDL DETKGPKEVQ EHIVERIYHR SERRLLPKRR KGYIREAYVG
GHKVFLRTGE YEDGALGEIF IDMYKEGASF KGLLNCFAVL ASKALQYGMP LEELVDSFTF
TRFEPAGMVQ GHNVIRNATS ILDYVFRSIG YDYLGRKDFV HVKAVDEVPE SGKGAKADHA
ASSNGEVTVT RTAEPITGHD KHASYAGGGT AVAAAADAKV IQARVQGYSG EQCENCGSMR
VKQNGTCMVC EDCGMTTGCS
//
