ID A0A0P1IU29_9RHOB Unreviewed; 1220 AA.
AC A0A0P1IU29;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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:CUK27051.1};
GN ORFNames=TA5114_02872 {ECO:0000313|EMBL:CUK27051.1};
OS Cognatishimia activa.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cognatishimia.
OX NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK27051.1, ECO:0000313|Proteomes:UP000051184};
RN [1] {ECO:0000313|Proteomes:UP000051184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-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|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; CYUE01000021; CUK27051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1IU29; -.
DR STRING; 1715691.TA5113_03130; -.
DR Proteomes; UP000051184; Unassembled WGS sequence.
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:UP000051184}.
FT DOMAIN 43..151
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 202..751
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 811..915
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1220 AA; 133331 MW; 4EFA10E20E0C19D2 CRC64;
MTKNDNKTSG QNMKIERKFT KAGQDAYADL DFISTTSEIR NPDGSIVFQA ENVEIPAKWS
QVASDVIAQK YFRKAGVPSK LKTVKEKGVP EFLWRSVPAD GAEFGGETSS KQVFDRLAGA
WAYWGWKGGY FTTEEDARAY YDEMRHMLAS QRAAPNSPQW FNTGLHWAYG IDGPAQGHHY
VDYKSGELTK STSSYEHPQP HACFIQSVSD DLVNDGGIMD LWVREARLFK YGSGTGTNFS
SIRAENEPLG GGGKSSGLMG FLKIGDRAAG AIKSGGTTRR AAKMVICDAD HPDIEEFINW
KVREEQKVAS IVAGSKVHEE KLNEIFAAIR GWDGATEDAV DPKKNDQLKT AIRGARKSKI
PETYVKRVLD YAKQGYASIE FPTYDTDWDS EAYASVSGQN SNNSIRVTDA FLQAVREDGD
WELIRRTDGA VAKTIKARDL WEQVGHAAWA CADPGIQFHD TVNAWHTCPE DGAIRGSNPC
SEYMFLDDTA CNLASLNLLT FLEDGKFQSE DYVHATRLWT VTLEISVMMA QFPSKEIAQL
SYDFRTLGLG YANIGGLLMN LGLSYDSDEG RALAGALTAI LTGVSYATSA EMAGELGPFA
GYQRNADHML RVIRNHRNAA YGATDGYEAL DVKPVPLDWA NVPDQELAKL AMACWDEALA
LGEQHGYRNA QVSVIAPTGT IGLVMDCDTT GIEPDFALVK FKKLAGGGYF KIINRSVPAA
LEKLGYGSAQ VEEIISYAVG HGTLGNAPAI NPTSLIQHGF TQTEIDKVEA AMETAFDIRF
VFNHFTLGEE FVTGPLGVPA EKLTDPEFNL LNHLGFTKAD IDAANDHICG TMTLEGAPHL
KEEHLSVFDC ANPCGKKGKR FLSVDSHITM MAAAQSFISG AISKTINMPN DATIEDCQKA
YELSWSLGVK ANALYRDGSK LSQPLAAALI EDDEDAEEVL ESGSTQEKAV VLAEKIIEKV
VIKEVQKRER ERMPERRKGY TQKAIVGGHK VYLRTGEYED GSLGEIFLDM HKEGAGFRAM
MNNFAIAVSV GLQYGVPLEE FVDAFTFTKF EPAGMVQGND SIKNATSILD YIFRELAVSY
LDRTDLAHVK PEGASFDDLG RGVEEGVSNL KELSDSAATR SLEMLKQVSS TGYLRKRLPQ
DLTMFQGGLD PEEALNTLVP ETAPVASGSD KGTVAVMDER TKAKMQGYEG EACGECGNYT
LVRNGTCMKC NTCGATSGCS
//
