ID A0A124IKG5_9PROT Unreviewed; 815 AA.
AC A0A124IKG5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=APF80_10280 {ECO:0000313|EMBL:KUO62689.1};
OS Alphaproteobacteria bacterium BRH_c36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1734406 {ECO:0000313|EMBL:KUO62689.1, ECO:0000313|Proteomes:UP000053382};
RN [1] {ECO:0000313|EMBL:KUO62689.1, ECO:0000313|Proteomes:UP000053382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c36 {ECO:0000313|EMBL:KUO62689.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-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:KUO62689.1}.
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DR EMBL; LOEV01000092; KUO62689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124IKG5; -.
DR STRING; 1734406.APF80_10280; -.
DR Proteomes; UP000053382; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
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 Pfam; PF00317; Ribonuc_red_lgN; 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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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}.
FT DOMAIN 5..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..552
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 741..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 88142 MW; 63D7BE0BD6E9499B CRC64;
MIPIAEEIWN LKYRLREPDG GSLDQSIDDT FWRVARAAAC AEPGGKRVRE AWAKKFHAAI
ADFGFLPGGR ILAGAGSKRN VTLFNCFVMA AVPDDLSGIF DEVRKAALTM QMGGGIGVDF
STLRPRGALV RSIGADASGP VSFMDVWNAM CRTIMSAGAR RGAMMATLRA DHPDIDEFIE
AKSSAGQLTN FNLSVLVPDA LMTAVACDDD WDLVFDGKVY RSVKARDLWE RIMRATYTNS
EPGVIFIDRI NAANNLAYCE TIHATNPCGE QPLPPYGACL LGALNLTVFV RDPFTDRASL
DLEALAGRTA IAVRLLDDVI DVSLYPLAEQ KKEALSKRRM GLGVTGLADA LIMCGQTYGS
AQAVQAAAAW MQTIQETAYR TSAGLAVEKG VFPLFDKDKI LSAPMIAKLS PDIGKAIAEK
GLRNGCLTTI APTGTISLLA GNVSSGIEPV FDFVYSRRVL EADGSHRSER VEDYAHALFR
QLHPGAAELP PYFVRAGDLA PEAHLKMQAA LQNYVDSSIS KTVNCPEDLG FADFKGIYKQ
AYDLGLKGCT TYRPSPLRGA VLSPLPDAGE PGGGGDDQIE DVAPIEARGR PSSGDPAAAT
PGAGRAAEVV YLSKPLAREP ILHGATYKLK WPGSDHALYV TINDIERGGR WRPFEVFINT
KSLEHYAWTV ALTRMISAVF RRGGDVTFVA EELQAIFDPQ GGRWIAGRYV PSLQAAIGEI
IEQHMKRIGF LANDESAEVE PSRVASVSAA EPPQNHDGPR SGSRRGHGAT PSALEYAEVR
DGIDRLRQCP RCGTTGYVRR EGCWTCERCG FSQCD
//
