ID A0A1M4N0Q9_9RHOB Unreviewed; 1212 AA.
AC A0A1M4N0Q9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:SCM68409.1};
GN ORFNames=KARMA_2627 {ECO:0000313|EMBL:SCM68409.1};
OS Donghicola eburneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Donghicola.
OX NCBI_TaxID=393278 {ECO:0000313|EMBL:SCM68409.1, ECO:0000313|Proteomes:UP000184085};
RN [1] {ECO:0000313|Proteomes:UP000184085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (SEP-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; FMJB01000055; SCM68409.1; -; Genomic_DNA.
DR RefSeq; WP_072707030.1; NZ_FOXY01000002.1.
DR AlphaFoldDB; A0A1M4N0Q9; -.
DR Proteomes; UP000184085; 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 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:UP000184085}.
FT DOMAIN 31..139
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 190..739
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 797..903
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1212 AA; 132567 MW; 4A00791E19D86342 CRC64;
MKIERKFTKA GQDAYSELEF VLTTSEIRNP DGTVVFKLDE VEVPAKWSQV ASDVIAQKYF
RKAGVPSATK RVKEKGVPEF LWRSVPADDA VMGGETSAKQ VFDRLAGAWT YWGWKGGYFT
TEEDAQAYFD EMRYMLARQM AAPNSPQWFN TGLHWAYGID GPSQGHFYVD YKTGKLTKSD
SAYEHPQPHA CFIQSVSDDL VNEGGIMDLW VREARLFKYG SGTGTNFSSL RGEGEALSGG
GKSSGLMGFL KIGDRAAGAI KSGGTTRRAA KMVICDADHP DIEDFINWKV KEEQKVASIV
AGSKMHEARL NEIFAAIRQW DGSTEDAVDP AKNDALKSAI RGAKKNAIPE TYIKRVLDYA
KQGYSSIEFP TYNTDWDSEA YASVSGQNSN NSVRVTDAFL QAVKDDADWE LIRRTDGTVA
KTIKARELWE QIGHAAWACA DPGIQYHDTV NAWHTCPEDG SIRGSNPCSE YMFLDDTACN
LASMNLLQFY KDGQFQVENY MHASRLWTLT LEISVMMAQF PSKEIAQLSY DFRTLGLGYA
NIGGLLMQMG YGYDSPEGRA MAASLTAIMT GVSYATSAEV AGELGTFPGY QRNAQHMLRV
IRNHRNAAHG NADGYEDLAV KPVPLDIANC PDPRLTAIAA SCWDEALRLG EQHGYRNAQA
TVIAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYFKI INRSVPSALE KLGYTSAQIE
EIVAYAVGHG SLGNAPGVNH TSLIGHGFGN AELEKIETAL ATAFDIRFVF NQWTLGEAFC
KDVLGIPAPK LVDPTFDLLR HLGYTKAEID AANDHVCGTM TLEGAPHLKT EHYSVFDCAN
PCGKKGKRYL SVESHIRMMA AAQSFISGAI SKTVNMPNDA SIEDCQKAYE LSWELGVKAN
ALYRDGSKLS QPLAAALVED DDDAAEVLET GTPQEKVAVI AEKIVEKIVV KEVIKTQRTK
LPERRKGYTQ KAIVGGHKVY LRTGEYGNGN LGEIFIDMHK EGAGFRAMMN NFAIAVSVGL
QYGVPLEEFV DAFTFTKFEP SGLVQGNDSI KNATSILDYI FRELAVSYLD RTDLAHIKPE
GASFDDLHRG DEQDKRNFRE VPESRGNDPL EVLKQISSSG YLRKRVPAEL VVLRGGGDIH
SESVDSKTES LQALTTLAPE ADSAPAVGID ARAKAKMQGY EGEACGDCGN YTLVRNGTCM
KCNTCGATSG CS
//
