ID A0A1I3CX70_9RHOB Unreviewed; 767 AA.
AC A0A1I3CX70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05216258_102259 {ECO:0000313|EMBL:SFH78988.1};
OS Albimonas pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=1114924 {ECO:0000313|EMBL:SFH78988.1, ECO:0000313|Proteomes:UP000199377};
RN [1] {ECO:0000313|EMBL:SFH78988.1, ECO:0000313|Proteomes:UP000199377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11030 {ECO:0000313|EMBL:SFH78988.1,
RC ECO:0000313|Proteomes:UP000199377};
RA de Groot N.N.;
RL Submitted (OCT-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|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOQH01000002; SFH78988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3CX70; -.
DR STRING; 1114924.SAMN05216258_102259; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000199377; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199377}.
FT DOMAIN 8..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..551
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 767 AA; 83232 MW; 9C7DF587B31CC927 CRC64;
MSGFDAPIAE QIWDMKYRFK TPDGEPIDAD VEASWSRVAR ALAAQEADPA AWTPRFEAAL
RDFRFLPAGR ILAGAGTGRS VTLFNCFVMG TIPDDLGGIF EALKEAALTM QQGGGIGYDF
STIRPKGASV AGVGADASGP LSFMDVWDSM CRTIMSAGAR RGAMMATLRC DHPDVEAFVE
AKKDPARLRN FNLSILVTDA FMEAVARDAD WPLVFEGRTY RTLRARELWD RIMRATYDYA
EPGVIFIDRI NRLNNLAYAE TISATNPCGE QPLPPYGACL LGSINLARLV REPFAPGAHI
DEAELSELVG VAVRMMDDVV DASRFPLPQQ AAEAQAKRRI GLGVTGLADA LLMTGLRYGS
DEAVAQTSAW MKALARAAYF ASVELAKEKG AFPLFDTEKF CASPSVQALG EDVVEAVRAH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAFAYTRKVL QRDGTRTEEE VVDQALALWR
ELHGDAPWPE HFVDAQTLTP ADHVRMQAAA QAWVDSSISK TINVPEDISF EAFKDVYLEA
WRTGCKGCTT YRPNAVTGSV LTVSAPAPET AASPPEEAGR RPADLSAARD GEVVWMHEPL
DRPEALEGRT YKITWPDSAH AIYITLNDVV VGGRRRPFEV FINSKNMEHY AWTVALTRMI
SAVFRRGGDV SFVVEELKAV FDPRGGAWME GRYVPSILAA IGGVIEKHMI QTGFLEGEGL
ALKTDPQARA VAVGEAPGAV CPSCGEYAMQ MMEGCETCLS CGYSKCG
//