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Database: UniProt
Entry: A0A1I3CX70_9RHOB
LinkDB: A0A1I3CX70_9RHOB
Original site: A0A1I3CX70_9RHOB 
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}.
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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
//
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