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Database: UniProt
Entry: A0A1G5PRM7_9GAMM
LinkDB: A0A1G5PRM7_9GAMM
Original site: A0A1G5PRM7_9GAMM 
ID   A0A1G5PRM7_9GAMM        Unreviewed;       719 AA.
AC   A0A1G5PRM7;
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=SAMN03097708_00722 {ECO:0000313|EMBL:SCZ52305.1};
OS   Thiohalomonas denitrificans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiohalomonas.
OX   NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ52305.1, ECO:0000313|Proteomes:UP000199648};
RN   [1] {ECO:0000313|EMBL:SCZ52305.1, ECO:0000313|Proteomes:UP000199648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLD2 {ECO:0000313|EMBL:SCZ52305.1,
RC   ECO:0000313|Proteomes:UP000199648};
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; FMWD01000002; SCZ52305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5PRM7; -.
DR   STRING; 415747.SAMN03097708_00722; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000199648; 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:UP000199648}.
FT   DOMAIN          21..93
FT                   /note="Ribonucleotide reductase large subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00317"
FT   DOMAIN          106..654
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   719 AA;  81147 MW;  A9E946CD69087545 CRC64;
     MTKPVQLKAV KNTQVTEIPF QAASLDIWDK KYRLKTKSGE VIDQELDDTF KRVAHALAEV
     EESNANKEHW YERFLWALRH GAIPAGRITS NAGALAYKPA TSTINCTVSG TVHDSMDDIL
     QKVHEAGLTL KAGCGIGYEF STLRPKGAFV AGAGAYTSGP LSFMDIYDRM CFTVSSAGGR
     RGAQMATFDV GHPDVMDFIR AKREDGRLRQ FNLSLLVTEE FMEAVKAEAV WKLAFPLTAK
     EVEIDAIDIE DPEQVVWREW PTNDDFLTNG EGLVACKVYK SVPARRLWDL IMTSTYDFAE
     PGFILIDQYN EMNNNWFCEN VRATNPCGEQ GLPPYGACLL GSVNLTKFVL DPFTDQARFD
     WESYREAVSV FTRMLDNVVE INGLPLPEQR AEIESKRRHG MGYLGLGSTL TMLRMEYGDE
     SSLEFTERVT RELALTGWRT GVELAKEKGP APIMEQEFTI TADMLRRRPE LKRDGIKVGD
     KLPGRVLHAK YSRYMQRVAE VDPELVEAMA ETGCRFTHHS SIAPTGTISL SLANNASNGI
     EPSFAHKYSR NIIREGRKTK EKVDVLSFEL LAYRELINQA ADPYAQEDDK KLPDYFITAE
     QVTPKQHVDI QAAAQKWIDS SISKTANVPT EYPFQDFKDI YLYAYEKDLK GCTTFRFNPE
     AFQGVLVQDK DLEATTYRFE LENGKTIELK GNEEVEYDGE MHTAANLYDA LKEGYYGKF
//
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