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
//