ID A0A1I7CRF9_9RHOB Unreviewed; 835 AA.
AC A0A1I7CRF9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05216236_11914 {ECO:0000313|EMBL:SFU02002.1};
OS Sedimentitalea nanhaiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Sedimentitalea.
OX NCBI_TaxID=999627 {ECO:0000313|EMBL:SFU02002.1, ECO:0000313|Proteomes:UP000182466};
RN [1] {ECO:0000313|EMBL:SFU02002.1, ECO:0000313|Proteomes:UP000182466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10959 {ECO:0000313|EMBL:SFU02002.1,
RC ECO:0000313|Proteomes:UP000182466};
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; FPAW01000019; SFU02002.1; -; Genomic_DNA.
DR RefSeq; WP_027262874.1; NZ_FPAW01000019.1.
DR AlphaFoldDB; A0A1I7CRF9; -.
DR STRING; 999627.SAMN05216236_11914; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000182466; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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; PF01381; HTH_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS50943; HTH_CROC1; 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:UP000182466}.
FT DOMAIN 591..635
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 835 AA; 91882 MW; 2E957019E67907D0 CRC64;
MSRFAAPIAD QIWDMKYRFK NADGTPIDQS VEDTWRRIAR DLAKGEQDPK IWEDRFYGAL
EDFKYLPAGR ITAGAGTARQ VTLFNCFVMG TVPDSMGGIF EMLKEAALTM QQGGGIGYDF
STIRPKGADV KGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDVEQFIT
AKSDSARLRM FNLSVLVTDD FMQAVKDDAP WDLQFDGKIY HTVQARDLWN KMMRATYDYA
EPGVIFIDRI NAANNLAYCE TIAATNPCGE QPLPPYGACL LGSINLAQLV AAPFEADAHL
DQDALSELVA TAVRMMDNVV DVSKFPLPQQ AEEARNKRRI GLGVTGLADA LLMLGLRYGS
EEAARQTERW LHAIARAAYL ASVQLAKEKG AFPLFDAEKY LASGTMQQMD EDVREAIREH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYSRKVL QKDGSRTEEE VVDYAVQMWR
DKFGEVDLPD YFVNAQTLTP VEHVRMQAAA QKWVDSSISK TINCPEDIDF DAFKDVYVQA
WDMGCKGCTT YRPNDVTGSV LSVSEEKKEL PQLPSVAARL DWAREYAGLP TKRALAEAVG
ASEQVLNLIL NNKRDLSKEI AVKAAKALNV PAGWLLFGKA ESAPEIVAQS DAEPQTPHGD
VIYMSDPLDR PGELGGSTYK LKWPDSEHAL YITVNDIVIN GRRRPFEVFI NSKNMEHFAW
TVALTRMISA VFRRGGDVSF VVEELKAVFD PRGGAWVQGK YIPSILAAIG GVIERHMISI
GFLEGEGMGL KSDPQAQVVN MDGPRGRACP SCGQFEMRMI EGCMTCGSCG HSKCG
//
