ID A0A251X1L6_9RHOB Unreviewed; 759 AA.
AC A0A251X1L6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=BVC71_01930 {ECO:0000313|EMBL:OUD10295.1};
OS Marivivens niveibacter.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marivivens group; Marivivens.
OX NCBI_TaxID=1930667 {ECO:0000313|EMBL:OUD10295.1, ECO:0000313|Proteomes:UP000194664};
RN [1] {ECO:0000313|EMBL:OUD10295.1, ECO:0000313|Proteomes:UP000194664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A06712 {ECO:0000313|EMBL:OUD10295.1};
RA Hu D., Wang L., Shao Z.;
RT "The draft genome sequence of HSLHS2.";
RL Submitted (DEC-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUD10295.1}.
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DR EMBL; MSPP01000001; OUD10295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251X1L6; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000194664; 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: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; 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:UP000194664}.
FT DOMAIN 9..79
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..552
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 759 AA; 83114 MW; A60B8EA1F405FE0F CRC64;
MTRFAVPIAE QIWDMKYRFK DADGKPIDGT VEDSWRRIAR ALAAVEKDPK KWEDKFYSAL
EDFKYLPAGR ITAGAGTARS VTLFNCFVMG TVPDSMGGIF DMLKEAALTM QQGGGIGYDF
STIRPKGALV KGVAADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDIEQFIT
AKSDPARLRM FNMSVLVTDP FMEAVKADGP WELVFDDKVY KTVQARDLWN QIMQSTYDFA
EPGVIFIDRI NGMNNLNYCE TIAATNPCGE QPLPPYGACL LGSINLARLV ENAFDKGARM
DVEALDDLVA TAVRMMDNVV DASRFPLEAQ AQEAAAKRRI GLGVTGLADA LLMVGLKYGT
PEAAAQTEAW MKQIARASYL ASVELAREKG AFPLFDKDKY LAAGNMMQMD DDVRAAIAEH
GIRNALLTSI APTGTISLYA GNVSSGIEPV FAYAYTRKVL QKDGSRTEEE VVDYAVKMYR
DKFGADAELP DYFVNAQTLE PLAHVRMQAA AQKWIDSSIS KTINCPEDID FETFKDVYME
AYETGCKGCT TYRPNDVTGS VLSVSESSEK TPSEAPQTAT DAEVIYMSEP LDRPAALEGN
TYKVKWPDSE HALYITVNDV VIAGHRRPFE VFINSKNMEH FAWTVALTRM ISAVFRRGGD
VSFVVEELKA VFDPRGGAWM KGKYVPSILA AIGGVLEQHM VAIGFIEGEG MGLKVDPQAE
AVAVGERPKG KPCPSCGEYG MKMESGCNSC PSCGYSKCG
//
