ID A0A196P9Q4_9RHOB Unreviewed; 755 AA.
AC A0A196P9Q4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=A8B82_13565 {ECO:0000313|EMBL:OAN77019.1};
OS Sulfitobacter sp. EhC04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1849168 {ECO:0000313|EMBL:OAN77019.1, ECO:0000313|Proteomes:UP000078479};
RN [1] {ECO:0000313|EMBL:OAN77019.1, ECO:0000313|Proteomes:UP000078479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC04 {ECO:0000313|EMBL:OAN77019.1,
RC ECO:0000313|Proteomes:UP000078479};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-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:OAN77019.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LXYI01000016; OAN77019.1; -; Genomic_DNA.
DR RefSeq; WP_067290547.1; NZ_LXYI01000016.1.
DR AlphaFoldDB; A0A196P9Q4; -.
DR STRING; 1849168.A8B82_13565; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000078479; 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}.
FT DOMAIN 8..80
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 755 AA; 82863 MW; 00E41E4FF7AE28D4 CRC64;
MSRFAAPIAE QIWDMKYRFK DADGTPRDVT VEDTWLRIAR NLAQVEKNPE EWEKPFYAAL
EDFKYLPAGR ITAGAGTARR VTLFNCFVMG TVPDSMGGIF DMLKEAALTM QQGGGIGYDF
STIRPRGADV KGVSADASGP LSFMDVWDAM CRTIMSAGSR RGAMMATMRC DHPDVEDFIA
AKSDPARLRM FNMSVLITDA FMDAVKADGP WELTFDNKVY RTLQARDLWN RIMRATYDFA
EPGVIFIDRI NQANNLSYCE TIAATNPCGE QPLPPYGACL LGSINLARLV SNPFEPDAGL
DLDALGELVA TAVRMMDNVV DASKFPLEAQ AREAQAKRRI GLGVTGLADA LLMTGLRYGS
DEAAAQTEEW MKQIARAAYL ASVDLAKEKG PFPLFDAEAY LASGTMQMMD EDVREAIRTH
GIRNALLTSV APTGTISLYA GNVSSGIEPV FAYAYTRKVL QKDGSRTEEE VVDYAVQMWR
ELKGDADLPD YFVNAQTLAP LDHVKMQAAA QKWVDSSISK TINCPEDISF DAFKDVYMAA
WDQGCKGCTT YRPNDVTGSV LSVSDTKSED SPLPVVEGGE VVYMSEPLDR PSELEGNTYK
VKWPDSEHAL YITINDIVLN GHRRPFEVFI NSKNMEHFAW TVALTRMISA VFRRGGDVSF
VVEELKAVFD PRGGAWMKGK YIPSILAAIG GVIEQHMIAT GFIAGEGLGL KTDPQARVVG
LDAPRGKACP SCGQFDMRMI EGCMTCASCG HSKCG
//
