ID A0A095ZET1_9FIRM Unreviewed; 709 AA.
AC A0A095ZET1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HMPREF1634_06555 {ECO:0000313|EMBL:KGF07019.1};
OS Tissierellia bacterium S7-1-4.
OC Bacteria; Bacillota; Tissierellia.
OX NCBI_TaxID=1284708 {ECO:0000313|EMBL:KGF07019.1, ECO:0000313|Proteomes:UP000029539};
RN [1] {ECO:0000313|EMBL:KGF07019.1, ECO:0000313|Proteomes:UP000029539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-4 {ECO:0000313|EMBL:KGF07019.1,
RC ECO:0000313|Proteomes:UP000029539};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF07019.1}.
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; JRMY01000027; KGF07019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095ZET1; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000029539; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR000788; RNR_lg_C.
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; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 2..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 709 AA; 80055 MW; 0DCA1C9B1A2F4627 CRC64;
MVQVIKRDGR EVDFETQKIV IAVEKAMKET EKGIDEIAAK EVGEAVHEKY KDSDKVSIEE
IQDLVEFELM KRAPEAAKKY ILYREERTRL REEGWAMTNL QRDIYDKKYR YDGENFEGFI
KRVSGDNDVI GKAIKDKKFM PAGRILAGRG LDKKGKKVTL SNCYVMPKVE DNIESIFDTA
KRLARTYSYG GGCGINISKL RPKGARVNNA ASTTTGAVSF MDLFALTTGL IGMRGRRGAL
MINMDVSHPD IMEFIDVKND LSKVNSANIS VNVNDEFLKA VKEDTNYTLH FDVESSGEEI
RKEVRARDLW NTLAKNNWNM AEPGILYWDR INSWHIMSAD ENFSYAGVNP CAEEPLPAWG
SCNLSSINLG AFVRDPFTDY GRFDFEAFAN LVREGVFYLN GVLDENENLH PIKEQRELAH
NLRQIGLGIM GLADMFIKLK IKYGSPESIK LIHQIGRLMI NEALKASAEL AKKDGPFPFF
NKEAVLKSEF IRSNADDDTL EMIEKYGLRN SQLLTIAPTG SISTLIGCSN GVEPIFQISY
TRKTESIHGI DTYYKVYTDI VKQYMDKNNI FDEADLPEFI VTTSNLNYRE RIDVQSAWQQ
YIDASISSTV NVPNEFTVEE VEDLYIYAWE KGLKGITIYR DGCARGGILI TDKKKSPTDR
IEELKREIDE LADTALKQDP DKCPICGGKM NHSGGCAECQ ECGFSPCAV
//
