ID A0A0A2E2B7_9PORP Unreviewed; 850 AA.
AC A0A0A2E2B7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HQ47_08865 {ECO:0000313|EMBL:KGN72961.1};
OS Porphyromonas macacae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN72961.1, ECO:0000313|Proteomes:UP000030103};
RN [1] {ECO:0000313|EMBL:KGN72961.1, ECO:0000313|Proteomes:UP000030103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL Submitted (SEP-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:KGN72961.1}.
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DR EMBL; JRFA01000025; KGN72961.1; -; Genomic_DNA.
DR RefSeq; WP_036874853.1; NZ_JRFA01000025.1.
DR AlphaFoldDB; A0A0A2E2B7; -.
DR STRING; 28115.HQ47_08865; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000030103; 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:UP000030103}.
FT DOMAIN 22..86
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 104..636
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 647..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95967 MW; EBFEBE3C277C9207 CRC64;
MDKKIYKFDD VYTATVEYFG GDELAAKVWA TKYALKDSQG NIYELTPADM HHRLAAEVAR
IEKKYPNPLS HEELFSLFDH FKYIVPQGSP MTGIGNNFQI ASLSNCFVIG LDGPADSYGA
VIKIDEEQVQ LMKRRGGVGH DLSHIRPSGS PVKNSALTST GLVPFMERYS NSTREVAQDG
RRGALMLSVS IKHPDSESFI DAKMTEGKVT GANVSVKIDD EFMKAVVDNK PYTQQYPIDS
DKPLYSKNIE ARQLWEKIIH NAWKSAEPGV LFWDTVLKES IPDCYADLGF RTVSTNPCGE
IPLCPYDSCR LLAINLYSYV KNPFTLWAEF DFELFEKHVG LAQRIMDDII DLESEKIEQI
LKKIDSDPES EEIKGSEIHL WHKIQDKTLK GRRTGVGITA EGDMIAAMGL RYGSDEATAF
SEKVQKTLAL SAYRSSVQMA KERGKFEIYD SKREENNPFI LRLKEADPEL YKEMTKHGRR
NIACLTIAPT GSTSLMTQTS SGIEPVFMPV YKRRRKVNPN DQNAAIDYVD EVGDSFEEFI
VYHPKFITWM EINGFDTKKK YTSGELDDLV AKSPYFHATA NDVDWVAKVK MQGRMQKWVD
HSISVTINLP EDVSEELVNT LYVEAWKNGC KGCTVYRDGS RSGVLISTDK KKKDGSATSE
NPSMADRTDP IKRPRSLDAD VVRFQNNKEK WIAFVGLKDG RPYEIFTGIA DDDEGIMVPK
SVSSGKIIRT YEDDGTKHYD FQFRNKRGFK MTIEGLDGKF NPEYWNYAKF ISGVLRYGMP
IEQVVNLVQG MSLNDESINT WKNGVERALR KYLPVGAEAQ GQECPNCHQK TLIYQEGCLL
CTNCGTSKCG
//
