ID G5H7Y1_9BACT Unreviewed; 852 AA.
AC G5H7Y1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HMPREF9450_00784 {ECO:0000313|EMBL:EHB92580.1};
OS Alistipes indistinctus YIT 12060.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB92580.1, ECO:0000313|Proteomes:UP000006008};
RN [1] {ECO:0000313|EMBL:EHB92580.1, ECO:0000313|Proteomes:UP000006008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB92580.1,
RC ECO:0000313|Proteomes:UP000006008};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL Submitted (AUG-2011) 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:EHB92580.1}.
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DR EMBL; ADLD01000009; EHB92580.1; -; Genomic_DNA.
DR RefSeq; WP_009133590.1; NZ_JH370371.1.
DR AlphaFoldDB; G5H7Y1; -.
DR STRING; 742725.HMPREF9450_00784; -.
DR GeneID; 78318542; -.
DR PATRIC; fig|742725.3.peg.836; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_2_10; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000006008; 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:UP000006008}.
FT DOMAIN 32..96
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 114..648
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 852 AA; 95690 MW; BCD9F20637AF9E6C CRC64;
MSNEKETNPA AGLKEYPYAE AVEGAKEYFG GDDLAATVWV SKYALKDSFG KIYEKSPEQM
HWRIANEIAR VEGKYPNPMD ASEVYHLLKD FKYVIPQGGP MTGIGNNLQI ASLSNCFVIG
HKNPADSYGG IIRIDEEQVQ LMKRRGGVGH DLSHIRPTGS PVLNSALTST GIVPFMERYS
NSTREVAQDG RRGALMLSLS IKHPDAENFI DAKVETGKVT GANVSIKMDD EFMRAAKEGK
KYHQQFPIDS DQPMYEKDID ARSLWNKIIH NAWKSAEPGV LFWDTILRES VPDCYADLGF
RTVSTNPCGE IPLCPYDSCR LMAINLYGYV DEPFTKNAKF NFDRFKKHIA QAMRMMDDII
DLELEKVNQI LAKISKDPED EDIRSVEVSL WEKIRTKAQQ GRRTGLGITA EGDMLAALGL
QYGSDEAIDF AVEVQKTLAV EAYRASVQLA KERGAFPIFD AGREKNNPMI GRIKEADPAL
YEEMVKSGRR NIAMLTIAPT GTTSLMSQTT SGIEPVFRPV YMRRRKVNPS DKDVKVTFVD
EVGDSWEEYN VFHHKFLVWL EANGYDVAKV KNMPQEELDA LVAKSPYHKA TANDIDWVSK
VKMQGAIQKW VDHSISVTVN LPNSVTEELV SQVYQTAWES GCKGVTVYRD GSRAGVLVEK
KKDGKDNSGE YKPPLKRPVE LTADIVRFKN GEENWIAFVG IYNDRPYEIF TGKLEEDAMF
IPKKVTKGVI LKVKDADGNK RYDFQYTDKY GYTNTIGGIS RLFDEEFWNY AKLISGVLRN
GMPILDVVTL IESLHLNTES INTWKNGVAR ALKQYIPDGT KAKEKCPNCG QETLVYQNNC
PVCMSCGHSK CG
//
