ID H1HMB3_9BACT Unreviewed; 861 AA.
AC H1HMB3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HMPREF9944_01367 {ECO:0000313|EMBL:EHO70748.1};
OS Segatella maculosa OT 289.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=999422 {ECO:0000313|EMBL:EHO70748.1, ECO:0000313|Proteomes:UP000003167};
RN [1] {ECO:0000313|EMBL:EHO70748.1, ECO:0000313|Proteomes:UP000003167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 289 {ECO:0000313|EMBL:EHO70748.1,
RC ECO:0000313|Proteomes:UP000003167};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella maculosa OT 289.";
RL Submitted (DEC-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:EHO70748.1}.
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DR EMBL; AGEK01000025; EHO70748.1; -; Genomic_DNA.
DR RefSeq; WP_008565323.1; NZ_JH594503.1.
DR AlphaFoldDB; H1HMB3; -.
DR STRING; 999422.HMPREF9944_01367; -.
DR PATRIC; fig|999422.3.peg.1416; -.
DR HOGENOM; CLU_000404_2_2_10; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000003167; 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:UP000003167}.
FT DOMAIN 23..94
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 105..637
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 652..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 97708 MW; EFCE49C029E27549 CRC64;
MEDNKTYSFE EAFQASLKYF GGDELAARVW VNKYAMKDSF GNIYEQSPEA MHWRIANELA
RIEQKYKNPM SAQEIFDLLD HFRYIVPAGS PMTGIGNSQQ VASLSNCFVI GLEGEADSYG
AIMRIDEEQV QLMKRRGGVG HDLSHIRPKG SPVNNSALTS TGLVPFMERY SNSTREVAQD
GRRGALMLSV SIKHPDSEAF IDAKMEEGKV TGANVSVKLD DAFMKAAISD KNYVQQWPID
AAEPKVTKEI SARKLWEKIV HNAWKSAEPG VLFWDTILRE SIPDCYADLG FRTVSTNPCG
EIPLCPYDSC RLLSINLFSY VEQPFTKEAH FNFEKFEKHV RFAQRIMDDI VDLEMEKIDL
IMEKIQVDPE NKEVKEAEYH LWEKIKRKSG MGRRTGVGIT AEGDMLAALG LRYGTQEATD
FSVSVHKTLA LNAYRSSVMM AKERGAFEIY DAKREAGNPF VQRIKEADPE LFADMQQYGR
RNIACLTIAP TGTTSLMTQT TSGIEPVFMP VYKRRRKVNP NDTDVHVDFV DEVGDSFEEY
IVYHRRFLQW MQANGYDTEK RYTQEEIDAL VAKSPYYKAT ANDVDWLMKV KMQGAIQKWV
DHSISVTVNL PNDVDEALVN RLYVEAWKSG CKGCTIYRDG SRAGVMISVS KKDKKKGSHA
EGAEVQEDEP KEPLCKQPEV TEVRPKELEC DVVRFQNNKE KWVAFVGLLN GYPYEIFTGL
QDDEEGIVLP KNITKGKIIK STLEDGSHRY DFQFENKRGY KTTVEGLSEK FNPEYWNYAK
LISGVLRYRM PIDHVMKLVS SLQLKDESIN TWKNGVERAL KKYIVDGTKA KGQKCPVCGH
ETLIYQEGCL ICTSCGASRC G
//
