ID A0A3E2YUX8_9ACTN Unreviewed; 1320 AA.
AC A0A3E2YUX8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN Name=nrdJ1 {ECO:0000313|EMBL:RGC70145.1};
GN ORFNames=C5N14_06930 {ECO:0000313|EMBL:RGC70145.1};
OS Micromonospora sp. MW-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC70145.1, ECO:0000313|Proteomes:UP000258607};
RN [1] {ECO:0000313|EMBL:RGC70145.1, ECO:0000313|Proteomes:UP000258607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW13 {ECO:0000313|EMBL:RGC70145.1,
RC ECO:0000313|Proteomes:UP000258607};
RA Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA Rokni-Zadeh H., Gross H.;
RT "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT possibly plant growth promotion properties.";
RL Submitted (MAY-2018) 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|ARBA:ARBA00025437, 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:RGC70145.1}.
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DR EMBL; QKKX01000009; RGC70145.1; -; Genomic_DNA.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000258607; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide 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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
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; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR PRINTS; PR00379; INTEIN.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000258607}.
FT DOMAIN 270..418
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 493..514
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1320 AA; 143853 MW; D6370C036B812157 CRC64;
MAGDGVTTSR TRTKAGAGLK IERVWTTDGV HPYDEVTWER RDIVMTNWRD GSINFEQRGV
EFPESWSVNA ANIVTTKYFR GAVGTPEREW SLRQLIDRVV STYRKAGEEH GYFATQADAE
VFAHELTWML LHQVFSFNSP VWFNVGTPSP QQVSACLPYD SLVSTPSGLV PIGKLVEENA
VGTKVYDGNS LTKIVAVKAN GVREVIRLHT KAGYRLDVTP DHVVWKSTGD GTGRWVEAGT
LTAGDQLEWH RTYAYGESEI DLREIREAAL AGWLQSDGFV GQYDEGTNRS LTIEAMTVND
DELDWVTGTL DEIFGGAHRH ERTVATQSDE LDCRRTRLYG ERLRPFVEKW DLLTRGVGME
VPEQLFTAPL PVVAAYLRSI FQAEGYVSAR EQSTLVAVDM ISEKLIRGVQ SLLLRFGIFS
RVGHKPDPRP DRKDCWSVRI QNDGDRDLFA THIGFIGADK MAKLEQSFAK PGRPANDVKR
LEIDHVEPLG TMEVYDIQTE SGEFLAGNLR VHNCFILAVD DSMDSILDWY KEEGLIFKGG
SGSGVNLSRI RSSRELLSSG GTASGPVSFM RGADASAGTI KSGGATRRAA KMVILDVDHP
DIEEFVITKA REEDKIRALR DAGFDMDLGG NDIVSVQYQN ANNSVRVSDE FMSAVESGGG
FDLRGRLDGQ TIETIDAKKL FRTISQAAWE CADPGLQYDD TINDWHTCPE TGRITASNPC
SEYLHLDNSS CNLASLNLMK FLRADGNFEV EKFVRSVEFV ITAMDISICF ADFPTEKIGE
TTRAYRQLGI GYANLGALLM ASGLPYDSEQ GRSVAAAITS LMTGTAYRRS AELAGIVGAY
DGYARNAEPH KRVMRKHAAA NDAIKPAGTV ATAIQREATK QWTQGNKVGD KFGWRNAQAS
VLAPTGTIGL MMDCDTTGVE PDLALVKFKK LVGGGSMQIV NQTVPRALRS LGYPEEQVEA
IVEHIADHGH VVDAPGLKPE HYPVFDCAMG ERSIAPMGHV RMMAAVQPFI SGAISKTVNM
PEQATVEDVE KIYFEGWKLG LKALAIYRDN CKVGQPLSVA KPNKAVAEAP AATAAVEPVV
EKVVEYRPVR KRLPKKRPSQ TVSFSVGGAE GYLTASSYPD DGLGEVFLKM SKQGSTLAGV
MDAFSVAISI GLQYGVPLET YVSKFTNMRF EPAGMTDDPD VRMAASVMDY IFRRLALDFL
PYERRAELGI FTAKERAAQL RAEAEAESAS VSGAELTAMA SSAPVEAPET KTGPVAQPAR
EVADVAAAKP APSVGSSTEL LEAVIGKAAD APLCFTCGTK MRPAGSCYVC EGCGSTSGCS
//
