ID U5WVT3_MYCKA Unreviewed; 696 AA.
AC U5WVT3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=MKAN_19005 {ECO:0000313|EMBL:AGZ52145.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ52145.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ52145.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ52145.1,
RC ECO:0000313|Proteomes:UP000017786};
RG McGill University Mycobacterium genome consortium;
RA Veyrier F.J., Behr M.A.;
RT "Genome sequence of Mycobacterium kansasii.";
RL Submitted (OCT-2013) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR EMBL; CP006835; AGZ52145.1; -; Genomic_DNA.
DR AlphaFoldDB; U5WVT3; -.
DR KEGG; mkn:MKAN_19005; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_3_11; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000017786; Chromosome.
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: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:UniProtKB-UniPathway.
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; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
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; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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 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, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 11..99
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 696 AA; 75121 MW; C0F6D24D6C6FDEE7 CRC64;
MESAMAARWP AQVRRRDATL VPFDIARIEA AVARAAREVA YDDPDMPATV ARAVADTLGP
RIASVERVGD FVEARLGEAG LDDVARAYII YRQRRAELRA GKALLGVRDE LKLSLAAVMV
LRERYLLRDA RGRPTESTGE MMDRTARCVA AAEDEYRTGS SAQWAERFAT LLRNLEFLPN
SPTLMNAGTD LGLLAGCFVL PVEDSLRSIF ATLGQAAEVQ RAGGGTGYTF SRVRPAGDRV
ASTGGTASGP MSFLRLYDTA ADVVSMGGRR RGACMAVLDA SHPDICDFIS AKAESTSHLT
HFNLSVGVGD AFLRAVERGG AHRLVNPRTG KTVARMPAAE LFDAICQAAH ACGDPGLVFL
DTINRANPVP ARGRIEATNP CGEVPLLPYE SCNLGSINLA RMITNGHLDW DRLGAVTEVA
VRFLDDVIDV SRYPFPELAE ATRASRKIGL GIMGLAELLA SLGIPYDSVE GVRLAGQVMR
RIQRHAHLAS RRLAEDRGSF PAFADSRLVR FGPRRNAQVT SVAPTGTISL IAGTTAGIEP
MFAIAFTRAI VGRQLLEVNP CFDRLARDQG FYRDELVAEI AQRGGVRGYP RLPAELRAAF
PTAAEIAPQW HLRMQAAVQR HVDAAVSKTV NLPAAATVDD VRAVYLSAWR AKVKGITVYR
YGSREGQVLS YAAPEPVLAR ADTEFSGGCA GRSCEF
//