ID K1E0L4_9MICO Unreviewed; 969 AA.
AC K1E0L4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=B277_04095 {ECO:0000313|EMBL:EKA62199.1}, CWN80_02720
GN {ECO:0000313|EMBL:RWU85080.1};
OS Janibacter hoylei PVAS-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1210046 {ECO:0000313|EMBL:EKA62199.1, ECO:0000313|Proteomes:UP000004474};
RN [1] {ECO:0000313|EMBL:RWU85080.1, ECO:0000313|Proteomes:UP000288711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU85080.1,
RC ECO:0000313|Proteomes:UP000288711};
RX PubMed=19643890; DOI=10.1099/ijs.0.002527-0;
RA Shivaji S., Chaturvedi P., Begum Z., Pindi P.K., Manorama R.,
RA Padmanaban D.A., Shouche Y.S., Pawar S., Vaishampayan P., Dutt C.B.,
RA Datta G.N., Manchanda R.K., Rao U.R., Bhargava P.M., Narlikar J.V.;
RT "Janibacter hoylei sp. nov., Bacillus isronensis sp. nov. and Bacillus
RT aryabhattai sp. nov., isolated from cryotubes used for collecting air from
RT the upper atmosphere.";
RL Int. J. Syst. Evol. Microbiol. 59:2977-2986(2009).
RN [2] {ECO:0000313|EMBL:EKA62199.1, ECO:0000313|Proteomes:UP000004474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:EKA62199.1,
RC ECO:0000313|Proteomes:UP000004474};
RX PubMed=23144385; DOI=10.1128/JB.01728-12;
RA Pawar S.P., Dhotre D.P., Shetty S.A., Chowdhury S.P., Chaudhari B.L.,
RA Shouche Y.S.;
RT "Genome Sequence of Janibacter hoylei MTCC8307, Isolated from the
RT Stratospheric Air.";
RL J. Bacteriol. 194:6629-6630(2012).
RN [3] {ECO:0000313|EMBL:RWU85080.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PVAS-1 {ECO:0000313|EMBL:RWU85080.1};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RL Submitted (NOV-2017) 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:EKA62199.1}.
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DR EMBL; ALWX01000014; EKA62199.1; -; Genomic_DNA.
DR EMBL; PIPF01000002; RWU85080.1; -; Genomic_DNA.
DR RefSeq; WP_007925395.1; NZ_PIPF01000002.1.
DR AlphaFoldDB; K1E0L4; -.
DR STRING; 1210046.B277_04095; -.
DR PATRIC; fig|1210046.3.peg.797; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000004474; Unassembled WGS sequence.
DR Proteomes; UP000288711; 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: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 CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 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 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}.
FT DOMAIN 50..133
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 154..689
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 859..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 105011 MW; A2925F9E2B2463C5 CRC64;
MTETAGKSSA RRGSRTKGLT ITRIHTTEGV HPYDEVVWEK RDVVQQNWKT GETIFEQRGV
EFPDFWSVNA STIVTTKYFR GAVGSPQRES GLKQLIDRVV LTYVKAGKEH GYFATDADAE
IFEHELTYAL LHQIFSFNSP VWFNVGTLSP QQVSACFILS VDDSMDSILN WYKEEGFIFK
GGSGAGLNLS RIRSSKELLS SGGTASGPVS FMRGADASAG TIKSGGATRR AAKMVVLDVD
HPDIEEFVET KAREEDKIRA LRDAGFDMDL GGADITSVQY QNANNSVRVT DEFMRAVDEG
TDFGLTSRKD GSVIETVDAR ELMGKIAKAA WECADPGIQY DGTINDWHTN PETGRITASN
PCSEYMSLDN SSCNLASLNL LKFLGDDDTF DAARFQAVAE LVITAMDISI CFADFPTESI
GQTTRDYRQL GIGYANLGAL LMATGHGYDS DGGRALAAAI TSLLTGASYK RSAELAGIVG
SYNGYARNAD AHKRVMRKHQ AANDQIRTMH TMDKDIHAYA TKAWDAVVKT GEKNGYRNAQ
ASVLAPTGTI GFMMDCDTTG IEPDFSLVKF KKLVGGGSMQ IVNLTIPRAL KKLGYAEETI
EAIVEYIADK GHVIDAPGLK PEHYEIFDTA MGARAIAPMG HVRMMAAVQP FLSGAISKTV
NLPESATVEE IEDVYMQGWK LGLKALAVYR DNCKVGQPLS DGGSTAKDAK AGAEAAAAET
EKVVEYRPLR RRLPKRRTSQ TTSFAVGGAE GYLTAGTYED GELGEIFLKF GKQGSTLAGL
MDAFSIAISI ALQHGVPLET YVEKFTNLRF EPAGMTDDPD VRMAQSIMDY VFRRLALDYL
DFDTRSFMGI HTAEERARQL ETGSYEATTS DDDESYDDDS YSQGVPTTEA KEAKASPAKD
EEADVTVQSG AGAASAREVD ATVHSSAELL EKFQGKTADA PMCMTCGTKM RPAGSCYVCE
GCGSTSGCS
//
