ID A0A1X4N739_9PROT Unreviewed; 1240 AA.
AC A0A1X4N739;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=THS27_16315 {ECO:0000313|EMBL:OSQ42061.1};
OS Thalassospira sp. MCCC 1A01428.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ42061.1, ECO:0000313|Proteomes:UP000193740};
RN [1] {ECO:0000313|EMBL:OSQ42061.1, ECO:0000313|Proteomes:UP000193740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ42061.1,
RC ECO:0000313|Proteomes:UP000193740};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL Submitted (MAR-2014) 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:OSQ42061.1}.
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DR EMBL; JFJZ01000022; OSQ42061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4N739; -.
DR STRING; 1470575.THS27_16315; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000193740; 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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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 31..147
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 198..735
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 808..914
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1147..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 135580 MW; 161FB173F6C45128 CRC64;
MRITRQFTQE DVSPYADIDF RKSSCKIKNP DGSTVFEMND IDVPSTWSQV ASDVLAQKYF
RKAGVPVALK PVKEKDVPQW LWRHEADKTK LEKMPAEERY TSELSATQVF DRLAGTWAYW
GWKGGYFDGE SDARAFFDEM RYQLAHQMGA PNSPQWFNTG LHWAYGIDGP AQGHSYVDYL
TGKLTKSTGS YEHPQPHACF IQSVSDDLVN EGGIMDLWTR EARLFKYGSG TGSNFSNVRG
EGESLSGGGR SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VVVDIDHPDI EKYIDWKVVE
EQKVAALVAG SKLAEKHLTA VLTACNNWDG AADSDERLNP RSNPQLKEAI LSARSVMIPD
SYINKIIQFA REGFTEISFK TYDTDWDSEA YLTVSGQNSN NSVRVSNDFL QAVLDDGNWN
LIRRTDGKIA QTISARDLWD KVGEAAWACA DPGIQYDTTI NEWHTCPTSG RINASNPCSE
YMFLDDTACN LASMNLMNFR SDDGGIDVAA YEHAVRLWTV VLEVSVLMAQ FPSDRIAELS
YRYRTLGLGY ANIGGLLMSM GISYDSDEGR AICASLTAIM CGVSYATSAE MAGELGAFAG
YADNADEMLR VMRNHRRAAH GEQEGYEGLS INPVPLIAAD SPYAELPVAA RAAWDKALEL
GEKHGYRNAQ TTVIAPTGTI GLVMDCDTTG IEPDFALVKF KKLAGGGYFK IINRTVPVAL
ATLGYTENQI RDMEKYAVGY GTLKGSPTIT HDALRAKGFD DAALAKIEGA LENAFDIKFV
FNKYTFGEEY CVKQLGLDGK AISDISFDML AALGFSKKEI EAANTYVCGA MTLEGAPHLR
DEDLSVFDCA NPCGRTGKRY LSADSHIRMM AAAQPFISGA ISKTINMPNN ASIQDCKDAY
IHSWKLGLKA NALYRDGSKL SQPLNSALVE EDDYADQPTA AKATEASEKI VEKIIERVIR
GDRRSLPSRR KGYTQKATVG GHKVYLRTGE YEDGKLGEIF IDMHKEGAAF RSLMNNFAIA
VSIGLQYGVP LEEYVEAFTF TRFEPSGMVS GNDAIKMATS ILDYMFRELA ISYLGRNDLA
HVQPNDILPD AVGSGVAEGN LGDEAKAEDK AIDTIRKVAS SGFVRRNLYV VDGGLPTEET
VTLKATGTDH AHSHDHDHSH HSAETASAAS AGTASSSQNN AILTVSEEVM SKTDAKMDRI
REARMKGYEG DACPDCGNFT LVRNGTCLKC DSCGGTTGCS
//
