ID A0A2U1WMY8_9PROT Unreviewed; 1232 AA.
AC A0A2U1WMY8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=TSO221_11795 {ECO:0000313|EMBL:PWC53083.1};
OS Azospirillum sp. TSO22-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC53083.1, ECO:0000313|Proteomes:UP000245126};
RN [1] {ECO:0000313|EMBL:PWC53083.1, ECO:0000313|Proteomes:UP000245126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC53083.1,
RC ECO:0000313|Proteomes:UP000245126};
RA Jang J., Ishii S.;
RT "Comparative genome analysis of Azospirillum sp. strains.";
RL Submitted (JUL-2015) 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:PWC53083.1}.
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DR EMBL; LGQZ01000039; PWC53083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1WMY8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000245126; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245126}.
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..743
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 816..905
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1232 AA; 134086 MW; 2BCB31BBA3DAA2BF CRC64;
MRIQRRFTSE GQDAYASIGF RRTGSEIRNP DGSVVFSQQD IEVPEGMSQV ASDILAQKYF
RKAGVPAALK AVEENTVPSW LWRKEADEAA LANLPKEKRA VGETSAKQVF DRLAGTWTYW
GWKGGYFDSE GDARAFFDEM RFMFASQMAA PNSPQWFNTG LHWAYGIDGP SQGHFYVDFK
TGLLTSSASA YEHPQPHACF IQSVADDLVN EGGIMDLWVR EARLFKYGSG TGSNFSKLRG
EGERLAGGGK SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VTVDLDHPDI EAYIDWKAVE
EQKVAALVAG SKICQQHLTQ VMAACQNGTD PKENRELKKA IVAARKAQIP ENYIQRVMQF
ASQGYTHIDF KTYDTDWDSE AYLTVAGQNS NNSVRVSDKF IHAVMDDGAW DLIGRTNGKV
VKTLRARDLW DKIGHAAWAC ADPGVQFDTT INDWHTCPAS GRINASNPCS EYMFLDDTAC
NLASLNLMTF RRPDGSFDVE SFEHACRLWT VVLEISVLMA QFPSKEIAQL SYEFRTLGLG
FANLGGLLMA SGLSYDSDEG RALCAAISAV MTGVAYATSA EMAQELGPFP AFETNREQML
RVIRNHRRAA YGESEGYEGL SVKPVPFVAD LCPDDELAFA ARRVWDEALS LGEQHGYRNA
QATVVAPTGT IGLVMDCDTT GIEPDFALVK FKKLAGGGYF KIVNRLVPEA LGTLGYSDEE
IEEIERYAVG HGTLKGAPGV NHESLRAKGF TTEALTKLEL SLGTAFDIKF VFNKWTLGVD
FITQQLGISA EQLDAPGFDL LTALGFGKAE IEEANTFCCG AMTLEGAPYL KDEHLAVFDC
ANPCGRIGKR FLSWESHITM MAAAQPFISG AISKTINMPN SATVEECKDA YLMSWRLGLK
ANALYRDGSK LSQPLSAALV EDEEDGVEAI VEAPNAARTQ MVSERIVEKV IEKIVERKIA
DRQKLPHRRK GYTQKAMVGG HKVYLRTGEY EDGRLGEIFI DMHKEGAAFR SLMNNFAIAV
SIGLQYGVPL EEFVEAFTFT RFEPSGMVSG NDAIKMATSV IDYLFRELAI SYLGRNDLAH
ATPDDLLPFT VGTGDKQADL PEAAQVQPSD IVRRVASTGY VRNNLRVLDG GQAQRAAAAM
QIAAQATVAT AAATGTTGAA PVSTAAAVAA SATVAVGTAY GGSYSDNRYD RVREAKARGY
EGDPCGECGN MTLVRNGTCL KCDTCGSTTG CS
//
