ID A0A3D8PCM8_9RHOB Unreviewed; 1205 AA.
AC A0A3D8PCM8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=DIE28_10720 {ECO:0000313|EMBL:RDW12975.1};
OS Paracoccus thiocyanatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW12975.1, ECO:0000313|Proteomes:UP000256679};
RN [1] {ECO:0000313|EMBL:RDW12975.1, ECO:0000313|Proteomes:UP000256679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST {ECO:0000313|EMBL:RDW12975.1,
RC ECO:0000313|Proteomes:UP000256679};
RA Ghosh W., Rameez M.J., Roy C.;
RT "Whole genome sequencing of Paracoccus thiocyanatus SST.";
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:RDW12975.1}.
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DR EMBL; QFCQ01000056; RDW12975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8PCM8; -.
DR Proteomes; UP000256679; 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 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:UP000256679}.
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..745
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 804..910
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1205 AA; 130597 MW; F448DDF3F6DB5537 CRC64;
MRIERRFTTA ESGAYGALSF TTTTSEIRNP DGTVVFRNDA VEVPQGWSQV ASDVIAQKYF
RKAGVPARLK RVKEKGVPEF LWRSVPDEEA LAALPQEARF GGESSARQVF DRMAGAWAYW
GWKGGYFSNE EDARTYYDEM RYTLAAQMGA PNSPQWFNTG LHWAYGIDGP GQGHFYVDYK
TGKLVRSDSA YEHPQPHACF IQSVADDLVN EGGIMDLWVR EARLFKYGSG TGTNFSSLRG
EGEKLSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VICDMDHPDI EQFINWKVIE
EQKVASLVAG SKMHERKLNE IFAAIRGWDG SIEDATDPAR NAALKSAIRS AKRSMIPETY
VNRVLQYARQ GFDSIEFPVY DTDWDSEAYV SVSGQNSNNS VRVTDAFLRA VREDLPWELV
RRTDGKVART VSARELWEQI GHAAWACADP GIQFHDTVNA WHTCPEDGPI RASNPCSEYM
FLDDTACNLA SMNLLSFWRG GEFDADGYVH ACRLWTVTLE ISVMMAQFPS REIAQRSYDF
RTLGLGYANI GGLLMTMGLS YDSEQGRALC GALSAIMTGV AYATSAEMAA ELGPFPGYGK
NAGAMLRVIR NHRAAAHGTG SYEGVNVAPV ALDAANCPDP RLVALAQGAW DEALALGQAH
GYRNAQATVI APTGTIGLVM DCDTTGIEPD FALVKFKKLA GGGYFKIINR SVPAALEALG
YGSAQIEEII AHAVGHASLG NCPGINHASL IGHGFGPREL EKIDAALASA FDIRFVFNQW
TLGEAFCRET LGIPADKLND PSFDLLRHLG FSRAQIDAAN DHVCGTMTLE GAPHLKPEHY
PVFDCANACG KKGTRYLSVD SHIRMMAAAQ SFISGAISKT INMPNSASIG DALAAYELSW
SLGIKANALY RDGSKLSQPL ASALVEDDEE AEEILAAGNA QEKAAVIAEK IVERIIVKEA
VRSHREKLPQ RRKGYTQKAI IGGHKVYLRT GEYDDGGLGE IFIDMHKEGA GFRAMMNNFA
IAVSVGLQYG VPLEEFVDAF TFTRFEPAGM VQGNDSIKNA TSILDYVFRE LAVSYLDRTD
LAHVQPQGAR FDDLGGGEAE SQPNVAPVSE GASRSLEMLR QISSTGYLRK RLPQDLVALQ
SGVSVAAVST AEGAAAVGVV TLDARAQARM QGYEGDPCGE CGNYTLVRNG TCMKCNTCGG
TSGCS
//
