ID A0A099GJH4_9RHOB Unreviewed; 1211 AA.
AC A0A099GJH4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=IX56_05115 {ECO:0000313|EMBL:KGJ22965.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ22965.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ22965.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22965.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ22965.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22965.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-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:KGJ22965.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRKQ01000015; KGJ22965.1; -; Genomic_DNA.
DR RefSeq; WP_036707889.1; NZ_JRKQ01000015.1.
DR AlphaFoldDB; A0A099GJH4; -.
DR Proteomes; UP000029858; 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:UP000029858}.
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 812..910
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1211 AA; 131282 MW; 71C8B52748B7723B CRC64;
MKIDRRYTTT ETGAYGGIDF VTTTSEIRNP DGTVVFRNDA VEVPEGWSQV ASDVIAQKYF
RKAGVPARLK RVKEKGVPEF LWRSVADEAA LAALPEGERN VGETSARQVF DRLAGAWAYW
GWKGGYFTTE ADARAYYDEM RHMLARQMGA PNSPQWFNTG LHWAYGIDGP SQGHFYVDYR
TGALVKSDSA YEHPQPHACF IQSVSDDLVN EGGIMDLWVR EARLFKYGSG TGTNFSSLRG
EGEKLSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VICDMDHPDI EQFINWKVIE
EQKVASLVAG SKQHEAKLNE IFAAIRQWDG SAEGATDPAQ NAALKGAIRA AKRAMIPETY
INRVLQYARQ GFDSIEFPTY DTDWDSEAYA SVSGQNSNNS VRVTDAFLKA VREDADWALI
RRTDGKTAKT VKARELWDQI GHAAWACADP GIQFHDTVNA WHTCPEDGPI RGSNPCSEYM
FLDDTACNLA SMNLLTFLNG GQFDAQGYVH ATRLWTVTLE ISVLMAQFPS KEIAQRSYDF
RTLGLGYANI GGLLMNLGLG YDSDEGRALC GALTALMTGV SYATSAEMAG ELGPFPGYAK
NADHMLRVIR NHRAAAHGTE AYEAVNVAPV ALDVENCPDP ELAVMAQRAW DKALALGEEH
GFRNAQTTVI APTGTIGLVM DCDTTGIEPD FALVKFKKLA GGGYFKIINQ SVPAALETLG
YGSAQIEEIV AYAVGHASLG NCPGINHSAL VGHGFGPREL EKVDAALASA FDIRFVFNQW
TLGEDFCKGT LGIPAEKLSD PGFDLLRHLG FTRAQIDAAN DHVCGTMTLE GAPFLKPEHY
AVFDCANACG KKGTRYLSVD SHIRMMAAAQ SFISGAISKT INMPNSATIA DALAAYELSW
SLGIKANALY RDGSKLSQPL ASALVEDDDE AAEVLESGSA QEKATVIAEK IVERIIVKEA
IRSNREKLPA RRKGYTQKAI IGGHKVYLRT GEYDDGKLGE IFIDMHKEGA GFRAMMNNFA
IAVSVGLQYG VPLEEFVDAF TFTRFEPAGM VQGNDSIKNA TSILDYIFRE LAVSYLDRTD
LAHVKPNGTS FDDLGNGHRE GQPELVPAET GASKSVELLK QISSTGYLRK RMPQELMVLQ
GGVSTVAVAS GMAEEAAVFE STTVAVTMDA RTKAKMQGYE GDPCGECGNY TLVRNGTCMK
CNTCGGTSGC S
//
