ID A0A2U2CGP4_9RHOB Unreviewed; 1235 AA.
AC A0A2U2CGP4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=C4N9_04100 {ECO:0000313|EMBL:PWE30944.1};
OS Pararhodobacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pararhodobacter.
OX NCBI_TaxID=2184063 {ECO:0000313|EMBL:PWE30944.1, ECO:0000313|Proteomes:UP000244940};
RN [1] {ECO:0000313|EMBL:PWE30944.1, ECO:0000313|Proteomes:UP000244940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIC4N-9 {ECO:0000313|EMBL:PWE30944.1,
RC ECO:0000313|Proteomes:UP000244940};
RA Lai Q.Sr., Liu X., Shao Z.;
RT "Pararhodobacter marina sp. nov., isolated from deep-sea water of the
RT Indian Ocean.";
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:PWE30944.1}.
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DR EMBL; QEYD01000002; PWE30944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2CGP4; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000244940; 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:UP000244940}.
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..747
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"
FT REGION 1088..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 134431 MW; A5C03986DD54AC04 CRC64;
MKIERKFTTE GKDAYAALAF TTTVSEIRNP DGKIVFRNDQ VEVPQGWSQV ASDVIAQKYF
RKAGVPARLK KVSEKGVPEF LWRSVPDEKA LAELPEDERF TGETSAKQVF DRLAGAWAYW
GWKGGYFSTE ADAQAYFDEM RVMLARQMAA PNSPQWFNTG LHWAYGIDGP SQGHFYVDPF
THKLVKSKSS YEHPQPHACF IQSVSDDLVN EGGIMDLWVR EARLFKYGSG TGTNFSSLRA
EGEKLSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VIIDMDHPDI EDFINWKVIE
EQKVASLVAG SKAHEARLNE IFDAIRTWDG SSEDAVDPAK NPTLKAAIRS AKKAMIPDTY
TNRVLQYARQ GYTSIEFPTY DTDWDSEAYV SVSGQNSNNS VRVTDAFLKA VKEDAPWELL
QRTDGKVAKT VSARELWDQV GHAAWACADP GIQFHDTVNA WHTCPEDGAI RGSNPCSEYM
FLDDTACNLA SMNLLKFFDG QKFDAEAYIH ASRLWTITLE ISVMMAQFPS KEIAQRSYDY
RTLGLGYANI GGLLMNMGFG YDSDEGRALA GALTAIMTGV SYATSAEMAA ELGAFPGYAR
NRQHMLRVIR NHRRAAHGLT DFEDVNVTPV LLDAANCPDA SLVALARSAW DEALALGEQH
GYRNAQATVI APTGTIGLVM DCDTTGIEPD FALVKFKKLA GGGYFKIINQ SVPAALTKLG
YKPSQIEEIV AYAVGHGTIG QAPGINHTAL IGHGFGPAEI KKVETALATA FDIRFVFNQW
TLGEEFCRET LGIPQAKLND PSFDLLKHLG FTKAQVEAAN DHVLGTMTLE GAPHLKPEHY
AVFDCANACG KKGKRYLSVD SHIRMMAAAQ SFISGAISKT INMPNSATID ETLAAYELSW
SLGIKANALY RDGSKLSQPL ASALIEDDEE AEEILANGSL QEKAAVIAEK IVEKVIVKEI
ARGREKLPER RKGYTQKAIV GGHKVYLRTG EYGDGRLGEI FIDMHKEGAG FRAMMNNFAI
AVSVGLQYGV PLEEFVDAFT FTRFEPAGMV QGNEAIKNAT SILDYIFREL AISYLDRTDL
AHVKPSGASF DDLGSGDKEG QKNVSPVSDD AASRGLEVLR QISSTGYLRK RLPQELVVLQ
GGSSSVSAVS SVQPLARTAD GTMAPQPIPP LGGVSIAART ETSVEAVSAM GMDARTKARM
QGYEGDPCGE CGNYTLVRNG TCMKCNTCGS TSGCS
//
