ID A0A212QXN0_9PROT Unreviewed; 1207 AA.
AC A0A212QXN0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-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=SAMN07250955_10491 {ECO:0000313|EMBL:SNB64487.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB64487.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB64487.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB64487.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FYEH01000004; SNB64487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212QXN0; -.
DR Proteomes; UP000197065; 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 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.
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:UP000197065}.
FT DOMAIN 33..149
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 200..754
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 808..913
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1207 AA; 131322 MW; FBE5EEC0C4262C58 CRC64;
MPLSITRKFT SDGESPYAAI PFRTTSSEIR NPDGSVVFKL DRADVPAAWS QVAVDVLAQK
YFRKAGVPAR LKSVPEKGVP AWLCRRVADE SALAKLPEDE RYGSETSAAQ VFDRLAGTWA
YWGWKGGYFS TEADVRAFYD ELRCMLARQM GAPNSPQWFN TGLNWAYGID GPAQGHFYVD
ETNGSVLASS SAYERPQPHA CFIQSIADDL VNQGGIMDLW VREARLFKYG SGTGTNFSAL
RGINEPLSGG GRSSGLMSFL KIGDRAAGAI KSGGTTRRAA KMVTVDVDHP DIEDYILWKV
QEEQKVAALA AGSKLLQRHA RAVMAACQTD GIEGDRFDPK NNPALRKALK EARKSLLPDA
AMQQVLFYAR QGYKDIEIRT YDTDWDSDAY LTVSGQNSNN SVRLSDDFVR AVLADRDWRL
IRRTDGKLAK SIKAKTLFDK IAYAAWASAD PGVQYDTTIN DWHTCPSAGR INASNPCSEY
MFLDDTACNL ASLNLMMFKQ TDGRFAVDDF IHAVRIWTIV LEISVLMAQF PSEKIAELSF
RFRTLGLGFA NLGGLLMASG LGYDSDGGRA FCAAITALMT GTAYAVSAEM AAALGPFPGF
APDRENALRV LRNHKRAAFG EATGYESLNT PPVPLDAAIC PDPDLAQAAR QAWEQAVVAA
EQHGLRNAQV SVIAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYFKI INRMVPDALR
TLGYGTAEIE AITLYAVGRG TLKDAPGINH ETLKIKGFTM EALEKLEQSL PAAFDIKYAF
NRFTLGEDLC KDVLGFTDAQ LAEPGFDMLK ALGFTKAEIE AANNYCCGTM TIEGAPHLKP
EHYEVFDCAN PCGRLGKRFL STSSHIRMMA AAQPFISGAI SKTINMPANA GIEDCAEAYL
EGWKLGLKAL ALYRDGSKLS QPLSSQLIEE LDDEEDDVEP VVLSQVDRVK EVTERIVERL
IGERRRLPSR RKGYTQKAVV GGHKVYLRTG EYEDGTLGEI FVDMHKEGAA FRSLMNSFAI
AVSIGLQYGV PLEEFVEAFS YTRFEPSGIV SGNDTIKLAT SVLDYIFREL AISYLGRTDL
ANVEPADVRH DAIGKGLREG ERIEQPATAF ASSGFVRANL RLLAGGGQSG VNTVAEKSSV
MKRSGHSGSQ GLAEPAATFT NSRTEQVQIA KLKGYVGDPC STCGNFTLVR NGTCLKCDTC
GSTTGCS
//
