ID A0A178M3X6_9PROT Unreviewed; 1216 AA.
AC A0A178M3X6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A6A04_09500 {ECO:0000313|EMBL:OAN42932.1};
OS Paramagnetospirillum marisnigri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1285242 {ECO:0000313|EMBL:OAN42932.1, ECO:0000313|Proteomes:UP000078428};
RN [1] {ECO:0000313|EMBL:OAN42932.1, ECO:0000313|Proteomes:UP000078428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP-1 {ECO:0000313|EMBL:OAN42932.1,
RC ECO:0000313|Proteomes:UP000078428};
RA Koziaeva V., Dziuba M.V., Ivanov T.M., Kuznetsov B., Grouzdev D.S.;
RT "Draft genome sequence of freshwater magnetotactic bacteria
RT Magnetospirillum marisnigri SP-1 and Magnetospirillum moscoviense BB-1.";
RL Submitted (APR-2016) 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:OAN42932.1}.
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DR EMBL; LWQT01000131; OAN42932.1; -; Genomic_DNA.
DR RefSeq; WP_068495925.1; NZ_LWQT01000131.1.
DR AlphaFoldDB; A0A178M3X6; -.
DR STRING; 1285242.A6A04_09500; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000078428; 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:UP000078428}.
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..752
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 827..913
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1216 AA; 133296 MW; 6F38A5279483C91E CRC64;
MRVQRYYTKA SETAYAGIEF RKASSEIRNP DGSVVFSAGD IEVPADWSQV ACDVLAQKYF
RKAGVPARLK RVPEKDVPEW LCRHEPDTEA LAALPEKERV AGETSAKQVF DRLAGTWTYW
GWKGGYFNAE EDAQAFRDEM ACMLARQMGA PNSPQWFNTG LHWAYGIDGP GQGHSYVDYK
TGKLVRSKSA YEHPQPHACF IQSIEDDLVN DGGIMDLWVR EARLFKYGSG TGTNFSKLRG
EGEKLSGGGR SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VVVDVDHPDV EKFIDWKVRE
EQKVAALVAG SRLAARTLTE VMAACREWDG EDGDARFDPK RNARLKRAIL DGRKCEIPEN
YIQRVIQFAR QGYTQIDFPV LDTDWDSEAY LTVSGQNSNN SVRVDNGFLN AVINDGDWNL
THRKNGKIAK TIKARDLWEQ IGEAAWACAD PGIQFDTTIN EWHTCPESGR INASNPCSEY
MFLDDTACNL ASLNLMCFRQ EDGSFDVEGY RHAVKLWTMV LEISVLMAQF PSPRIAELSY
EFRTLGLGYA NVGGLLMASG IPYDSDKGRA LIAAITALTT GEAYATSADM AEELGAFEGF
EKNRAAMLRV IRNHRRAAYG LGTGYENLSV LPVPLDSANC PDEPLVAAAR QSWDEALAKG
EKHGFRNAQT TVVAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYFKI INRMVPEALR
TLGYAADDIA EMIRYAVGHG SLRAAPHINH DSLRAKGFDE ETLEKLESQL EAAFDIKFVF
NKYSLGEQFC TETLGIPAAK LNDFSFDMLD FLGFTRDQID AANTYCSGAM TLEGAPFLKA
EHLPVFDCAS PCGRIGKRSL SVEAHIRMMA AAQSFITGAI SKTINMSNSA TVEDCKEAYM
LSWRLGVKAN ALYRDGSKLS QPLQASLLDD AGALADELAE ASAASRAEIV AERIVERVIQ
VQRRAKLPDR RKGYTQKAIV GGHKVYLRTG EYEDGKLGEI FIDMHKEGAA FRAMMNNFAI
AISVGLQYGV PLEEFVEAFT FTRFEPSGMV EGNETIKMSS SILDYIFREL AISYLGRNDL
AHVEPADLTP DAIGRGASES QLDQQNQHLA VVEKVASKGY VRSNLLFLKR GNGPTSMSTD
ISGGGMQLAA AAPAVVSVGG DTEALIMEFD ARAEQIRTAR MKGYEGDACP ECGNFTLVRN
GTCLKCDTCG GTTGCS
//
