ID A0A0C1F5D6_9FLAO Unreviewed; 850 AA.
AC A0A0C1F5D6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=OA86_10265 {ECO:0000313|EMBL:KIA88417.1};
OS Kaistella jeonii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Kaistella.
OX NCBI_TaxID=266749 {ECO:0000313|EMBL:KIA88417.1, ECO:0000313|Proteomes:UP000031473};
RN [1] {ECO:0000313|EMBL:KIA88417.1, ECO:0000313|Proteomes:UP000031473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17048 {ECO:0000313|EMBL:KIA88417.1,
RC ECO:0000313|Proteomes:UP000031473};
RA Clayton J.T., Newman J.D.;
RT "Kaistella jeonii genome.";
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|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:KIA88417.1}.
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DR EMBL; JSYL01000007; KIA88417.1; -; Genomic_DNA.
DR RefSeq; WP_039352617.1; NZ_LR134503.1.
DR AlphaFoldDB; A0A0C1F5D6; -.
DR STRING; 266749.SAMN05421876_10811; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000031473; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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}.
FT DOMAIN 29..93
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 111..643
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 850 AA; 95972 MW; 7F8409CB9FB35AB1 CRC64;
MEATAFAKKI KTYTYDEAIQ SSLQYFEGDD LAAKVWVSKY ALKDSAGNIY EQNPDDMHHR
IASEIARVEA KYPNSLSEEK VFDLIKKFKY IIPQGSPMTG IGNNFQIASL SNCFVIGSGT
QSDSYGSIMK IDEEQVQLMK RRGGVGHDLS HIRPKGSAVK NSALTSTGLV PFMERYSNST
REVAQDGRRG ALMLSVSVNH PDSEDFVDAK LEQGKITGAN ISVRIDDEFM KAVVGKEKYI
QKYPIHSQNP KFQKEIKATD LWDKIIHNAW KSAEPGILFW DTIINESLPD CYADLGYETV
STNPCGEIPL CPYDSCRLLA VNLFSYVENP FTKKAKFNFE LFKQHVGYAQ RMMDDIIDLE
IEKIDAILAK IESDPEGDEI KATEKNLWTK IRHKTIEGRR TGVGITAEGD MLAALNIQYG
SKEGNEFATS VHKTLALAAY RSSVEMAKER GAFAIYDAKR EAKNPFILRL KEADPKLYED
LIKYGRRNIA LLTIAPTGST SLMSQTSSGI EPVFMPVYKR RRKVNPNDQD IRVDFVDEVG
DSWEEYLVFH HRFKEWMEVN GIDTDKNYSQ EELNKIIEQS PYYKATSNDV DWLSKVEMQG
SIQKWVDHSI SVTINVPNDA TEELVNQLYI KAWEVGCKGV TVYRDGSRSG VLISADEKKD
EKPEMITSVF PTKRPHILEA DVVRFQNNKE KWIAFVGLIE GKPYEIFTGL AEDEEGISVP
RWVNDGVIIK NQDENGKSRY DFQFKNQRGY KTTIEGLSHK FKPEFWNYAK LISGTLRHGM
PIENAVELIN RLELDSESIN NWKAGVARAL KRYIADGTEA AGKCSSCGSD QVVYQEGCLT
CKNCGNSKCG
//
