ID A0A0J5QE79_9RHOB Unreviewed; 1245 AA.
AC A0A0J5QE79;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-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=IMCC21224_112091 {ECO:0000313|EMBL:KMK67226.1};
OS Puniceibacterium sp. IMCC21224.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1618204 {ECO:0000313|EMBL:KMK67226.1, ECO:0000313|Proteomes:UP000036046};
RN [1] {ECO:0000313|EMBL:KMK67226.1, ECO:0000313|Proteomes:UP000036046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21224 {ECO:0000313|EMBL:KMK67226.1,
RC ECO:0000313|Proteomes:UP000036046};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21224 belonging to the
RT Alphaproteobacteria.";
RL Submitted (MAY-2015) 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:KMK67226.1}.
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DR EMBL; LDPY01000001; KMK67226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J5QE79; -.
DR STRING; 1618204.IMCC21224_112091; -.
DR PATRIC; fig|1618204.4.peg.2141; -.
DR Proteomes; UP000036046; 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:UP000036046}.
FT DOMAIN 54..163
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 214..764
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 822..927
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1245 AA; 135265 MW; 2EFBC749A5DB7907 CRC64;
MLPLQNGTSV GETTNDWKHG AKQMQIERKF TSAGQDAYQG IDFATTVSEI RNPDGTIVFK
LDNVEVPTKW SQVASDVIAQ KYFRKAGVPV ELKKVAEKGV PEFLWRSVPA SDKTEKVGET
SSKQVFDRLA GAWTYWGWKG GYFTTESDAR AYYDEMRNML ASQRAAPNSP QWFNTGLHWA
YGIDGPGQGH YYVDYKTGKL TKSKSAYEHP QPHACFIQSV KDDLVGEGGI MDLWVREARL
FKYGSGTGTN FSSLRAANEP LSGGGKSSGL MGFLKIGDRA AGAIKSGGTT RRAAKMVIID
ADHPDIEEFI NWKVKEEQKV ASIVAGSKMH EQKLNLIFAA IREWDGAEAD AYDPKKNETL
KAAIRQAKKV AIPETYVKRV LDYAKQGYGS IEFPTYDTDW DSEAYASVSG QNSNNSIRVT
DAFLKAVKDD ADWELIRRTD GSVAKTIKAR DLWEDVGHAA WACADPGIQF HDTVNAWHTC
PEDGAIRGSN PCSEYMFLDD TACNLASMNL LTFLKDGAFQ SEDYIHATRL WTLTLEISVT
MAQFPSQEIA QRSYDFRTLG LGYANIGGLL MNMGYSYDSD EGRALCGALS AVMTGVSYAT
SAEIAGELGA FSGYERNKAH MLRVIRNHRK AAHGATDGYE ALDVKPVPLD HANCPDATLI
GLAKSSWDEA LRLGEANGYR NAQVSVIAPT GTIGLVMDCD TTGIEPDFAL VKFKKLAGGG
YFKIINHSVP AALDKLGYSS SQIEEIVAYA VGHGTIGNAP GINHTSLIGH GFGPAQIEKV
ESALASAFDI RFVFNQWTLG ETFCREVLGI PVAKLSDPTF DLLRHLGYSK RDIELANDHV
CGTMTLEGAP FLKTEHYAIF DCANPCGKKG TRYLGVKSHI YMMAAAQSFI SGAISKTINM
PNDATITDCQ AAYELSWSLG VKANALYRDG SKLSQPLASA LVEDDDEAME VLESGSMHEK
AAVLAQKVVE KIIVKEVARG REKMPERRKG YTQKAIVGGH KVYLRTGEYK DGNLGEIFID
MHKEGAGFRA MMNNFAIAVS VGLQYGVPLE EFVDAFTFTK FEPAGMVQGN DSIKNATSIL
DYIFRELAVS YLDRTDLAHV KPQGATFDDI GRGVEEGVSN VKEISESAAS RSLEVLKQIS
STGYLRKRLP QDLMVLQGGQ SGFGAATQVT SLVAEKAVAS GGTSVSYATS TTTTAATSGL
AINAVTKAKM QGYEGEACGE CGNYTLVRNG TCMKCNTCGG TSGCS
//
