ID A0A1G9CUT4_9BACI Unreviewed; 853 AA.
AC A0A1G9CUT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05216243_3552 {ECO:0000313|EMBL:SDK55432.1};
OS Sediminibacillus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sediminibacillus.
OX NCBI_TaxID=407036 {ECO:0000313|EMBL:SDK55432.1, ECO:0000313|Proteomes:UP000198694};
RN [1] {ECO:0000313|EMBL:SDK55432.1, ECO:0000313|Proteomes:UP000198694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6502 {ECO:0000313|EMBL:SDK55432.1,
RC ECO:0000313|Proteomes:UP000198694};
RA de Groot N.N.;
RL Submitted (OCT-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|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; FNFL01000008; SDK55432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9CUT4; -.
DR STRING; 407036.SAMN05216243_3552; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000198694; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198694}.
FT DOMAIN 130..181
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 188..767
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 95907 MW; B6224D4C4D08EB87 CRC64;
MKTITEIQNK INVEQLNKDI ELFEQVHPIS PDMKITHKGV SRLVMLDRYA FKDTEKNTLK
QGDFVVLTVK ADPKFPARGF GFVKAIDWEN KLVDIQVDKD FISVLDNDDE AKTGVVTRPL
DVIDKPLEIY YEQIAKRNAT GLAKVETSKE KQNEAFERFY HELSNMNFIP AGRVLYGAGA
ETDVTYFNCY VMPYIQDSRE GISEHRKQVM EIMSRGGGVG TNGSTLRPRN TLARGVNGKS
SGSVSWLDDI AKLTHLVEQG GSRRGAQMIM LADWHPDIVE FIISKMQNPR ILRFLIENTE
DEQIKRLAQE KLKFTPLTPT EMDLYQGIVN YKNMPGLGGF PENAIKEAEE KLNTGGTYSV
HNSEFLTGAN ISVCLTKEFM EAVENDAEYE LRFPNVENYS TEEMKAYNEN WHEVGDVRRW
EEQGYSIRVY RRMKAKELWN LINICATYSA EPGIFFIDNA NDMTNAKAYG QQVVATNPCG
EQPLAPYSVC NLAAVNLASV ADKVNKKVDF DKLRSIVETG VRMQDNVIDA TPYFLEANKK
QALGERRVGL GVMGLHDLLI YTETEYGSAE GNRLVDEIFE TIATTAYRSS IELAKEKGSF
PFLVGDTEQE TKELRERFIN TGYLKKMPED IRQDILDYGI RNSHLLTVAP TGSTGTMVGV
STGLEPYFSF SYYRSGRLGK FIEVKADIVQ EYLDNHPEQD ADNLPKWFVT AMELAPEAHA
DTQCVIQKWV DSSISKTVNA PKGYSVEQVE SVYRRLYNGG AKGGTVYVDG SRDTQVLSLK
AEDNSFDEDG REKEESNKPH VVLMDTIHEL EKTKVTIGSE VGDTCPVCRK GTVEDIGGCN
TCTNCNAQLK CGL
//
