ID A0A081PH09_9SPHI Unreviewed; 792 AA.
AC A0A081PH09;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=N180_13115 {ECO:0000313|EMBL:KEQ29982.1};
OS Pedobacter antarcticus 4BY.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ29982.1, ECO:0000313|Proteomes:UP000028007};
RN [1] {ECO:0000313|EMBL:KEQ29982.1, ECO:0000313|Proteomes:UP000028007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4BY {ECO:0000313|EMBL:KEQ29982.1,
RC ECO:0000313|Proteomes:UP000028007};
RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA Reddy G., Bhargava P.M.;
RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT Soils of Schirmacher Oasis, Antarctica.";
RL Int. J. Syst. Bacteriol. 42:102-106(1992).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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:KEQ29982.1}.
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DR EMBL; JNFF01000054; KEQ29982.1; -; Genomic_DNA.
DR RefSeq; WP_037440793.1; NZ_JNFF01000054.1.
DR AlphaFoldDB; A0A081PH09; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000028007; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000028007}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 792 AA; 89328 MW; 0E4F226E23C3C7E1 CRC64;
MFVEKRDGRK EAVRFDKITA RIEKLCYGFN AELVDPIDVA KKVIEGLYDG VTTSELDNLA
AETAASLTTK HPDYALLASR IAVSNLHKNT TKSFSKTMEM LYKYIDPKTD KSASLIAEDV
WEVIQENADL LDSTIIYDRD FGFDYFGFKT LEKSYLLKVN GQIVERPQHL FMRVAVGIHK
SDIESAIATY NLMSERWFTH ATPTLFNAAT PKPQMSSCFL LTMQDDSIEG IYDTLKQTAK
ISQSAGGIGL SIHNVRATGS YISGTNGTSN GIVPMLKVFN DTARYVDQGG GKRKGAFAIY
LEPWHADVIA FLDLRKNHGK EEMRARDLFY ALWVSDLFMQ RVEANEDWSL FCPHEAPGLA
DCFGEEFNAL YERYEKEGRA RKTIKAQELW FAILDSQIET GTPYLLYKDA ANSKSNQQNL
GTIKSSNLCT EIIEYTSKDE VAVCNLASLA LPRYVINGEF DHQRLYDVTY QVTINLNKII
DHNYYPIEEA RNSNMRHRPV GLGVQGLADA FILMRLPFES EAAKELNKEI FETIYFAAMT
ASHDLAVKEG AYQTFEGSPL SKGKFQFDLW NVKPESNRWD WETLRTKVMK DGVRNSLLVA
PMPTASTSQI LGNNECFEPY TSNIYTRRVL SGEFIVVNKH LLKDLVALGL WTPAMKDRII
LANGSIQHIA EIPDYIKELY KTVWEIKMRS IIDMAADRGA YICQSQSLNL FINAPNTSKL
TSMHFYAWKK GLKTGMYYLR TQAASQAVKF TVENQAGKNM EPVIPAQIDQ AVEEITDGPV
CSMEEGCISC SG
//
