ID U4T7P2_9GAMM Unreviewed; 758 AA.
AC U4T7P2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=M917_2100 {ECO:0000313|EMBL:ERL54754.1};
OS Psychrobacter aquaticus CMS 56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL54754.1, ECO:0000313|Proteomes:UP000016761};
RN [1] {ECO:0000313|EMBL:ERL54754.1, ECO:0000313|Proteomes:UP000016761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 56 {ECO:0000313|EMBL:ERL54754.1,
RC ECO:0000313|Proteomes:UP000016761};
RX PubMed=24201199;
RA Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT Dry Valley Region of Antarctica.";
RL Genome Announc. 1:e00918-13(2013).
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:ERL54754.1}.
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DR EMBL; AUSW01000034; ERL54754.1; -; Genomic_DNA.
DR RefSeq; WP_021814724.1; NZ_AUSW01000034.1.
DR AlphaFoldDB; U4T7P2; -.
DR STRING; 1354303.M917_2100; -.
DR PATRIC; fig|1354303.4.peg.2066; -.
DR eggNOG; COG0209; Bacteria.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016761; 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 Gene3D; 1.10.1650.20; -; 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}.
FT DOMAIN 7..97
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 758 AA; 85288 MW; 45C03CCD7F7FAE46 CRC64;
MTHIDKIQVT KRDGRLEPID LDKIHKVIAW AAHGLDNVSV SQVELKSHIQ FYEGIKTRDI
HETIIKSAAD LISETTPDYQ YLAARLAIFH LRKIAYNRFT PPHLYDHVKK LTDAGKYDEH
ILADYSRAEF DELEAYLDHW RDMNLAYAAV EQMAGKYLVQ DRVSKTVYES PQFLYMLVGM
CLFSQYDKSD RLDYVKRFYD ATSQFKISLP TPIMSGVRTP SRQFSSCVLI ECGDSLDSIN
ATTSAIVRYV SQRAGIGINA GRIRALGSPI RGGEAQHTGC IPFYKLFQTA VKCCSQGGVR
GGAATLFYPL WHLEVESLLV LKNNRGVEDN RVRHMDYGVQ LNKTMYTRLI KGQDISLFSP
GDTPGLYDAF FEDQDKFEEL YTKYENDPAI RSRQIPAADL FSLMMQERAS TGRIYIQNVD
HCNTHSPFDP TVAPIRQSNL CMEIALPTKP MDNINDEEGE IALCTLSAVN LGKVENVSDI
EEPAELIVRA LDALLDYQDY PVKAAQNGSM RRRTLGVGVI NYAYYLAKNG VRYSDDSALG
LTHQTFEALQ FYLLKASNKL AKEQGACPAF NETTYSQGIL PIDTYKADLD KICQEPLHLD
WETLRGEITE HGLRNSTLTA LMPSETSSQI ANATNGIEPP RGLVSIKASK DGILKQVVPE
IDKLKDQYEL LWQMPNNDGY LKLVAVMQKF VDQSISANTN YDPVRYEGGR VPMKILLKDL
LNAYKMGVKT LYYHNTRDGA NDAQADMEDD CAGGACKI
//
