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Database: UniProt
Entry: U1LMZ5_9GAMM
LinkDB: U1LMZ5_9GAMM
Original site: U1LMZ5_9GAMM 
ID   U1LMZ5_9GAMM            Unreviewed;       761 AA.
AC   U1LMZ5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=PRUB_17262 {ECO:0000313|EMBL:ERG43717.1};
OS   Pseudoalteromonas rubra DSM 6842.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117318 {ECO:0000313|EMBL:ERG43717.1};
RN   [1] {ECO:0000313|EMBL:ERG43717.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG43717.1};
RX   PubMed=22374963; DOI=10.1128/JB.06822-11;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Zhou B.C.,
RA   Zhang Y.Z.;
RT   "Genome sequence of the cycloprodigiosin-producing bacterial strain
RT   Pseudoalteromonas rubra ATCC 29570(T).";
RL   J. Bacteriol. 194:1637-1638(2012).
RN   [2] {ECO:0000313|EMBL:ERG43717.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 29570 {ECO:0000313|EMBL:ERG43717.1};
RA   Xie B.-B., Rong J.-C., Qin Q.-L., Shu Y.-L., Zhang Y.-Z.;
RT   "Genome sequence of Pseudoalteromonas rubra.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:ERG43717.1}.
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DR   EMBL; AHCD02000139; ERG43717.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1LMZ5; -.
DR   eggNOG; COG0209; Bacteria.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
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          5..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          737..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  85732 MW;  84DDE74E7E216C32 CRC64;
     MNQQLSVSKR NGRKEPLDLD KIHRVINWAA EGLNNVSVSQ VELKSHIQFY DGIRTEDIHE
     TIIKAAADLI SKDTPDYQYL AARLAVFHLR KKAYGQFEPP HLYDHVTKLV EDKRYDAGLL
     TDYTREEYEQ LNGFLEHDRD MSFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYILVAASL
     FSDYPKETRL GYIKRFYDAV SQFKISLPTP IMSGVRTPTR QFSSCVLIET ADSLDSINAT
     SSAIVKYVSQ RAGIGVNAGR IRALGSPIRN GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
     AATLFYPLWH LEVENLLVLK NNRGVEENRV RHLDYGVQFN KTMYSRLIKD DYITLFSPSD
     VPGLYDAFFE DQEKFERLYV QYEQDESIRK KRIKALELFS MFAQERASTG RIYLQNVDHC
     NTHSPFDAKV APIRQSNLCL EIALPTKPLS HVNDEEGEIA LCTLSAFNLG AISSLDELEE
     LAELAVRALD NLLDFQDYPV PAAKNATMGR RTLGIGVINF AYYLAKNGVK YSDGSANGLT
     HRTFEAIQYY LMKASNKLAQ ERGACPKFNE TTYAKGIMPI DTYKKDVDGI CNEPLHLDWD
     GLRQDVMQYG MRNSTLSALM PSETSSQISN ATNGIEPPRG HISVKASKDG ILKQVVPEYE
     RLKDNYELLW DIPSNDGYLG LVGIMQKFVD QTISANTNYD PTKFEGGKVP MKLLLKDLLT
     AYKLGVKTLY YHNTRDGASD AQDEMKPEAE DDDCAGGACK I
//
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