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Database: UniProt
Entry: A0KKQ5_AERHH
LinkDB: A0KKQ5_AERHH
Original site: A0KKQ5_AERHH 
ID   A0KKQ5_AERHH            Unreviewed;       767 AA.
AC   A0KKQ5;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
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   Name=nrdA {ECO:0000313|EMBL:ABK38421.1};
GN   OrderedLocusNames=AHA_2333 {ECO:0000313|EMBL:ABK38421.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38421.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK38421.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
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DR   EMBL; CP000462; ABK38421.1; -; Genomic_DNA.
DR   RefSeq; YP_856856.1; NC_008570.1.
DR   AlphaFoldDB; A0KKQ5; -.
DR   STRING; 380703.AHA_2333; -.
DR   EnsemblBacteria; ABK38421; ABK38421; AHA_2333.
DR   KEGG; aha:AHA_2333; -.
DR   PATRIC; fig|380703.7.peg.2335; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_6; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000756; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN          15..105
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   767 AA;  86403 MW;  956F2B60CA4A2EEC CRC64;
     MVFRESTKGH QPMNLFVTKR NGHKEPIDLD KIHRVLDWAA EGLDNVSVSQ VELKSHIQFY
     DGIRTADIHE TVIKAAADLI SEQSPDYQYM AARLAIFHLR KKAYGQFEPP HLYQHVAKLV
     DMGKYDKHLL EDYSQAEFEE LNQHLDHWRD MDFSYAAVKQ LEGKYLVQNR VTGEIYESPQ
     FLYILVAACL FSKYPKDTRL DYIKRFYDAV STFKISLPTP IMSGVRTPTR QFSSCVLIEC
     DDSLDSINAT ASAIVRYVSQ RAGIGINAGR IRGLGSPIRG GEAFHTGCIP FYKYFQTAVK
     CCSQGGVRGG AATLFYPLWH TEVESLLVLK NNRGVEENRV RHMDYGVQIN KLMYQRLIKG
     GDITLFSPSD APGLYDAFFA DQDKFEALYV KYEQDPSIRK KTLKAVDLFS LMMQERAGTG
     RIYIQNVDHC NTHSPFDPSV APVRQSNLCL EIALPTKPLN NVDDEEGEIA LCTLSAFNLG
     AIEKLEDLEE MADLAVRALD ALLDYQDYPL KAAMKGSMNR RTLGIGVINY AYYLAKNGAR
     YSDGSGLALT HRTFEAIQYY LLKASVQLAR EFGPCPAFNE TTYAQGILPI DTYKKDLDNL
     CNEPLHLDWE ALREEIRTVG LRNSTLTALM PSETSSQISN ATNGIEPPRG LVSVKASKDG
     ILKQVVPEYD RLKDQYELLW KQPSVDGYLQ LVGIMQKFVD QAISANTNYD PARFEGNKVP
     MKQLLKDLLT AYKYGLKTLY YHNTRDGADD AQTDLQDDGC AGGACKI
//
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