RTPR_DICDI
ID RTPR_DICDI Reviewed; 758 AA.
AC Q54CW7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Probable adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE Short=RTPR;
DE EC=1.17.4.2;
GN Name=rtpR; ORFNames=DDB_G0292654;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC reductase family. {ECO:0000305}.
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DR EMBL; AAFI02000194; EAL61130.1; -; Genomic_DNA.
DR RefSeq; XP_629553.1; XM_629551.1.
DR AlphaFoldDB; Q54CW7; -.
DR SMR; Q54CW7; -.
DR STRING; 44689.DDB0233056; -.
DR PaxDb; Q54CW7; -.
DR EnsemblProtists; EAL61130; EAL61130; DDB_G0292654.
DR GeneID; 8628811; -.
DR KEGG; ddi:DDB_G0292654; -.
DR dictyBase; DDB_G0292654; ndrJ.
DR eggNOG; ENOG502QRRC; Eukaryota.
DR HOGENOM; CLU_002384_0_0_1; -.
DR InParanoid; Q54CW7; -.
DR OMA; FHCNLAE; -.
DR PRO; PR:Q54CW7; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:dictyBase.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:dictyBase.
DR InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR Pfam; PF17975; RNR_Alpha; 1.
DR TIGRFAMs; TIGR02505; RTPR; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Disulfide bond; DNA replication; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..758
FT /note="Probable adenosylcobalamin-dependent ribonucleoside-
FT triphosphate reductase"
FT /id="PRO_0000326544"
FT REGION 233..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /evidence="ECO:0000250"
FT ACT_SITE 450
FT /evidence="ECO:0000250"
FT DISULFID 194..459
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 758 AA; 86008 MW; 31A26E078E105F8E CRC64;
MLTIKRLLLN QNLFKSSCNS TGIISINYNS NNKICFFSSS STLINKTNEI LDIEDNNNNN
NEISSSPLFL KETIKEFKLK KEFIEKYSKK KAPFGFGVLG EIVYRRSYSR VKEDNTNEQW
FETVERVVNG TYNIQRKWIE RHGLEWNQNK AQKSAQEMYN RIFEMKFLPP GRGLYSCGSS
TTESKGLFAA LNNCAFVSTL DIKKNPSKPF IFLMDASMLG VGVGFDTKGE NSIIIKGQLP
PPPPQQQPQQ QQQQHGQNNN IFIVPDSREG WVESVQLLLD SYFLKRNNPI FDYSSIRKKG
EPIKGFGGVC CGYEPLKELH DEIRALLNKC IGKPISSTNI VDLMNLIGKC VVSGNVRQAA
EIAFGDPNSQ EYIDLKNYQI NPQRASFGWC SNNSVFAELG MDYSKVCQSI LHNGEPGLAW
LDNMKAYSRM VPTELDYKDR RAMGGNPCLE QTLESYELCC LVETFPNNHE SLEDYLKTLK
YAFLYAKTVT LGSTQWPDTN KVLLRNRRIG CSMSGIAQFI HFNGLHQLKD WCVNGFKLLN
ELDEKYSEWL AIPKSIKRTS IKPSGTVSLL AGATPGMHYP ISEYYIRRIR IQKESNLIPP
LVEAGYHVEP AFENSTNVVV EIPIHSGKGI RSANSITMWE QLSLASFLQK YWADNQVSCT
VSFDPIKEGP QLKHALDYFQ YQLKGVSFLP NSSTTTSVYK QMPYEEIDET RYNQIIANLK
PVDFQKLNNS PLEPTPDKFC DSSSCTIVSD NSETLNNL
