RIR1_TREPA
ID RIR1_TREPA Reviewed; 845 AA.
AC O83972;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=TP_1008;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; AE000520; AAC65956.1; -; Genomic_DNA.
DR PIR; B71255; B71255.
DR RefSeq; WP_010882452.1; NC_021490.2.
DR AlphaFoldDB; O83972; -.
DR SMR; O83972; -.
DR IntAct; O83972; 2.
DR STRING; 243276.TPANIC_1008; -.
DR PRIDE; O83972; -.
DR EnsemblBacteria; AAC65956; AAC65956; TP_1008.
DR GeneID; 57879519; -.
DR KEGG; tpa:TP_1008; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_12; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 357568at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 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; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..845
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187223"
FT DOMAIN 1..98
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 534
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 536
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 538
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318..319
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 534..538
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 725..729
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 319
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 326
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 356
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 574
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 828
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 829
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 840
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 843
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 319..574
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 845 AA; 95987 MW; 47DC688E4D0B356C CRC64;
MHIIKRNGEP QPYMREKIIV AISAAFRSVQ NPLAPEVPAI ITDLAAEVER QLFEMNRAGV
PVHVEKIQDF VEKTLTKYNH SDEVKSFILY RDDRTKKRIA REQIACCFTD SSVLGVLKEI
QQDFPFPEYS LDALASKFLL FKKEVTDERR SMQLLIKAAV ELTAQEAPQW ELIAARLLML
DFSLALGTSL EKLNIHSFYE KITYLEEAGL YGVYIRTHYS RAEIEEAATY LECSRDKLFT
YSSLDMILRR YVIRTRAHVP LETPQEMFLG IALHLAMNET QDRMQWVKRF YTVLSKLQVT
VATPTLSNAR KPFHQLSSCF VDTVPDSLDG IYRSIDNFSQ VSKFGGGMGL YFGKVRAVGA
PIRGFQGAAG GILRWIKLAN DTAVAVDQLG VRQGSVAVYL DVWHKDIPEF LQLRTNNGDD
RMKAHDVFPA VCYPDLFWKT VRDNLGASWY LMCPHEILTV KGYALEDFYA EEWEKRYWDC
VKDARISKRT IPIKELVRLV LKSVVETGTP FAFYRDHANR ANPNGHRGII YCSNLCTEIA
QNMSAINLVS VKITEVDGQK VVVQTTRPGD FVVCNLASLV LSNIDLSDDK ELREVVRVAV
RALDNVIDLT YYPVPYAQVT NAYYRAIGLG VSGYHHVLAQ QGIDWESDEH LAFADRIFER
INRAAIEASM TIAREKGAYG CFTGSDWCTG AYFRKRGYVS EDWQRLQREV ATHGMRNGYL
LAVAPTSSTS IIAGTTAGVD PIMKQYFLEE KKGMLMPRVA PSLSQKTCPL YKSAHAVEQR
WSIRAAGLRQ RHIDQAQSVN LYITTDFTLK QVLDLYVYAW EVGMKSLYYV RSQSLEIDLC
GYCAS
