RIR1_CHLTR
ID RIR1_CHLTR Reviewed; 1047 AA.
AC O84834;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=CT_827;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(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; AE001273; AAC68424.2; -; Genomic_DNA.
DR PIR; D71466; D71466.
DR RefSeq; NP_220348.1; NC_000117.1.
DR RefSeq; WP_009872213.1; NC_000117.1.
DR AlphaFoldDB; O84834; -.
DR SMR; O84834; -.
DR STRING; 813.O172_04620; -.
DR PRIDE; O84834; -.
DR EnsemblBacteria; AAC68424; AAC68424; CT_827.
DR GeneID; 884629; -.
DR KEGG; ctr:CT_827; -.
DR PATRIC; fig|272561.5.peg.913; -.
DR HOGENOM; CLU_000404_3_0_0; -.
DR InParanoid; O84834; -.
DR OMA; RGSIQNI; -.
DR BioCyc; MetaCyc:MON-15783; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
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; 2.
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; 3.
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;
KW Repeat.
FT CHAIN 1..1047
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187212"
FT DOMAIN 9..111
FT /note="ATP-cone 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 118..219
FT /note="ATP-cone 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 237..327
FT /note="ATP-cone 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 670
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 672
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 674
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 457..458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 670..674
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 857..861
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 458
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 465
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 495
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 687
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 990
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 991
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 1043
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 1046
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 458..687
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1047 AA; 119421 MW; A3658C187B4668AE CRC64;
MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ESSIRSITHQ
VVKEVVQKIT DGQVVTVERI QDMVESQLYV NGLQDVARDY IVYRDDRKAH RKKSWQSLSV
VRRCGTVVHF NPMKISAALE KAFRATDKTE GMTPSSVREE INALTQNIVA EIEECCPQQD
RRIDIEKIQD IVEQQLMVVG HYAVAKNYIL YREARARVRD NREEDGSTEK TIAEEAVEVL
SKDGSTYTMT HSQLLAHLAR ACSRFPETTD AALLTDMAFA NFYSGIKESE VVLACIMAAR
ANIEKEPDYA FVAAELLLDV VYKEALGKSK YAEDLEQAHR DHFKRYIAEG DTYRLNAELK
HLFDLDALAD AMDLSRDLQF SYMGIQNLYD RYFNHHEGCR LETPQIFWMR VAMGLALNEQ
DKTSWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDNLVNI YKVIADNAML
SKWAGGIGND WTAIRATGAL IKGTNGRSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE
VWHLDYEDFL ELRKNTGDER RRAHDVNIAS WIPDLFFKRL QQKGTWTLFS PDDVPGLHDA
YGEEFERLYE EYERKVDTGE IRLFKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ
DHKGVVRCSN LCTEILLNCS ETETAVCNLG SINLVQHIVG DGLDEEKLSE TISIAVRMLD
NVIDINFYPT KEAKEANFAH RAIGLGVMGF QDALYKLDIS YASQEAVEFA DYSSELISYY
AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GEANLQMDTS SRKDWEPIRS
LVKEHGMRHC QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK
KLGIWDADML DDLKYFDGSL LEIERIPDHL KHIFLTAFEI EPEWIIECAS RRQKWIDMGQ
SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV EKSFVDINKR GIQPRWMKNK
SASAGIIVER AKKAPVCSLE EGCEACQ
