RIR1_CHLMU
ID RIR1_CHLMU Reviewed; 1047 AA.
AC Q9PL93;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=TC_0214;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39086.1; -; Genomic_DNA.
DR PIR; F81728; F81728.
DR RefSeq; WP_010229837.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PL93; -.
DR SMR; Q9PL93; -.
DR STRING; 243161.TC_0214; -.
DR PRIDE; Q9PL93; -.
DR EnsemblBacteria; AAF39086; AAF39086; TC_0214.
DR GeneID; 1246340; -.
DR KEGG; cmu:TC_0214; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1327; Bacteria.
DR HOGENOM; CLU_000404_3_0_0; -.
DR OMA; YIVYRDQ; -.
DR OrthoDB; 357568at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000800; 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; 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; Repeat.
FT CHAIN 1..1047
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187210"
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; 120036 MW; 9B3FFD9BFAF817AA CRC64;
MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ENSIRSITHQ
VVKEVVQKIT DGQVVTVERI QDMVESQLYI NGLQDVARDY VVYRDDRKAH REKSWQSLSV
IRRCGTTVHF NPMKISAALE KAFRATDRIE GMTPDFVREE VNALTQKIVA EIEERCSQQD
SRIDIEQIQD IVEQQLMVVG HYATAKNYIL YREARARVRD NRVEDQIVEE APSEETFEVL
SKDGSTYMIT HSQLLARLAR ACSRFPETTD AALLTDMAFS NFYSGIKESE VVLACIMAAR
ANIEKEPDYA FVAAELLLDV VYKEALDRSR GDEDLEQVYR DHFKRYIMEG DSYRLNPELK
NLFDLDALAN AMDLSRDLQF SYMGIQNLYD RYFNHDDGRR LETPQIFWMR VAMGLALKEQ
DKTYWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDDLVNI YKVISDNAML
SKWAGGIGND WTAIRATGAL IKGTNGKSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE
VWHLDYEDFL ELRKNTGDDR RRAHDVNTAS WIPDLFFKRL QQKGSWTLFS PDDVPGLHDA
YGEEFERLYE EYERKVDSGE IRLYKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ
DHTGVVRCSN LCTEILLNCS ETETAVCNLG SVNLVQHILD DGLDEEKLSE TISIAVRMLD
NVIDINFYPT KEAKEANFAH RAIGLGVMGF QDALYKLDIS YASQEAVEFA DYSSELISYY
AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GKDNLQMDTS VRKDWEPIRS
LIREHGMRNC QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK
KLGIWDADML DDLKYFDGSL LEIERVPDHI KHIFLTAFEI EPEWILECAS RRQKWIDMGQ
SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV EKSFVDINKR GIQPRWMKNK
SASAGIVVER ASKTPVCSLE EGCEVCQ
