ID E7NY82_TREPH Unreviewed; 845 AA.
AC E7NY82;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ORFNames=HMPREF9554_03052 {ECO:0000313|EMBL:EFW36468.1};
OS Treponema phagedenis F0421.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW36468.1, ECO:0000313|Proteomes:UP000004157};
RN [1] {ECO:0000313|EMBL:EFW36468.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0421 {ECO:0000313|EMBL:EFW36468.1};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFW36468.1}.
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DR EMBL; AEFH01000263; EFW36468.1; -; Genomic_DNA.
DR RefSeq; WP_002701385.1; NZ_GL638123.1.
DR AlphaFoldDB; E7NY82; -.
DR STRING; 162.TPHV1_30224; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_12; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004157; Unassembled WGS sequence.
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 CDD; cd01679; RNR_I; 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}.
FT DOMAIN 1..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 845 AA; 96956 MW; EF657BEECE3650E0 CRC64;
MEIIKRNGER RPYEAEKIGR AIRAAFDSVP ASPHTDIGKI VDSLTMEIEG DIKDLSKNGN
LVQVETIQDL VEKTLIEHNY YAEVKNFILY RVDRTKKRDA RKTIEQSFPT IDVRSVLLEV
QNDFTEDEYN LNLLSHKFHS FKKNDMSERE CLNLLIKAAV ELTAQEAPRW ELIASRLLML
SFTEELSVEL EKRNIHSFYE KISYLEENGL YGDYIRKHYT KEELETAFSY IDTERNKLLT
YSSLDMLLRR YVIRTRGHIP LETPQEMFLG IALHLAMLEK EKRMYWVKQF YDMLSKLQVT
MATPTISNAR KPYHQLSSCF IDTVPDSLDG IYRSIDNFAK ISKFGGGMGL YFGKVRAVGS
PIRGFQGAAG GIIRWIKLAN DTAVAVDQLG VRQGSVAVYL DIWHKDVPEF LQLRTNNGDD
RMKAHDVFPA ICYPDLFWKT VRDDINASWY LMCPHEILSV KGYSLEDYFG DEWEKRYKDC
VQDSRISKRE IPIKELVRLI LKSAVETGTP FAFYRDAANK TNPNGHKGMI YCSNLCTEIA
QNMSPIQSQS QEIKTVDGET VVVTTTKPGD FVVCNLASLV LGNIEVTDRK ELQRIVYSVV
RALDNVIDLN YYPVPYAKIT NGQYRAIGLG TSGYHHMLAK QNIAWESEEH LRFVDKVFED
INFAAIEASM QIAKEKGSYL YFEGSDWQTG AYFTKRNYTS ERWQALQKEV QTSGMRNGYL
LAIAPTSSTS IIAGTTAGTD PVMKRYFLEE KKGALMPRVA PALSMKTFWL YKNAHLIDQE
WSMRAAGVRQ RHVDQAQSVN LYITTDYTFK KVLGLYLKAW EEGVKSIYYV RSQSLEVEEC
ETCSS
//
