ID E1J8R5_ECOLX Unreviewed; 707 AA.
AC E1J8R5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:EFK67823.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:EFK67823.1};
GN Name=nrdD {ECO:0000313|EMBL:EFK67823.1};
GN ORFNames=HMPREF9347_03322 {ECO:0000313|EMBL:EFK67823.1};
OS Escherichia coli MS 124-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679205 {ECO:0000313|EMBL:EFK67823.1, ECO:0000313|Proteomes:UP000003390};
RN [1] {ECO:0000313|EMBL:EFK67823.1, ECO:0000313|Proteomes:UP000003390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 124-1 {ECO:0000313|EMBL:EFK67823.1,
RC ECO:0000313|Proteomes:UP000003390};
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 (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:EFK67823.1}.
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DR EMBL; ADWT01000028; EFK67823.1; -; Genomic_DNA.
DR AlphaFoldDB; E1J8R5; -.
DR Proteomes; UP000003390; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01675; RNR_III; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR012833; NrdD.
DR NCBIfam; TIGR02487; NrdD; 1.
DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF13597; NRDD; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Organic radical {ECO:0000256|ARBA:ARBA00022818, ECO:0000256|PROSITE-
KW ProRule:PRU00493}; Oxidoreductase {ECO:0000313|EMBL:EFK67823.1}.
FT DOMAIN 1..87
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 578..703
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 676
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 707 AA; 79457 MW; 129366E17765B73C CRC64;
MKRDGCKVPF KSERIKEAIL RAAKAAEVDD ADYCATVAAV VSEQMQGRNQ VDINEIQTAV
ENQLMSGPYK QLARAYIEYR HDRDIEREKR GRLNQEIRGL VEQTNASLLN ENANKDSKVI
PTQRDLLAGI VAKHYARQHL LPRDVVQAHE RGDIHYHDLD YSPFFPMFNC MLIDLKGMLT
QGFKMGNAEI EPPKSISTAT AVTAQIIAQV ASHIYGGTTI NRIDEVLAPF VTASYNKHRK
TAEEWNIPDA EGYANSRTIK ECYDAFQSLE YEVNTLHTAN GQTPFVTFGF GLGTSWESRL
IQESILRNRI AGLGKNRKTA VFPKLVFAIR DGLNHKKGDP NYDIKQLALE CASKRMYPDI
LNYDQVVKVT GSFKTPMGCR SFLGVWENEN GEQIHDGRNN LGVISLNLPR IALEAKGDEA
TFWKLLDERL VLARKALMTR IARLEGVKAR VAPILYMEGA CGVRLNADDD VSEIFKNGRA
SISLGYIGIH ETINALFGGE HVYDNEQLRA KGIAIVERLR QAVDQWKEET GYGFSLYSTP
SENLCDRFCR LDTAEFGVVP GVTDKGYYTN SFHLDVEKKV NPYDKIDFEA PYPPLANGGF
ICYGEYPNIQ HNLKALEDVW DYSYQHVPYY GTNTPIDECY ECGFTGEFEC TSKGFTCPKC
GNHDASRVSV TRRVCGYLGS PDARPFNAGK QEEVKRRVKH LGNGQIG
//