ID A0A2G8EGS5_9GAMM Unreviewed; 712 AA.
AC A0A2G8EGS5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:PIJ73723.1};
GN ORFNames=BK416_06350 {ECO:0000313|EMBL:PIJ73723.1};
OS Erwinia sp. OLSSP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1912096 {ECO:0000313|EMBL:PIJ73723.1, ECO:0000313|Proteomes:UP000229786};
RN [1] {ECO:0000313|EMBL:PIJ73723.1, ECO:0000313|Proteomes:UP000229786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLSSP12 {ECO:0000313|EMBL:PIJ73723.1,
RC ECO:0000313|Proteomes:UP000229786};
RX PubMed=29067021; DOI=10.3389/fmicb.2017.01969;
RA Chen X., Hitchings M.D., Mendoza J.E., Balanza V., Facey P.D., Dyson P.J.,
RA Bielza P., Del Sol R.;
RT "Comparative Genomics of Facultative Bacterial Symbionts Isolated from
RT European Orius Species Reveals an Ancestral Symbiotic Association.";
RL Front. Microbiol. 8:1969-1969(2017).
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:PIJ73723.1}.
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DR EMBL; MNCH01000013; PIJ73723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8EGS5; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000229786; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
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}; Reference proteome {ECO:0000313|Proteomes:UP000229786}.
FT DOMAIN 3..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 583..708
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 681
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 712 AA; 79358 MW; 9EFD4E5638F210DC CRC64;
MATQVIKRDG CKVAFDASRI EQAVRRAAQA AGVADSPLSQ TITASVCERL QTQHEVDISD
IQRAVEDALM ASAWPQVARC WIEYRHDRDL AREQRGRLNT AIRGLIEQSD AALLSENANK
DGKVIPTQRD LLAGIVAKHY ATRYLLPREV VEGHERGEIH YHDLDYAPFF PMFNCMLIDL
QGMLTRGFKM GNAEIEPPKS IATATAVTAQ IIAQVASHIY GGTTINRIDE VLAPYVRASQ
EKHRAIARQW QIADVEGYAD ARTRKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTD
EAARLIQQAI LENRLAGLGR NHKTAVFPKL VFALREGVNL RPQDANYDIK QLALRCASQR
MYPDILNFEQ VVKVTGSFKT PMGCRSFLGR YEENGEEIHE GRNNLGVISL NLPRIALEAA
GDESRFWSLL DERLTLARCA LMTRVARLEG VKARVAPILY MEGACGVRLQ ADDDIAPLFR
HGRASLSLGY IGLHETINAL YGTECHLFDS PARREKALAI VQHLRTATEK WKAETGYGFS
LYSTPSENLC DRFCRLDAAR FGLVAGVTDK GYYTNSYHLD VEKKVNPYDK LDFEAPYPAI
ASGGFICYGE YPNLQHNLKA LEDVWDYSYS RVPYYGTNTP IDECYACGYH GEFTCTSKGF
VCPGCGNHDP ASVSVTRRVC GYLGSPDARP FNAGKQEEVK RRVKHLPAGV AE
//
