ID   A0A0G1QY11_9BACT        Unreviewed;       765 AA.
AC   A0A0G1QY11;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:KKU49856.1};
GN   ORFNames=UX71_C0005G0069 {ECO:0000313|EMBL:KKU49856.1};
OS   Parcubacteria group bacterium GW2011_GWA1_47_10.
OC   Bacteria.
OX   NCBI_TaxID=1618791 {ECO:0000313|EMBL:KKU49856.1, ECO:0000313|Proteomes:UP000033978};
RN   [1] {ECO:0000313|EMBL:KKU49856.1, ECO:0000313|Proteomes:UP000033978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
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:KKU49856.1}.
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DR   EMBL; LCNF01000005; KKU49856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QY11; -.
DR   PATRIC; fig|1618791.3.peg.636; -.
DR   Proteomes; UP000033978; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.70.20; -; 2.
DR   Gene3D; 3.30.1620.10; b-12 dependent (class ii) ribonucleotide reductase, Chain A, Domain 2; 1.
DR   Gene3D; 3.90.1390.10; b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51161; ATP_CONE; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          14..109
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   765 AA;  86609 MW;  B4D1AB3FD9D9A200 CRC64;
     MKPKFATSKN ANLKTIIKRD GSKVPLNPKK ITNAVTRALQ ETKEYRPGVA EKITDAVVRK
     LALRKSYDKK YVPMVEGIQD LVEMELMLQK FTATAKAYIL YRAERTKSRE QNAMIPQEVK
     DKIAESSKYF KAPYQEFIFY QFYSKWRPEF GRRETWVEAI DRFMDYMKVK MGSMLTTGEY
     SEVREAILKQ DICPSMRLLW SAGKACDASN VCAYNCAYIA PVSWRDLSEI MYVSMCGAGC
     GFSVEPENVG KFPQIKKQTG HMAPKIVIED SKEGWCKAFV EACTAWEKGK DVELDYSLIR
     PAGAKLATMG GRASGPAPLQ ELMQFTKRKM LAKQGRRLTT LDLHDIICQI GLIVVAGGVR
     RSALISLSSL DDTDIRDAKK GTFWQTEGQR SMANNSAVYE AKPTAEEFMQ EWTSLVTSHS
     GERGIFNRGG LQFQVPKRRW EVLKKAKLPG VNPCGEIYLQ SKQFCNLTSI VVRPADDMEN
     LKKKMRLATL LGTYQATLTD FGYLSKEWKK NCEKEQLLGV SITGYYDNEL IRDDKNLQAL
     REESIKTNKK YAKRFGKNES TAITCVKPHG NSGQLLGVGS GMHTWYSHYY IRRVRISAND
     PLLKLARNQG VPVFPEVGYS TSNAATMVME FPCKAPEGAL VNKDVTALEM LEEWKRLKVN
     FTEHNPSVTI YIGDDEWISV ANFVYKNWDI VGGLSFLPRS NHVYQLAPYE EITKEEYERR
     VKELRHLDFS KLVVYEQEDN TVGARELACA GGVCEIDVVP AEAAA
//