ID A0KYG1_SHESA Unreviewed; 705 AA.
AC A0KYG1;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Ribonucleoside-triphosphate reductase class III catalytic subunit / ribonucleoside-triphosphate reductase {ECO:0000313|EMBL:ABK48830.1};
DE EC=1.17.4.2 {ECO:0000313|EMBL:ABK48830.1};
GN OrderedLocusNames=Shewana3_2603 {ECO:0000313|EMBL:ABK48830.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK48830.1, ECO:0000313|Proteomes:UP000002589};
RN [1] {ECO:0000313|Proteomes:UP000002589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000469; ABK48830.1; -; Genomic_DNA.
DR RefSeq; WP_011717502.1; NC_008577.1.
DR AlphaFoldDB; A0KYG1; -.
DR STRING; 94122.Shewana3_2603; -.
DR KEGG; shn:Shewana3_2603; -.
DR eggNOG; COG1328; Bacteria.
DR HOGENOM; CLU_002707_2_0_6; -.
DR OrthoDB; 9804622at2; -.
DR Proteomes; UP000002589; Chromosome.
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:ABK48830.1}.
FT DOMAIN 2..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 582..705
FT /note="Glycine radical"
FT /evidence="ECO:0000259|PROSITE:PS51149"
FT MOD_RES 680
FT /note="Glycine radical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 705 AA; 78741 MW; 2DF882103C3EFD45 CRC64;
MPVVIKRDGC RTPFDETRIR DAVIAAANSV GIEDADYAAT VAACVRERVA NLAEVEIHHL
QDAVENLLME GPYKSLARVY IEYRHDRDIC RDATSKLNLE IRGLVEQSNA ALLNENANKD
SKVIPTQRDL LAGIVAKHYA KSHILPKDVV AAHELGEIHY HDLDYSPFFP MFNCMLIDLA
GMLTHGFKMG NAEIETPKSI STATAVTAQI IAQVASHIYG GTTINRIDEV LAPFVAKSYD
KHYQVALNWQ IKDAKAYATA LTEKECHDAF QSLEYEVNTL HTANGQTPFV TFGFGLGTSW
ESRLIQQSML KVRMTGLGKN RKTAVFPKLV FAIRDGINHK AGDCNYDVKQ MALKCASMRM
YPDILNYEQV EKVTGSFKTP MGCRSFLGSY KENGELVHEG RNNLGVVSLN LPRVALEANG
NEAEFYRILD ERLLLARRAL DTRIERLNGV KARVAPILYM EGACGVRLRA DDDIAQIFKN
GRASISLGYI GLHETINALY GTETHVFDDA KLREKAVAIV AHLKAATDAW KAETGYGFSL
YSTPSESLCS RFCKLDARQF GVVAGVTDKG YYTNSFHLDV EKRVNPYDKI DFEQPYPAIA
NGGFICYGEY PNMQHNIEAL ENVWDYSYSR VPYYGTNTPI DECYDCGFTG EFSCTSKGFT
CPKCGNHEPS RVSVTRRVCG YLGSPDARPF NHGKQEEVKR RIKHL
//