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Database: UniProt
Entry: A0A377Z7D2_KLEPO
LinkDB: A0A377Z7D2_KLEPO
Original site: A0A377Z7D2_KLEPO 
ID   A0A377Z7D2_KLEPO        Unreviewed;       439 AA.
AC   A0A377Z7D2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Ribonucleotide reductase of class Ib (Aerobic) subunit alpha {ECO:0000313|EMBL:STU62752.1};
DE            EC=1.17.4.1 {ECO:0000313|EMBL:STU62752.1};
GN   Name=nrdE_1 {ECO:0000313|EMBL:STU62752.1};
GN   ORFNames=NCTC5050_01000 {ECO:0000313|EMBL:STU62752.1};
OS   Klebsiella pneumoniae subsp. ozaenae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=574 {ECO:0000313|EMBL:STU62752.1, ECO:0000313|Proteomes:UP000255382};
RN   [1] {ECO:0000313|EMBL:STU62752.1, ECO:0000313|Proteomes:UP000255382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC5050 {ECO:0000313|EMBL:STU62752.1,
RC   ECO:0000313|Proteomes:UP000255382};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406}.
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DR   EMBL; UGLZ01000004; STU62752.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A377Z7D2; -.
DR   Proteomes; UP000255382; Unassembled WGS sequence.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
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; PF02867; Ribonuc_red_lgC; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:STU62752.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000255382}.
FT   DOMAIN          291..313
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   439 AA;  49387 MW;  DCB2C28B77E4D4FA CRC64;
     MPMRKSASKT LSLGVVIPDI TFQLAKEDAQ MALFSPYDVE RLYGKPFADC AIGDLYPQLV
     ADERVRKRWI RARDLFQRLA EIQFESGYPY IMFEDTVNRA SPVAGRVTMS NLCSEILQVS
     TPSAYNEDLS YAHIGEDISC NLGSLNIAHT MDSPDFGRTI ATAVRALTAV SDMSDIQSVP
     SVAAGNAASH AIGLGQMNLH GYLAREGIAY GSPEGLDFTN IYFYTVTWHA LHTSMQLARE
     RGQRFAGFEQ SRYASGAYFD KYLQEEWQPK TERVRTLFAR AGISLPDRES WRQLRDDVMR
     YGIYNRYLQA VPPTGSISYI NHATSSIHPI VSKIEIRKEG KTGRVYYPAP FMNNDNLALY
     QDAYEIGPEK IIDTYAEATR HVDQGLSLTL FFPDTATTRD INKAQIYAWK KGIKTLYYIR
     LRQLALEGTE IEGCVSCAL
//
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