ID A0A066UP75_9GAMM Unreviewed; 376 AA.
AC A0A066UP75;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
GN Name=nrdB {ECO:0000313|EMBL:KDN26018.1};
GN ORFNames=MBO_02475 {ECO:0000313|EMBL:KDN26018.1};
OS Moraxella bovoculi 237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN26018.1, ECO:0000313|Proteomes:UP000035860};
RN [1] {ECO:0000313|EMBL:KDN26018.1, ECO:0000313|Proteomes:UP000035860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=237 {ECO:0000313|EMBL:KDN26018.1,
RC ECO:0000313|Proteomes:UP000035860};
RX PubMed=24970830;
RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA Reilly T.J.;
RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL Genome Announc. 2:e00612-14(2014).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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:KDN26018.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOMT01000005; KDN26018.1; -; Genomic_DNA.
DR RefSeq; WP_036363233.1; NZ_AOMT01000005.1.
DR AlphaFoldDB; A0A066UP75; -.
DR eggNOG; COG0208; Bacteria.
DR OrthoDB; 9765051at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000035860; Unassembled WGS sequence.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:KDN26018.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035860}.
SQ SEQUENCE 376 AA; 43478 MW; E7D9834595553E5C CRC64;
MHYSIFCQTK NDVLKEPMFF GQPVNVSRYD QQKHPIFEQL IEKQLSFFWR PEEIDVSRDR
IDFAELSVHE QHIFLSNLKY QTLLDSIQGR SPNVVLLPLV SIPELETWIE TWSFSETIHS
RSYTHIIRNV VNDPSKIFDD IIENEHILER ASDIARYYDD LHRAAQLYDL HGEGTYTVCD
ETVEVSLKDL KKKLYLCIVA VNVLEAIRFY VSFACSFAFA ERKVMEGNAK IIKMIARDEA
LHLNGTQHMI NLMRSGRDDP EMLEIAKSCE DEAIDIFRSA AEQEKAWAEY LFKDGSMIGL
NKDILCQYVE FITNTRMAAI GLPAIFETKS NPIPWINAWL SSDNVQVAPQ ETEITTYLVG
QIDSDLDDVD LDDFEL
//
