NRDI_BACSU
ID NRDI_BACSU Reviewed; 130 AA.
AC P50618;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein NrdI;
GN Name=nrdI; Synonyms=ymaA; OrderedLocusNames=BSU17370;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND OPERON.
RC STRAIN=168;
RX PubMed=8969495; DOI=10.1099/13500872-142-11-2995;
RA Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.;
RT "The Bacillus subtilis genes for ribonucleotide reductase are similar to
RT the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae.";
RL Microbiology 142:2995-3004(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Probably involved in ribonucleotide reductase function.
CC -!- INDUCTION: Part of the probable nrdI(ymaA)-nrdE-nrdF-ymaB operon.
CC Expression is constitutive but low, dramatically induced by thymidine
CC starvation which requires recA. {ECO:0000269|PubMed:8969495}.
CC -!- SIMILARITY: Belongs to the NrdI family. {ECO:0000305}.
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DR EMBL; Z68500; CAA92809.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13621.1; -; Genomic_DNA.
DR PIR; C69883; C69883.
DR RefSeq; NP_389619.1; NC_000964.3.
DR RefSeq; WP_003231758.1; NZ_JNCM01000035.1.
DR PDB; 1RLJ; X-ray; 2.00 A; A=1-130.
DR PDBsum; 1RLJ; -.
DR AlphaFoldDB; P50618; -.
DR SMR; P50618; -.
DR STRING; 224308.BSU17370; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; P50618; -.
DR DNASU; 940075; -.
DR EnsemblBacteria; CAB13621; CAB13621; BSU_17370.
DR GeneID; 940075; -.
DR KEGG; bsu:BSU17370; -.
DR PATRIC; fig|224308.179.peg.1883; -.
DR eggNOG; COG1780; Bacteria.
DR InParanoid; P50618; -.
DR OMA; GLADFWK; -.
DR PhylomeDB; P50618; -.
DR BioCyc; BSUB:BSU17370-MON; -.
DR EvolutionaryTrace; P50618; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR Gene3D; 3.40.50.360; -; 1.
DR HAMAP; MF_00128; NrdI; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR020852; RNR_Ib_NrdI_bac.
DR InterPro; IPR004465; RNR_NrdI.
DR PANTHER; PTHR37297; PTHR37297; 1.
DR Pfam; PF07972; Flavodoxin_NdrI; 1.
DR PIRSF; PIRSF005087; NrdI; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR00333; nrdI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..130
FT /note="Protein NrdI"
FT /id="PRO_0000164305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1RLJ"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:1RLJ"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1RLJ"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 52..61
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1RLJ"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1RLJ"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1RLJ"
FT HELIX 105..122
FT /evidence="ECO:0007829|PDB:1RLJ"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1RLJ"
SQ SEQUENCE 130 AA; 14603 MW; EF76AAB3842CDFF3 CRC64;
MVQIIFDSKT GNVQRFVNKT GFQQIRKVDE MDHVDTPFVL VTYTTNFGQV PASTQSFLEK
YAHLLLGVAA SGNKVWGDNF AKSADTISRQ YQVPILHKFE LSGTSKDVEL FTQEVERVVT
KSSAKMDPVK
