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Database: UniProt
Entry: E0RVU6_BUTPB
LinkDB: E0RVU6_BUTPB
Original site: E0RVU6_BUTPB 
ID   E0RVU6_BUTPB            Unreviewed;       398 AA.
AC   E0RVU6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Flavodoxin/beta-lactamase domain-containing protein {ECO:0000313|EMBL:ADL35628.1};
GN   OrderedLocusNames=bpr_I2898 {ECO:0000313|EMBL:ADL35628.1};
OS   Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS   (Clostridium proteoclasticum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL35628.1, ECO:0000313|Proteomes:UP000001299};
RN   [1] {ECO:0000313|EMBL:ADL35628.1, ECO:0000313|Proteomes:UP000001299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51982 / DSM 14932 / B316
RC   {ECO:0000313|Proteomes:UP000001299};
RX   PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA   Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA   Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT   "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT   highlights adaptation to a polysaccharide-rich environment.";
RL   PLoS ONE 5:E11942-E11942(2010).
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC       hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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DR   EMBL; CP001810; ADL35628.1; -; Genomic_DNA.
DR   RefSeq; WP_013282280.1; NC_014387.1.
DR   AlphaFoldDB; E0RVU6; -.
DR   STRING; 515622.bpr_I2898; -.
DR   KEGG; bpb:bpr_I2898; -.
DR   eggNOG; COG0426; Bacteria.
DR   HOGENOM; CLU_017490_1_0_9; -.
DR   Proteomes; UP000001299; Chromosome 1.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR   CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR045761; ODP_dom.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR   PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR   PANTHER; PTHR32145:SF20; FLAVOPROTEIN-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF19583; ODP; 1.
DR   PIRSF; PIRSF005243; ROO; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001299}.
FT   DOMAIN          256..396
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   398 AA;  44424 MW;  B16432391E6275B8 CRC64;
     MNGVKKVTDG IFWIGGSDRR LERFENIFPI PEGVSYNSYF IDDDKTAVFD TADITISDQY
     LENLKDCLDG RKLDYLVVLH MEPDHCSLIS TVTGLFPEVT VVGNAKTFQI MEQFFPEAAG
     FNKLEVKEGD SLSTGNHNFK FVTAPMVHWP EVLFAYDDTS KALLCADAFG TFGALDGGLF
     ADEYDFEKVF LNSARRYYAN IVGKYGMQVQ AVLKKAQGLD IQMLLPLHGP VWRKDIAWFI
     DKYQKWSTYE PETEDIVVIY GSLYGHTASA AEAVAASIRN KTKAGVKVYD VSGTDVSYLI
     GEVWRCKNIV IMCPTYNNGI YPPMESFIAD MAALGVQNRS FALAQNGTWA PVTVKLMTEK
     LQTLKNVTIL EESLTIKSAL HKKDTDSLEA FTDAIVKA
//
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