ID B2TLE9_CLOBB Unreviewed; 410 AA.
AC B2TLE9; U4PGM5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Flavodoxin {ECO:0000313|EMBL:ACD24125.1};
GN OrderedLocusNames=CLL_A2042 {ECO:0000313|EMBL:ACD24125.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24125.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD24125.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TLE9; -.
DR KEGG; cbk:CLL_A2042; -.
DR PATRIC; fig|935198.13.peg.1997; -.
DR HOGENOM; CLU_017490_0_0_9; -.
DR Proteomes; UP000001195; Chromosome.
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; PTHR43717; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR PANTHER; PTHR43717:SF1; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 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;
FT DOMAIN 251..406
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 410 AA; 47132 MW; 3BE9B5B323FFBD07 CRC64;
MEKNIMLNEN IFWVGKVDDR DVPFHRLTLT KGTTYNSYLL MTEKPTVIDT VDISFGREFV
ENLKNVIELD KIKYIVINHT EPDHSGSLRS LATKATNAVI VCTKPAVNEL KEMYKLHDRE
FLVVGDGDTL DIGGKTLKFI ETPYLHTEET MVTYCEEDKI LFPCDIFSTH VANYEYFNDM
AKKDIKDDFI GYYKLIMHPH RRYVQNMIEK IRNLDIRMIA PSHGFIIRDD IKSFIDIYDN
MSKNTDLDKK ALILYSTMTG STKKIATILN EKFEEQNITS EVMDVNKIPM EEVMKSINEA
DVIFFGSSTR YGDMIGNMED ILKNLKSLNL ESKLGAAFGS YGWSGEAIEV VQDYLNETNL
KVLNTSHVIK STGMIDIELP LRIRFSPKED ILKNIERLVT YVSDLLLSTI
//
