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Database: UniProt
Entry: N2B604_9FIRM
LinkDB: N2B604_9FIRM
Original site: N2B604_9FIRM 
ID   N2B604_9FIRM            Unreviewed;       405 AA.
AC   N2B604;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN   ORFNames=C823_00933 {ECO:0000313|EMBL:EMZ35861.1};
OS   Eubacterium plexicaudatum ASF492.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235802 {ECO:0000313|EMBL:EMZ35861.1, ECO:0000313|Proteomes:UP000012589};
RN   [1] {ECO:0000313|EMBL:EMZ35861.1, ECO:0000313|Proteomes:UP000012589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF492 {ECO:0000313|EMBL:EMZ35861.1,
RC   ECO:0000313|Proteomes:UP000012589};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT   community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-e00214(2014).
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}.
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:EMZ35861.1}.
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DR   EMBL; AQFT01000024; EMZ35861.1; -; Genomic_DNA.
DR   RefSeq; WP_004053830.1; NZ_AQFT02000001.1.
DR   AlphaFoldDB; N2B604; -.
DR   STRING; 1235802.C823_00933; -.
DR   GeneID; 78432265; -.
DR   PATRIC; fig|1235802.3.peg.1003; -.
DR   eggNOG; COG0426; Bacteria.
DR   HOGENOM; CLU_017490_1_0_9; -.
DR   OrthoDB; 9807946at2; -.
DR   Proteomes; UP000012589; Unassembled WGS sequence.
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; 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; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000012589}.
FT   DOMAIN          258..405
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   405 AA;  46183 MW;  805F7AF431220FFB CRC64;
     MYCVRNITED LYWVGANDHR LHLFENIHPI PYGVSYNAYL LLDKETVLFD TVDWSACRQL
     LENLDYLLDG RPLDWLVVNH MEPDHGACVE QILLRYPHVK VISTEKAFML MRQFHFHPDD
     HECVTVAEGD THCFGKHTVT FVAAPMVHWP EAMVTFDTTN GVLFSADAFG SFIALDGKLF
     ADEVDFDRDW LDEARRYLVN IVGKYGPHIQ LLLKKAGGIV DQIKYICPLH GPVWRENFGY
     FIEKYDKWSR YEPEEKGVMI AYASMYGNTE AAAQALACKL CEKGCTNVKV HDVSNTHVSY
     LISDAFKYSH IVLASVTYNL GIYPVMHNFL MDMKALNMQN RTFALIENGS WACKSGDLMQ
     KFIDVELKNM TVLNERLSIA SSMGADKTIE LDSLANAIID SMKES
//
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