ID R9LPV6_9FIRM Unreviewed; 404 AA.
AC R9LPV6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=C815_01051 {ECO:0000313|EMBL:EOS60799.1};
OS Firmicutes bacterium M10-2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS60799.1, ECO:0000313|Proteomes:UP000014154};
RN [1] {ECO:0000313|EMBL:EOS60799.1, ECO:0000313|Proteomes:UP000014154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M10-2 {ECO:0000313|EMBL:EOS60799.1,
RC ECO:0000313|Proteomes:UP000014154};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Firmicutes bacterium M10-2.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOS60799.1}.
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DR EMBL; ASTB01000023; EOS60799.1; -; Genomic_DNA.
DR AlphaFoldDB; R9LPV6; -.
DR STRING; 1235796.C815_01051; -.
DR PATRIC; fig|1235796.3.peg.1049; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_1_0_9; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000014154; 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:UP000014154}.
FT DOMAIN 258..403
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 404 AA; 46154 MW; 4C01F17F80CF4FB9 CRC64;
MHIVREVTEG LYWIGANDHR LTLFENIHPI PEGVSYNSYI ALGEKTILFD TVDWDACRQM
LENLKYVLDG RDLDYIVINH WEPDHAASLQ EVLIEYPNAK IIGNLKGFQL AEQFGFHIDE
EKKIIVNEGD VIDAGNHQLT FLFMPMVHWP EAMVTFDLSN GALFTADAFG SFKALDGKLF
NDEVDYDRDW LDENRRYLTN IVGKYGPHIR KILKKAAPLL DQVKFICPLH GLVWRNNFSY
LLEKYELWAN YEPEQKGVMI CYASMYGNTE QAAQALAAKL CDLGVPNVSV FDVSNTHVSY
LIAEVFKKSH VVLASCTYNL GIFPVMKNFL EDMKALNVQN RTFAIIENGS WAIRSGDLIS
QFLDEQMKTI TVLNDRVTIA SHLKEGQNEE IEDLALEIKE SMRG
//
