ID R8VWX9_9CLOT Unreviewed; 372 AA.
AC R8VWX9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=HMPREF1526_01941 {ECO:0000313|EMBL:EOQ37250.1};
OS Butyricicoccus pullicaecorum 1.2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Butyricicoccus.
OX NCBI_TaxID=1203606 {ECO:0000313|EMBL:EOQ37250.1, ECO:0000313|Proteomes:UP000013981};
RN [1] {ECO:0000313|EMBL:EOQ37250.1, ECO:0000313|Proteomes:UP000013981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1.2 {ECO:0000313|EMBL:EOQ37250.1,
RC ECO:0000313|Proteomes:UP000013981};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Van Immerseel F., Eeckhaut V.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Butyricicoccus pullicaecorum 1.2.";
RL Submitted (JAN-2013) 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}.
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:EOQ37250.1}.
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DR EMBL; AQOB01000006; EOQ37250.1; -; Genomic_DNA.
DR RefSeq; WP_016148075.1; NZ_KB976104.1.
DR AlphaFoldDB; R8VWX9; -.
DR PATRIC; fig|1203606.4.peg.1896; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_0_0_9; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000013981; 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; 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; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000013981}.
FT DOMAIN 251..372
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 372 AA; 41525 MW; 3EFE5640182B66A6 CRC64;
MSAIKIRDNI YAVGARDPEV RIFHGYATPF GATYNCYLIL DGDKKILVDN VKAAFTEEFF
RNIEEICPVE SLDILIQNHI EPDHSGSFPA LLERCPNLEV YCTAGAQKGL KAYYGWEGAC
HVVKMGETLN TGSYTFHFIP APMVHWPDSM LTYLAEEKIL FSNDAFGQHI CPPVNYDDEL
GEERLMERAV DYYGNIVLPF GMQVTNLLKA ASALDIELVC PSHGVMLRTY IGKMVESYAK
WAKNETDPNK VVMVYDSMWG STAEMTRKIC AEFEAEGKQV HVHCLADEHY SAVMGDIVEA
KTICIGASTL NNTMMPTVAA FLTYLKGLKP KNRVGLAYGS YGWSGEATKE VAAVMEGMGW
EVLPIRKQLY RG
//
