ID R9JQJ6_9FIRM Unreviewed; 596 AA.
AC R9JQJ6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C808_04112 {ECO:0000313|EMBL:EOS36231.1};
OS Lachnospiraceae bacterium M18-1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS36231.1, ECO:0000313|Proteomes:UP000014090};
RN [1] {ECO:0000313|EMBL:EOS36231.1, ECO:0000313|Proteomes:UP000014090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18-1 {ECO:0000313|EMBL:EOS36231.1,
RC ECO:0000313|Proteomes:UP000014090};
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 Lachnospiraceae bacterium M18-1.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates electron transfer from NADH to oxygen, reducing it
CC to water. This modular protein has 3 redox cofactors, in other
CC organisms the same activity requires 2 or 3 proteins.
CC {ECO:0000256|ARBA:ARBA00025633}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|ARBA:ARBA00001965};
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavodoxin
CC reductase family. {ECO:0000256|ARBA:ARBA00006098}.
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:EOS36231.1}.
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DR EMBL; ASSV01000037; EOS36231.1; -; Genomic_DNA.
DR AlphaFoldDB; R9JQJ6; -.
DR STRING; 1235792.C808_04112; -.
DR PATRIC; fig|1235792.3.peg.4448; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1773; Bacteria.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_456880_0_0_9; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000014090; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:UniProt.
DR GO; GO:0016646; F:oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR CDD; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR CDD; cd00350; rubredoxin_like; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR026816; Flavodoxin_dom.
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; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR048574; RUBY_RBDX.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR PANTHER; PTHR32145:SF20; FLAVOPROTEIN-RELATED; 1.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR Pfam; PF12724; Flavodoxin_5; 1.
DR Pfam; PF19583; ODP; 1.
DR Pfam; PF21349; RUBY_RBDX; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Reference proteome {ECO:0000313|Proteomes:UP000014090};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 243..383
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 559..595
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 596 AA; 66828 MW; 66FAA21C7EF6CCCF CRC64;
MDITNDIRYV GVNDHEVDLF EGQYVVENGM AYNSYVILDE KTAVMDTVDA HFTHEWLDNV
GAVLGSRKPD YLIIQHMEPD HSANIANFMQ VYKDTKIVSS AKAFVMMKQF FGTDYEDRQI
VVKEGDTLSL GKHELSFVAA PMVHWPEVIV TYDSYDKVLF SADGFGKFGA LDVEEDWACE
ARRYYIGIVG KYGAQVQNLL KKASGLDIQT ICPLHGPVLK ENLGYYLGLY QTWSSYSAET
EGIMIAYTSI YGNTKKAVDA LAAKLTAKGC PKVVVTDLAR EDMAEAVEDA FRYSKLVLAT
TTYNAGIFPF MRQFIDHLTE RNFQNRIVGL IENGSWAPLA AKTMKNMLEG CKKLTFTKTT
VQIKSALNDE SNAQLEALAE ELCRDYLAQH DETADKNDLT ALFKIGYGLY VVTSNDGKKD
NGLIVNTVSQ VTNTPNRVAV TINKDNYSHH VIKQTGIMNL NCLSTDAPFK VFETFGFQSG
RTADKFADME PLRSDNGLAF LPRYINSFMS LKVEQYVDLD THGMFICTIT EARVISNVDT
MTYTYYQNHV KPKPQTEGKK GFVCVVCGYI YEGDELPEDF VCPLCKHGAA DFEPIE
//
