ID N1ZK91_9CLOT Unreviewed; 841 AA.
AC N1ZK91;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Anaerobic nitric oxide reductase flavorubredoxin {ECO:0000313|EMBL:USF30101.1};
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:NDO46230.1};
GN Name=norV {ECO:0000313|EMBL:USF30101.1};
GN ORFNames=C820_001542 {ECO:0000313|EMBL:USF30101.1}, C820_01024
GN {ECO:0000313|EMBL:EMZ14438.1}, FMM67_05085
GN {ECO:0000313|EMBL:NDO46230.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ14438.1};
RN [1] {ECO:0000313|EMBL:EMZ14438.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ14438.1};
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).
RN [2] {ECO:0000313|EMBL:NDO46230.1, ECO:0000313|Proteomes:UP000462571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|Proteomes:UP000462571}, and MD294
RC {ECO:0000313|EMBL:NDO46230.1};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF30101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF30101.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQFQ01000011; EMZ14438.1; -; Genomic_DNA.
DR EMBL; VIRC01000011; NDO46230.1; -; Genomic_DNA.
DR EMBL; CP097810; USF30101.1; -; Genomic_DNA.
DR RefSeq; WP_004035105.1; NZ_VIRC01000011.1.
DR AlphaFoldDB; N1ZK91; -.
DR STRING; 97138.C820_01024; -.
DR PATRIC; fig|97138.3.peg.1042; -.
DR eggNOG; COG0426; Bacteria.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_017490_2_0_9; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000012445; Chromosome.
DR Proteomes; UP000462571; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN 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 CDD; cd00350; rubredoxin_like; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
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; IPR041575; Rubredoxin_C.
DR PANTHER; PTHR32145; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR PANTHER; PTHR32145:SF11; DIFLAVIN FLAVOPROTEIN A 2-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF19583; ODP; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000012445}.
FT DOMAIN 255..393
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 841 AA; 93071 MW; F82114763A87AA2C CRC64;
MKAYQLKQDL YWAGVLDKDL RVFDIIMETE FGTTYNSYVL KGSEKTALFE TAKVKFFDEY
LEKLQEVVDV NDIDYVVMNH TEPDHAGSIV KLVEMNPRIC VVATACAIGF LKNIINHDFY
SIAVKENDTL SLGNKTLQFM LLPNLHWPDT MYTYVKEDKL LFTCDSFGSH YCLDDIVLSK
LKDNEGYMRA TKYYFDNIIG PFKPFMLKAL DRIKELDIDM ICTGHGPVID SRIDEIQQTY
KDWCTVVNPN TKKTVVIPYV SAYGYTGQLA EEIKKGIQDS GDIDVRIYDM VVSDQAKVLG
ELGFADGILF GTPTIVGEAL KPIWDLTTSI FAGTHGGKLA SAFGSYGWSG EGVPHIIERL
KQLRMKVVDG YRIKLRPGEN DLTGAYEYGY NFGCILLNKE NDKLKSAKKS LVKCLVCGEI
FPEGMDTCPV CGVGKENFVS VELNESDYQK DTEEKFVVIG NGVAGLNAAK EIRNRNKTAS
ITMITNEPYI SYNRPMLTKT LLAGVTAKQL VVEDQQWYEQ NNIEVMLNEE VKSLDSNKKE
ITLASGAVLS YDKCIYALGA ECFVPPIKGA DKKEVVTIRR MEDVDKVRKL VKTAKNAVVI
GGGVLGLEAA WEIKKANCHV TVVEMMPSLM SRQLDSEASD MILKAAQSQG IVMKLGASVE
SIEGESSVTG VRLGDGEIVA ADVVILSSGV RANVAIAKQA GAQINKAIVV NEKMETSLKD
VYACGDCAEY DNINFALWSE AAEMGKVAGA NAAGEETSYK TIVAPLAFHG MDTSLYAVGD
NGKNANRKYK TVVFKDDTKH TFEKYYFANN RLVGVTLIGD TSKMAKVTQA LEKPALFNEM
F
//
