ID U2NNY6_9CLOT Unreviewed; 630 AA.
AC U2NNY6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=NADH-flavin oxidoreductase, Old yellow enzyme family protein {ECO:0000313|EMBL:ERK30536.1};
GN ORFNames=CINTURNW_2224 {ECO:0000313|EMBL:ERK30536.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK30536.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK30536.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK30536.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000256|ARBA:ARBA00011048}.
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:ERK30536.1}.
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DR EMBL; APJA01000012; ERK30536.1; -; Genomic_DNA.
DR RefSeq; WP_021802222.1; NZ_KI273145.1.
DR AlphaFoldDB; U2NNY6; -.
DR STRING; 1294142.CINTURNW_2224; -.
DR PATRIC; fig|1294142.3.peg.2288; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_1_9; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000016721; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023014};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000016721}.
FT DOMAIN 7..106
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 119..320
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 367..593
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 630 AA; 69067 MW; C475F663771A6A3B CRC64;
MNKKSNIFKP IQIGNVISKN RIEVSPAGAF LCGRDGGNTP EYLAYVKSLA KSGAGIVTLG
VSSIDEQSSG VPITNVGNSL YIADLMDLAE VIHRYDALAS IELVSGQYMI MPPEVVATKS
SKEEIKHLIE LYANAAERCM IAGFDMIMIH GGHGNVPAMF FSRKHNHRTD EYGGSFENRC
RFGEELLSAI REKVGNRIAI EYRISGEELL EGYSELEETL AYAKKIQDKV DIMHVSRGLL
EEESLLPYLF QPTYFPRAMN LEAAKRFKKE LNIPVSVVGS FDLETAEEVV SNGDVDIVAM
MRNILADTDC VTNAYKGKSD ETRPCVRCNT CINRTHTQFV RLRCAVNPLI GRETQFPELR
EEVHSKNIVI IGGGPAGLEA ARVSAKRGYN VTIFEKNSEL GGALRMASIA PFKKDMQRYL
DWSIRSVMKN PKIKVKLNTF ATVDNVMAEK PDAVLVGVGA KPIIPKFTLS GTEKVAWVGD
VELKKVPVGQ DVVMVGAGFT GLEAALTLAQ EGKNVKVIDM IPEDKIGADG IQISMIALKE
LLKEAGITFE CEVKLSDVTE EGAIVEDKDG NKKVIKCDTV ILSLGVRADK AQVDMFKDAL
YEVYPIGDCA TKGGTLWNAT KTAFNVAMEI
//
