ID F9VEY9_LACGL Unreviewed; 553 AA.
AC F9VEY9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=NADH oxidase {ECO:0000256|ARBA:ARBA00039201};
DE EC=1.6.3.4 {ECO:0000256|ARBA:ARBA00039092};
GN OrderedLocusNames=LCGL_1430 {ECO:0000313|EMBL:BAK60890.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60890.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK60890.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK60890.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036014};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; AP009333; BAK60890.1; -; Genomic_DNA.
DR RefSeq; WP_014025148.1; NC_017490.1.
DR AlphaFoldDB; F9VEY9; -.
DR STRING; 420890.LCGL_1430; -.
DR KEGG; lgv:LCGL_1430; -.
DR PATRIC; fig|420890.5.peg.1412; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR Proteomes; UP000008520; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Reference proteome {ECO:0000313|Proteomes:UP000008520}.
FT DOMAIN 465..553
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 553 AA; 60511 MW; 5635A5E18687630B CRC64;
MKIIIIGSVA SGTSVAAKAR RNTESAKITL YDKDTDISYA VCGIPYAIGG EIADFEELTP
RDAKWFKKRY NVDIHTSHEV LSINHSTKTV TVKNLLSGEV FEDNYDILVF ATGATYRTPD
VFSGKHFENV FQVRNINSGK EIKSFIENKK PMTAAVIGAG YIGLEVAEQL KERGIEVTIL
QRGKHPMSHL DWDMSIRIED EMIKQGIDFR PEETIQTLIG ETQLDEAITS KGTKLSADMY
ILATGVQPNV SLAQSIGVNI GETGAIATDN TLQTNIPGVY AVGDAAESFH VITGKPTYRP
LASTANKMGR IAGDAMTGGP LRFQGILGTG ILRFFDLTIA QTGLTEKEAL AEGYEVAVLF
NIKPDKPDYM HGKEMVIKAV ADKLTHRILG VQIIGSQGVD KRIDVFASTI TLGVTAEDLF
HMDLAYAPPF STTKDPVAYT GMALTNALTT APLITPHDLM ELQKNNENIT IIDTRATKSY
DKNHVPNAIN IPLAELREKA STLDKNKKTI VYCNKGVTGN ASQNVLRNEG FKEVYNLSGG
NKNYQELAKK QQN
//