ID D4YNH2_9MICO Unreviewed; 476 AA.
AC D4YNH2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Flavoprotein disulfide reductase {ECO:0000313|EMBL:EFG47218.1};
DE EC=1.8.1.4 {ECO:0000313|EMBL:EFG47218.1};
GN Name=lpd3 {ECO:0000313|EMBL:EFG47218.1};
GN ORFNames=HMPREF0183_1482 {ECO:0000313|EMBL:EFG47218.1};
OS Brevibacterium mcbrellneri ATCC 49030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=585530 {ECO:0000313|EMBL:EFG47218.1, ECO:0000313|Proteomes:UP000005714};
RN [1] {ECO:0000313|EMBL:EFG47218.1, ECO:0000313|Proteomes:UP000005714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49030 {ECO:0000313|EMBL:EFG47218.1,
RC ECO:0000313|Proteomes:UP000005714};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:EFG47218.1}.
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DR EMBL; ADNU01000043; EFG47218.1; -; Genomic_DNA.
DR RefSeq; WP_005884484.1; NZ_ADNU01000043.1.
DR AlphaFoldDB; D4YNH2; -.
DR STRING; 585530.HMPREF0183_1482; -.
DR eggNOG; COG1249; Bacteria.
DR OrthoDB; 4678789at2; -.
DR Proteomes; UP000005714; Unassembled WGS sequence.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF1; NAD(P)H DEHYDROGENASE (QUINONE); 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000313|EMBL:EFG47218.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005714}.
FT DOMAIN 11..336
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 357..464
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 193..200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
SQ SEQUENCE 476 AA; 50262 MW; 3E73D76C5ECDED2D CRC64;
MKNVLDPSQN RVVIIGGGPG GYEAALVAAR SGADVMLIEK NRTGGSAVLT DVVPSKSLIA
TAEVMVEFTE SSQLGLRVGE GEADLDGQVW VDLEAMNRRI MKLANAQASD IHDSLVSEGV
KVITGAGRLT SASEVHVTET NGTEYELTAD TVLIAVGAHP RELQSAMPDG ERILSWTQLY
DLKELPEHLV VVGSGVTGAE FASAYNALGS EVTLVSSRDR VLPGQDEDAA EVIESAFRRR
GMNVLSRSRA DSVTRTEDGV EVVLADGRKV RASHCLMAVG SIPNTADLGL EAAGVHLEDS
GHIIVDGVSR TSVPGIYAAG DCTSVFPLAS VAAMQGRIAM WHALGDAVAP LKLRNVASNV
FTAPEIATVG FTQADLATAG HDVEWSMVSL ATNPRAKMQG NEEGFIKVFA RRGSGSVLGG
VVVGPKASEL ITPIALAVEN RLTVDQLSST FMVYPSVSGS LSEATRRLHH RREFRE
//
