ID A0A177HX57_9ACTN Unreviewed; 458 AA.
AC A0A177HX57;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=NADH peroxidase {ECO:0000313|EMBL:OAH15481.1};
DE EC=1.11.1.1 {ECO:0000313|EMBL:OAH15481.1};
GN Name=npr {ECO:0000313|EMBL:OAH15481.1};
GN ORFNames=STSP_11680 {ECO:0000313|EMBL:OAH15481.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH15481.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH15481.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:OAH15481.1}.
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DR EMBL; LOHS01000042; OAH15481.1; -; Genomic_DNA.
DR RefSeq; WP_067272905.1; NZ_LOHS01000042.1.
DR AlphaFoldDB; A0A177HX57; -.
DR STRING; 1716141.STSP_11680; -.
DR PATRIC; fig|1716141.3.peg.1235; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016692; F:NADH peroxidase activity; IEA:UniProtKB-EC.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:OAH15481.1};
KW Peroxidase {ECO:0000313|EMBL:OAH15481.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 4..310
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 458 AA; 48432 MW; BEEC5624CC99A240 CRC64;
MRERLVIIGG DAAGMSAASQ ARRLKGPDEL EIIAFERGHF TSYSACGIPY WVSGDVPERH
RLIARTPEEH RARAIDLRMR TEVTEIDVAA GRVRARDLES GAEEWTAYDN LVIATGARPD
RPPLPGMDAP GVHGVQTLDD GQALLDTLER AEGRRAVVVG AGYIGVEMAE AMMKRGYEVT
VVNRGQEPMA TLDPDMGRLV HEAMTGLGIT MVGDAEVTKV LTDAEGRARA VATDDAEFPA
DVVVLGMGVR PETALARAAG LPLGEYGGLL TDLAMRVRGH DGIWAGGDCV EVLDLVSGRE
RHIALGTHAN KHGQVIGTNV GGGYATFPGV VGTAVSKVCD LEIARTGLRE KDARAVGLQY
VTVTVESTSR AGYYPGAAPM TVKMLAERRT GRLLGVQIVG REGAAKRVDV AAVALTAGMT
VEQMTALDLG YAPPFSPVWD PVLIAARKAS VAVRAGGA
//
