ID A0A380BSP9_SPOPA Unreviewed; 509 AA.
AC A0A380BSP9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:SUJ06423.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:SUJ06423.1};
GN Name=ahpF {ECO:0000313|EMBL:SUJ06423.1};
GN ORFNames=NCTC4822_01735 {ECO:0000313|EMBL:SUJ06423.1};
OS Sporosarcina pasteurii (Bacillus pasteurii).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1474 {ECO:0000313|EMBL:SUJ06423.1, ECO:0000313|Proteomes:UP000254519};
RN [1] {ECO:0000313|EMBL:SUJ06423.1, ECO:0000313|Proteomes:UP000254519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11859 / DSM 33 / NCIB 8841 / NCTC 4822
RC {ECO:0000313|Proteomes:UP000254519};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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DR EMBL; UGYZ01000002; SUJ06423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380BSP9; -.
DR Proteomes; UP000254519; Unassembled WGS sequence.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR CDD; cd03026; AhpF_NTD_C; 1.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR044141; AhpF_NTD_C.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03140; AhpF; 1.
DR PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000238-2}; FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000238-1};
KW NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SUJ06423.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000254519}.
FT DOMAIN 123..192
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 208..493
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 209..224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 348..362
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 468..478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 336..339
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 509 AA; 54603 MW; EDFF5A53242E0948 CRC64;
MLDKDIKAQL AQYLEMMEGD VLLKISAGTD KVSNEMIALV EELASMSSHI KVEKAELERT
PSFSVNRVGE ETGVTFAGIP LGHEFTSLVL ALLQVSGRAP RVDEKVIEQV KNLEGEYHFE
SYISLSCQNC PEVVQALNVM SVLNPNITHT MIDGAVFKEE VESKNVMAVP TVFLNGESFS
SGRQSIEEIL AKLGSGPDAS EFENKEPFDV LVVGGGPAGA SAAIYAARKG VRTGIVADRF
GGQILDTATI ENFISVNRTE GPKLAASLEE HVKDYEIEVM NLQTATGLEK KDLFEIELEN
GAVLKSKSVI LSTGASWRNV GVPGEAEFRN KGVAYCPHCD GPLFEGKDIA VIGGGNSGIE
AAIDLAGIVN HVTVLEFASE LKADSVLQDR LYKLPNVTVV KNAQTKEITG TDSVNGITYI
DRDTNEEHHI ELAGVFVQIG LVPNTNWLGN AVERNNFGEI IVDKRGATNV PGVFGAGDCT
DSAYKQIIIS MGSGATAALS AYDYLGKTE
//
