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Database: UniProt
Entry: A0A0M0G0C4_9BACI
LinkDB: A0A0M0G0C4_9BACI
Original site: A0A0M0G0C4_9BACI 
ID   A0A0M0G0C4_9BACI        Unreviewed;       508 AA.
AC   A0A0M0G0C4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:KON83228.1};
GN   ORFNames=AF331_20630 {ECO:0000313|EMBL:KON83228.1};
OS   Rossellomorea marisflavi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=189381 {ECO:0000313|EMBL:KON83228.1, ECO:0000313|Proteomes:UP000037405};
RN   [1] {ECO:0000313|Proteomes:UP000037405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14235 jcm11544.";
RL   Submitted (JUL-2015) 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}.
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:KON83228.1}.
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DR   EMBL; LGUE01000008; KON83228.1; -; Genomic_DNA.
DR   RefSeq; WP_053429850.1; NZ_LGUE01000008.1.
DR   AlphaFoldDB; A0A0M0G0C4; -.
DR   STRING; 189381.GCA_900166615_00091; -.
DR   GeneID; 42294343; -.
DR   PATRIC; fig|189381.12.peg.3666; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000037405; 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   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000238-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037405}.
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   508 AA;  54678 MW;  685A9184F14660B4 CRC64;
     MLDANIKAQL EQYLQMLESD ILLKVSAGED KASHDMLSLV DQLATMSPRI KVENTELERT
     PSFSVNRIGE DTGITFAGVP LGHEFTSLVL ALLQVSGRAP KVDQTVIDQI KNVKGEYHFE
     SYISLTCHNC PDVVQALNIM SLLNDGISHT MIDGAAFKEE VESKEIMAVP TVFLNGEEFG
     SGRMTLEEML NKMGSGPDAA EFADKDPYDV LVVGGGPAGA SAAIYAARKG IRTGLVAERF
     GGQVMDTLGI ENFISMTKTE GPKLVASLEE HVKDYNIDVM NLQRAKGLEK KDLVELELEN
     GAVLKSKTVI LSTGARWRNV GVPGEAEFKN KGVAYCPHCD GPLFEGKDVA VIGGGNSGVE
     AAIDLAGIVK HVTVLEFMPE LKADAVLQER LNSLPNVTVV KNAQTKEITG TDKVNGITYI
     DRATEEEHHV ELAGVFVQIG LVPNTEWLGD SLEKTRMGEI VVDKHGATSM PGVFAAGDCT
     DSAYKQIIIS MGSGATASLG AFDYMIRN
//
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