ID A0A1C0YHI6_9BACL Unreviewed; 442 AA.
AC A0A1C0YHI6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:OCS86617.1};
GN ORFNames=A6M13_12960 {ECO:0000313|EMBL:OCS86617.1};
OS Caryophanon tenue.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Caryophanon.
OX NCBI_TaxID=33978 {ECO:0000313|EMBL:OCS86617.1, ECO:0000313|Proteomes:UP000093199};
RN [1] {ECO:0000313|EMBL:OCS86617.1, ECO:0000313|Proteomes:UP000093199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14152 {ECO:0000313|EMBL:OCS86617.1,
RC ECO:0000313|Proteomes:UP000093199};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Caryophanon tenue genome sequencing.";
RL Submitted (JUL-2016) 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:OCS86617.1}.
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DR EMBL; MASJ01000010; OCS86617.1; -; Genomic_DNA.
DR RefSeq; WP_066544640.1; NZ_MASJ01000010.1.
DR AlphaFoldDB; A0A1C0YHI6; -.
DR STRING; 33978.A6M13_12960; -.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000093199; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000093199}.
FT DOMAIN 1..304
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 327..427
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 442 AA; 48026 MW; 0CA338D854A31D92 CRC64;
MNIVIIGGDA AGMSAAMEIV RSPYEANITV LEKGGIYSYG QCGLPYVIDG SIAHTDELIA
RSVEAFREQG IDARTYHEVT AVDVQQQIVT GIHTTTNEPF TIHYDKLLIA SGASPTMPNW
ENRSLQGIHT VKTIPQMHAL LEDVVEAKHA TVIGAGYIAL EVAETLKKRG LAVRLIQRGK
QLMSTVDEQL AVHILEEAER QGIDVRLNTN TLGFIGDSRV EAVCTTAGEL ATDVVIVATG
VRPNTQFLEG TGIHLFDNGA VIVNGQMETN IANVYAAGDC ATHHLRNANR HTYIPLGTTA
NKQGRIAGRV MSGQQAVFKG IVGTSVLKFF DLTIGQTGAN HAAITELGTP VHVLRTTANN
HAGYYPHVEQ LHMCMWVHEK THELLGLQIV GGEGVDKRID VFATALVANM HIEDLLDLDL
SYAPPYNGVW DPLQQMARKY VK
//
