ID A0A0Q2LMA5_MYCGO Unreviewed; 399 AA.
AC A0A0Q2LMA5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KQH77113.1};
GN ORFNames=AO501_20400 {ECO:0000313|EMBL:KQH77113.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH77113.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH77113.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH77113.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KQH77113.1}.
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DR EMBL; LKTM01000338; KQH77113.1; -; Genomic_DNA.
DR RefSeq; WP_029644203.1; NZ_LKTM01000338.1.
DR AlphaFoldDB; A0A0Q2LMA5; -.
DR STRING; 1778.A9W97_13100; -.
DR OrthoDB; 4213189at2; -.
DR Proteomes; UP000051677; 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; 3.30.390.30; -; 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; IPR028202; Reductase_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF14759; Reductase_C; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051677}.
FT DOMAIN 6..300
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..394
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 399 AA; 42545 MW; 321E7616751C06BF CRC64;
MTPERAVIVG ASHAGAQLAA NLRREGWSGE VVLIGDEGGL PYHRPPLSKG YLAGKNGLDD
LLIRGADFYE KQHIRLLNAT VEAIHRSAKR VSLSTGDTLT YTKLALCTGA RARRLPTPGV
DLPGIHYLRT AADVELIRAA ATPGRRVVIV GGGYIGLETA ASLCSLGMNV TVLEATERVL
ERVTAPEVSA FYTRIHNGEG VEIRTHALVE AFFGNGGVQE VVLADGEPIP ADLVIVGVGV
VPNTELASAA GLSVDNGIVI DDQARTSDPD IVAAGDCTSH TMARYGSRIR LESVSSAGEQ
AKIAAATICG KHSAIAALPW FWSDQYDLKL QIAGLNAGYD EVLLSGDPSR ERDFSCFYFR
EGELIAADCV NRPRDFMSSK RAISQQLRVD RSELLAGSI
//
