ID A0A1A2MNB0_9MYCO Unreviewed; 400 AA.
AC A0A1A2MNB0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OBH04468.1};
GN ORFNames=A5695_00895 {ECO:0000313|EMBL:OBH04468.1};
OS Mycobacterium sp. E1747.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834128 {ECO:0000313|EMBL:OBH04468.1, ECO:0000313|Proteomes:UP000092218};
RN [1] {ECO:0000313|Proteomes:UP000092218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1747 {ECO:0000313|Proteomes:UP000092218};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-2016) 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:OBH04468.1}.
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DR EMBL; LZJI01000221; OBH04468.1; -; Genomic_DNA.
DR RefSeq; WP_068088101.1; NZ_LZJI01000221.1.
DR AlphaFoldDB; A0A1A2MNB0; -.
DR STRING; 1834128.A5695_00895; -.
DR OrthoDB; 4213189at2; -.
DR Proteomes; UP000092218; 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;
FT DOMAIN 4..304
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 326..396
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 400 AA; 42201 MW; 94CEC05FD16D6B3F CRC64;
MLKNVVVVGA GVAGTRAAET LRQEGYDGAL TIVGAERHAP YHRPPLSKKL LTGKVHRAGV
DLAPQFDMDA RVLRGASALN LDMPSRTVHV RDDGQELSLP FDGLVIASGA VPRQWPGGPV
PDGVLLLRTV EDCLAIRDRL ASRPRVVVVG GGFIGAEVAA SCRSIGLDVV LIEKADSPLL
SALGKELASR WADLHRQHGV DLRVGVGVDG FVGNGRVEGV RLTDGSRVPA DLVIVGLGVS
PATDWLDGSG LRVDDGVVCD ACGVAEGSTA DAPVVAAGDV ARWWHPLYER HLRTEHWDDA
GRQGAAAARA LLAGPQGAEP DGGVPYFWSD QYAIKLQMLG VPRDYDSVEI VEGDPGSWEF
VAAYGRGGHT IAALGTIPGR VYAYREAVEK RAEFPPSPPG
//
