ID A0A0M3T5I6_9MICC Unreviewed; 403 AA.
AC A0A0M3T5I6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ALE07915.1};
GN ORFNames=AL755_16535 {ECO:0000313|EMBL:ALE07915.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE07915.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE07915.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE07915.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP012479; ALE07915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3T5I6; -.
DR STRING; 1704044.AL755_16535; -.
DR KEGG; are:AL755_16535; -.
DR PATRIC; fig|1704044.3.peg.2637; -.
DR OrthoDB; 1145at2; -.
DR Proteomes; UP000060433; Chromosome.
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:UP000060433}.
FT DOMAIN 2..299
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 318..402
FT /note="Reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14759"
SQ SEQUENCE 403 AA; 41930 MW; 0DC6169FD5F78182 CRC64;
MVIIGGGLAG ATAADTLRAE GYTGPVTIVA EEPEIPYQRP PLSKGFLAGK EGDDALLPYP
ASWYPEHDVT VRTGTAATAI DPAAHAVSLS DGSVLPYAKL LIATGALPRV IPFPGVELDG
VHYFRSKADA VAMKELLSAG GHNLVMIGSG WIGMEIAATA RELGNNVTLL GLEDVPLSVA
IGKELGAVFA ARHEEAGVRF VLPASAAEIK GDAGRVTGVV TTTGVTLPAD LVIVAVGVVP
NIALAKEAGL AIDNGIQVSG SLQSSDPDIF AAGDVANSLH PVTGAYARSE HWANAIAAGK
VAARSMLGRD AVLDDIPYFY TDQFDLGMEY SGYGALTRDA ELVVRGSLEK REFIAFWVLE
GRVVAGMNVN IWDVQDAIKE LIGSGRTVDT QALADPQIPL EAI
//
