ID A0A0N1NM09_9ACTN Unreviewed; 529 AA.
AC A0A0N1NM09;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=OK074_1154 {ECO:0000313|EMBL:KPI20325.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI20325.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI20325.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI20325.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC mitochondrial function. {ECO:0000256|ARBA:ARBA00037217}.
CC -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC {ECO:0000256|ARBA:ARBA00038825}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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:KPI20325.1}.
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DR EMBL; LJCV01000044; KPI20325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NM09; -.
DR PATRIC; fig|1592327.3.peg.1129; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR PANTHER; PTHR10668:SF103; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 26..308
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 529 AA; 56457 MW; DDED4749E9D63C6E CRC64;
MPAHEGHQSP VSGRYDTVIV GGGHNGLVAA AYLARAGRSV LVLERLGTTG GAAVSTRPFA
GVDARLSRYS YLVSLLPAKI VRDLGLDFRV RARTVSSYTP CERAGRPTGL LVGGGERRTR
EAFERLTGSP REYEAWQRFY GMTGRLARQV FPTLTEPLPT REALRRRIDD EDAWRTLFEE
PVGAAIEERF ADDLVRGVVL TDALIGTFAD AHDPSLAQNR CFLYHVIGGG TGAWDVPVGG
MGALTDALAE AARTAGAVLA TGHEAIRIES DGRSAEVAYR TADGEGVAAA RHVLVNASPQ
ELARLTGETP PTPAEGAQLK VNMLLTRLPR LRDTAVDPRE AFAGTFHIAE GYGQLAAAHA
QAASGALPEA PPSEIYCHSL TDPSILGPEL ADSGHHTLTL FGLHTPARLF ERDNDAVREE
LLKSTLAQLD AHLAEPLADC LATDADGRPC IEAKTPLDLE RDLRLPGGNI FHRELAWPYA
QEGTGRWGVE TRQPNVLLCG AGAVRGGGVS GVPGHNAAMA VLEEDLSPR
//