ID A0A0Q8VYG4_9ACTN Unreviewed; 524 AA.
AC A0A0Q8VYG4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=ASE19_01780 {ECO:0000313|EMBL:KRC59773.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC59773.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC59773.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC59773.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC59773.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC59773.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRC59773.1}.
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DR EMBL; LMIP01000001; KRC59773.1; -; Genomic_DNA.
DR RefSeq; WP_056896566.1; NZ_LMIP01000001.1.
DR AlphaFoldDB; A0A0Q8VYG4; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000051414; 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 Pfam; PF12831; FAD_oxidored; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051414}.
FT DOMAIN 183..333
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 524 AA; 55681 MW; DD26C4DEBCA95B80 CRC64;
MAESFDFVVI GGGHNGLSAA CTLGAAGASV LVVEQQPVLG GLSTSHAYLP EAPDHVLSLG
AMDDMFMSCT SIVDDLRLRR HGFETITVPA PYGWIGPDGE TLLLFADLDR TLAEVRRFSP
YDARAYADLQ PALSWIFRAL VTVMSRHPAE LPKRELGRHL LRLAPDRTTR RRLGQIMSSN
LVELMAETFR SDAMRSLGTY WGSMIGPIDA DGGGFYCVGL AAVHSRPGVQ RPRGGMRSIV
GALEGRARSL GVEVRSGCGV EQVLVDGGEV RGVRLTDGTV VDARRGVLAA VPPQTAYGPL
LEPGVLDYSV TAKVAMLPAS GNNSATFKVD LAVGGPVTFP VAQGQRDRLD GHDLRTVSLM
TGTFADQIEQ LRLIRQGRSL AAPPSYLAVL SGLDPTVAPP GQDVVYLASN VPAQPREDWP
DIRDRYADGV LATARTHLSG LDAEIGRVVT SPADFGEQYA TPNGSYFHVD MTPLRLAMNR
PAPGLGGYRS PVAGYFHAGA GSHPGGGVSG WPGRLAARTA LAER
//
