ID A0A0Q9KLT3_9MICO Unreviewed; 530 AA.
AC A0A0Q9KLT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=ASG74_15185 {ECO:0000313|EMBL:KRE40821.1};
OS Knoellia sp. Soil729.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE40821.1, ECO:0000313|Proteomes:UP000051965};
RN [1] {ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE40821.1, ECO:0000313|Proteomes:UP000051965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil729 {ECO:0000313|EMBL:KRE40821.1,
RC ECO:0000313|Proteomes:UP000051965};
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:KRE40821.1}.
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DR EMBL; LMSA01000005; KRE40821.1; -; Genomic_DNA.
DR RefSeq; WP_056145525.1; NZ_LMSA01000005.1.
DR AlphaFoldDB; A0A0Q9KLT3; -.
DR STRING; 1736394.ASG74_15185; -.
DR Proteomes; UP000051965; 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:SF105; DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 15..496
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 530 AA; 55339 MW; 1AE372EDFAB24D61 CRC64;
MTTADAVVVG AGPNGLVAAI ALADAGWDVT LVEANDTVGG AVASGEVTAP GFSSDLFSAF
YPLAAASPVI RDLDLAAHGL VWRRAPDVVS HALEDGPAAV MHADPDRTAA ELDAAAAGDG
AAWLDLCAGW QRVRDPLLDA LFTPFPPVVS GLRMARRLGL ADGLDFARLA VTPVRRLAKE
RFRGDGPGLL LTGNAMHSDV PPDAAGSGVF GWLLAMLGQD VGFPVPEGGA GQLAQALRSR
AESASVQVLT GARVTQVVVS GGRASGVRLA DGTLIKARHA VLADVTAPSL YEQLLSEHHL
PPRLLRDLGR FQWDNATIKV NWALDRPVPW ADSRLAGSGT VHLGVDLDGF VDMAADLSVG
RVPERPFLLF GQMATADPTR CPPGRETAWA YTHVPHGHDW SGSLLSEHVD RMQSAVERVA
PGFGDTVLAR HVQSPQDLQH ADANLVDGAL NAGTSALHQE LVFRPTPGLG RAETPVTGLY
LASASAHPGG GVHGACGWNA ARSALVAHGR TGVLHRAITR TAWARLLADH
//
