ID A0A2I0K664_PUNGR Unreviewed; 562 AA.
AC A0A2I0K664;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=CRG98_015948 {ECO:0000313|EMBL:PKI63660.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:PKI63660.1, ECO:0000313|Proteomes:UP000233551};
RN [1] {ECO:0000313|EMBL:PKI63660.1, ECO:0000313|Proteomes:UP000233551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AG2017 {ECO:0000313|Proteomes:UP000233551};
RC TISSUE=Leaf {ECO:0000313|EMBL:PKI63660.1};
RA Akparov Z., Amiraslanov A., Hajiyeva S., Abbasov M., Kaur K., Hamwieh A.,
RA Solovyev V., Salamov A., Braich B., Kosarev P., Mahmoud A., Hajiyev E.,
RA Babayeva S., Izzatullayeva V., Mammadov A., Mammadov A., Sharifova S.,
RA Ojaghi J., Eynullazada K., Bayramov B., Abdulazimova A., Shahmuradov I.;
RT "De-novo sequencing of pomegranate (Punica granatum L.) genome.";
RL Submitted (NOV-2017) 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 -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046}.
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:PKI63660.1}.
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DR EMBL; PGOL01000878; PKI63660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0K664; -.
DR STRING; 22663.A0A2I0K664; -.
DR Proteomes; UP000233551; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233551}.
FT DOMAIN 29..368
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 562 AA; 61509 MW; 30D0F2B917CAB277 CRC64;
MWRRSFSTGT AALKDKKYDA LVIGGGHNGL TTAAYLARGG LSVAVLERRH VIGGAAVTEE
LIPGFKFSRC SYLQSLLRPA VIKELELARH GLKLLKRSPS SFTPCLDGRY LLLGPDRELN
HAEISKFSKR DAEAYPRYEH QLENFCKFMD PLLDSQTPEA RRGATSFTER FKDKLQKSVF
WAHCLRRAQS LGQKDMVDFM DLLLSPASKV LNNWFETDVL KATLATDAVI GTTASVHTPG
SGYVLLHHVM GETDGDRGIW SYVEGGMGSV SLAIGNAAKE AGANIITGAE VHKLLVEEDG
RVEGVLLNDG TRVQSSVVLS NATPYRTFVE LVPDSVLPDD FLRAIKHADY SSGTTKINLA
VDRLPQFESC KLNHPDAGPQ HRGTIHIGSE RMEEIHSACQ DAVNGVPSRR PIIEMTIPSV
LDKTISPPGK HVVNLFIQYT PYDPSDGSWK DPAYRESFAQ RCFSLIDEYA PGFSSSVIGY
DMLTPPDLER EIGLTGGNIF HGAMGLDSLF LMRPVKGWSD YRTPVRGLYL CGSGAHPGGG
VMGAPGRNAA HVVLQDIKQS LK
//
