ID A0A3M0KE26_HIRRU Unreviewed; 570 AA.
AC A0A3M0KE26;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=DUI87_11617 {ECO:0000313|EMBL:RMC11498.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC11498.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC11498.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC11498.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC11498.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) 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:RMC11498.1}.
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DR EMBL; QRBI01000108; RMC11498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0KE26; -.
DR STRING; 333673.A0A3M0KE26; -.
DR Proteomes; UP000269221; 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 Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221}.
FT DOMAIN 291..414
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 570 AA; 61065 MW; BA5F5B7C4BA44560 CRC64;
MAAGLRGAPS LVRSSRWLQR WHPSLRPSGA RSAHAGAAAQ LQREYDAVVI GAGHNGLVAA
AYLQQAGLRT AVLEKRHVLG GAAVTEEIVP GFKFSRASYL LSLLRPQIYA DLELQGGSCS
GDIPVLQRHG LRVLPRDPFS FTPLLEDRSP PRSLLLGHDM AQTQQQIAQF SQKDAQAYPE
YEAFMGRMVL ALDPLLDAPP VDTAALGKGS LLQQLRNLRT LKPLLQAGLA LGRQLPRYYE
VLTAPISKVL DHWFESEPLK ATLATDAVIG AMASPHTPGS GYVLLHHVMG ELEGRQGAWG
YVAGGMGALS QAIAQAAAAR GAHIFAEKAV CHVLLGRDGE AQGVALQDGT EVRSKLVLSN
ASPQITFLEL IPQEQLPKDF VQRIQQIDTR SPVTKINVAV DRLPSFLAAP NARDGQPLPH
HQCSIHLNCE GTQLLHQAFT EATQGHPSSR PMIELCIPSA LDPGLAPPGC HVVSLFTQYT
PSVLAGGRSW DEQARNAYAD TVFDCIEDYA PGFKASVIGR DILTPPDLER IFGLPGGVGT
MHVNSEHGSG ARAGGHTALG QAQLAHTELC
//
