ID F9F3V3_FUSOF Unreviewed; 533 AA.
AC F9F3V3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN ORFNames=FOXB_01078 {ECO:0000313|EMBL:EGU88411.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU88411.1};
RN [1] {ECO:0000313|EMBL:EGU88411.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88411.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU88411.1}.
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DR EMBL; AFQF01000428; EGU88411.1; -; Genomic_DNA.
DR AlphaFoldDB; F9F3V3; -.
DR STRING; 660025.F9F3V3; -.
DR PaxDb; 5507-FOXG_15187P0; -.
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;
FT DOMAIN 30..510
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 533 AA; 57732 MW; 04F5CE77653E6ED7 CRC64;
MVYNYAKLGH LSSSKDPQHD IIVVGSGHNG LIAAAYLAKA GKKVLVLEKA SYPGGGVASL
TMAEEGFTSE RHSAIHQMIL ANPLVTKDEL ELQSKYGLRY LPLEPAYAII FEDGVLPLYH
DVKRTVDTIT DFSNEAEGQA YLKFATLATK FVELSMPSMF VPPTTPVDLS AHPDIAQAVE
FAAKNSSLEV VEQYFKNPTV QVAILRFVTE VQLANPKTPG TGVMAYMAIG LLHKYGLAVP
QGGGSAFTAA VIRAIEAHGG EVRLNTEVIK IVTENGRAIG VRTRAGEIRA RKAVVAQIHP
HILDRLVDGL DPEVTIPAKE TRLSEYTLFV VHAAMESPLR FRAGGVANKV VMNTICPGSV
ESLLKSYEEI DQGKIPEDLI IGASIITNAD QTRAPPGKSL LHAVVMVRAD NAEVGFHGWD
AIKDEVTYKV FRYLSKYVED LTPDQIRGYH AVTPLDHEHD TSSFQRGDIC GLSMAFDQMG
GSRPTLALAQ YRVPGVNGLY LAGPFMHPGG GVWGGGRPVA IRVLEDLGIK FKL
//
